Feeds:
Posts
Comments

Archive for the ‘Chemical Biology and its relations to Metabolic Disease’ Category

Acidosis vs Alkalosis: Perspectives from Cardiology and from Pulmonology

Authors: Justin D Pearlman, MD, PhD, FACC and Larry H Bernstein, MD, FCAP

Acidosis vs Alkalosis: Perspectives from Cardiology

Justin D Pearlman, MD, PhD, FACC

Your concern about alkylosis is justified. The concentration of free protons H+ is indeed not generally given the strict and prompt attention it deserves, to prevent  harm from too little H+ (alkylosis) as well as to much (acidosis).

Your concern about deleterious impact on vasomotor control of microcirculation is valid. In addition, precise control of acidity is vital not only for proper auto regulation, but also protein conformation and enzyme activities throughout the body.

The use of the term pH by physicians can be considered pedantic. It shows doctors can share discussions with chemists, who deal with H+ values that shift many orders of magntude, but it belies the fact that the body does not tolerate such ranges. Rather, life requires H+ to stay well within the range 10 – 90 and it strongly prefers the range of 35-45, both for bio control such as metarterioles and precapillary sphincters, and for protein conformations and enzyme functions. Clinically, H+ should be maintained near 40 mEq/L, and I attribute my high success rate with code blue situations to paying close attention to that fact.

SOURCE

From: Justin MDMEPhD <jdpmdphd@gmail.com>

Date: Saturday, September 19, 2015 at 4:43 PM

To: “Dr. Larry Bernstein” <larry.bernstein@gmail.com>

Cc: Aviva Lev-Ari <AvivaLev-Ari@alum.berkeley.edu>

Acidosis vs Alkalosis: Perspectives from Pulmonology

Larry H Bernstein, MD, FCAP

As the state of alkalosis develops, there is a disequilibrium across the cell membrane with excess OH- uncompensated by a positive ion.  This leaves a disequilibrium across the cell membrane that can only be balanced by the movement of Na+ from within the cell.  If the OH- was taken up by the RBC, it would have to produce water through carbonic anhydrase, which would disrupt the mechanism for release of CO2.  In the case of the kidney, I don’t see a mechanism for compensation across the cell membrane. There is a reciprocal loss of H+ and K+. The H+ has to be retained to balance the OH-, and the end result would be a net loss of K+.  A continued loss of K+ would lead to cardiac arrest. 

All cells in the body are seriously hurt by alkalosis.  In medical intensive care there is a preoccupation with metabolic acidosis, the result being that the retained H+ has to be captured in H2CO3 in the RBC and in the kidney, and CO2 is exhaled in the alveoli. There is also the reciprocal loss of K+, which is interchangeable with H+ in the kidney.  The kidney does not handle acidosis well, and the most efficient mechanism is respiratory via conversion of H2CO3 to H2O and CO2.

The sphincters opening in response to acidotic blood. This supplies oxygen, etc to the capillary bed*

I am not familiar with the precapillary sphincters, but can see merit to this statement.  The sphincter would control the volume of blood entering the capillary, and it would determine the volume of blood entering the venuous circulation.  The gas exchange is at the capillary level.  

Acidosis is itself problematic, and it is associated with a low flow state and with acute renal failure.

ALL mechanical respirators are preset to retain alkalosis*   I am not aware of this.

Complete renal shutdown with complete recovery is only possible if he is not on life support systems, which are currently used everywhere.*

I think that the goal of respiratory support should be to maintain efficient gas exchange, to eliminate H+ ion formed from peripheral vasoconstriction, and a corellary should be to maintain a neutral pH.  While there is a mechanism for eliminating H+ ion, I think that it is the case that excess OH- is more difficult.  The kidney has no mechanism I can think of for balancing a metabolic acidosis.  

The large volume of fluid used in resuscitation is only to maintain volume of plasma.  

In not so recent history, the ICU was not serviced by the main laboratory, but pulmonary had its own blood gas measurements. This became unfeasible, and especially when the demands of open heart surgery needed support that pulmonary could not provide.   I still remember the situation in 1982, when the laboratory, and not pulmonary were entrusted with servicing the cardiovascular program.  Measurement of blood gases includes the measurement of pH.  

SOURCE

From: “Dr. Larry Bernstein” <larry.bernstein@gmail.com>

Date: Saturday, September 19, 2015 at 3:18 PM

To: Aviva Lev-Ari <aviva.lev-ari@comcast.net>

Cc: Justin MDMEPhD <jdpmdphd@gmail.com>

Read Full Post »

Insights in Biological and Synthetic Medicinal Chemistry

Larry H. Bernstein, M.D., FCAP, Curator

Leaders in Pharmaceutical Intelligence

Series E. 2;  10

Selected Articles Linking the Biological and Synthetic Worlds

The worlds of biological and synthetic chemistry both offer incredible diversity. Biology provides complex architectures including proteins, nucleic acids, and polysaccharides. Synthetic chemistry, on the other hand, provides a tool for atom-by-atom control over molecular structure that can be used to obtain molecules and materials inaccessible through biology.

In this ACS Select Virtual Issue, we highlight some of the recent advances in bioconjugation chemistry. These publications describe new strategies for functionalization of biomacromolecules, as well as the use of synthetic molecules as building blocks for assembly using biological machinery. The resultant conjugate systems have new and exciting properties, as demonstrated in new therapeutic and imaging applications.

– Vincent Rotello, Editor-in-Chief, Bioconjugate Chemistry
– C. Dale Poulter, Editor-in-Chief, The Journal of Organic Chemistry
– Amos Smith, III, Editor-in-Chief, Organic Letters

10.1  Bioconjugate Chemistry

10.1.1 Production of Site-Specific Antibody-Drug Conjugates Using Optimized Non-Natural Amino Acids in a Cell-Free Expression System
Zimmerman, E. S.; Heibeck, T. H.; Gill, A.; Li, X. F.; Murray, C. J.; Madlansacay, M. R.; Tran, C.; Uter, N. T.; Yin, G.; Rivers, P. J.; Yam, A. Y.; Wang, W. D.; Steiner, A. R.; Bajad, S. U.; Penta, K.; Yang, W. J.; Hallam, T. J.; Thanos, C. D.; Sato, A. K.
Bioconjugate Chem.201425 (2), pp 351-361
DOI: 10.1021/bc400490z

10.1.2 General Chemoselective and Redox-Responsive Ligation and Release Strategy
Park, S.; Westcott, N. P.; Luo, W.; Dutta, D.; Yousaf, M. N.
Bioconjugate Chem.201425 (3), pp 543-551
DOI: 10.1021/bc400565y

10.1.3 Chemoenzymatic Fc Glycosylation via Engineered Aldehyde Tags
Smith, E. L.; Giddens, J. P.; Iavarone, A. T.; Godula, K.; Wang, L. X.; Bertozzi, C. R.
Bioconjugate Chem.201425 (4), pp 788-795
DOI: 10.1021/bc500061s

10.1.4 Triazine-Based Tool Box for Developing Peptidic PET Imaging Probes: Syntheses, Microfluidic Radio labeling, and Structure-Activity Evaluation
Li, H. R.; Zhou, H. Y.; Krieger, S.; Parry, J. J.; Whittenberg, J. J.; Desai, A. V.; Rogers, B. E.; Kenis, P. J. A.; Reichert, D. E.
Bioconjugate Chem.201425 (4), pp 761-772
DOI: 10.1021/bc500034n

10.1.5 Developments in the Field of Bioorthogonal Bond Forming Reactions-Past and Present Trends
King, M.; Wagner, A.
Bioconjugate Chem.201425 (5), pp 825-839
DOI: 10.1021/bc500028d

10.1.6 Diels-Alder Cycloadditions on Synthetic RNA in Mammalian Cells
Pyka, A. M.; Domnick, C.; Braun, F.; Kath-Schorr, S.
Bioconjugate Chem.201425 (8), pp 1438-1443
DOI: 10.1021/bc500302y

10.1.7 High-Density Functionalization and Cross-Linking of DNA: “Click” and “Bis-Click” Cycloadditions Performed on Alkynylated Oligonucleotides with Fluorogenic Anthracene Azides
Pujari, S. S.; Ingale, S. A.; Seela, F.
Bioconjugate Chem.201425 (10), pp 1855-1870
DOI: 10.1021/bc5003532

10.1.8 Surface Functionalization of Exosomes Using Click Chemistry
Smyth, T.; Petrova, K.; Payton, N. M.; Persaud, I.; Redzic, J. S.; Gruner, M. W.; Smith-Jones, P.; Anchordoquy, T. J.
Bioconjugate Chem.201425 (10), pp 1777-1784
DOI: 10.1021/bc500291r

10.1.9 Site-Specific Antibody-Drug Conjugates: The Nexus of Biciorthogonal Chemistry, Protein Engineering, and Drug Development.
Agarwal, P.; Bertozzi, C. R.
Bioconjugate Chem.201526 (2), pp 176-192
DOI: 10.1021/bc5004982

10.1.10 Strain-Promoted Oxidation-Controlled Cyclooctyne-1,2-Quinone Cycloaddition (SPOCQ) for Fast and Activatable Protein Conjugation
Borrmann, A.; Fatunsin, O.; Dommerholt, J.; Jonker, A. M.; Lowik, D.; van Hest, J. C. M.; van Delft, F. L.
Bioconjugate Chem.201526 (2), pp 257-261
DOI: 10.1021/bc500534d

10.2 The Journal of Organic Chemistry

10.2.1 Sequential “Click” – “Photo-Click” Cross-Linker for Catalyst-Free Ligation of Azide-Tagged Substrates
Arumugam, S.; Popik, V. V.
J. Org. Chem.201479 (6), pp 2702-2708
DOI: 10.1021/jo500143v

10.2.3 Diazirine-Containing RNA Photo-Cross-Linking Probes for Capturing microRNA Targets
Nakamoto, K.; Ueno, Y.
J. Org. Chem.201479 (6), pp 2463-2472
DOI: 10.1021/jo402738t

10.2.4 Interstrand Cross-Link and Bioconjugate Formation in RNA from a Modified Nucleotide
Sloane, J. L.; Greenberg, M. M.
J. Org. Chem.201479 (20), pp 9792-9798
DOI: 10.1021/jo501982r

10.2.5 Synthesis of Base-Modified 2 ‘-Deoxyribonucleoside Triphosphates and Their Use in Enzymatic Synthesis of Modified DNA for Applications in Bioanalysis and Chemical Biology
Hocek, M.
J. Org. Chem.201479 (21), pp 9914-9921
DOI: 10.1021/jo5020799

10.2.6 Site-specific PEGylation of Proteins: Recent Developments
Nischan, N.; Hackenberger, C. P. R.
J. Org. Chem.201479 (22), pp 10727-10733
DOI: 10.1021/jo502136n

10.3 Organic Letters

10.3.1 One-Pot Peptide Ligation-Desulfurization at Glutamate
Cergol, K. M.; Thompson, R. E.; Malins, L. R.; Turner, P.; Payne, R. J.
Org. Lett.201416 (1), pp 290-293
DOI: 10.1021/ol403288n

10.3.2 Semisynthesis of Peptoid-Protein Hybrids by Chemical Ligation at Serine
Levine, P. M.; Craven, T. W.; Bonneau, R.; Kirshenbaum, K
Org. Lett.201416 (2), pp 512-515
DOI: 10.1021/ol4033978

10.3.3 A Photoinduced, Benzyne Click Reaction
Gann, A. W.; Amoroso, J. W.; Einck, V. J.; Rice, W. P.; Chambers, J. J.; Schnarr, N. A.
Org. Lett.201416 (7), pp 2003-2005
DOI: 10.1021/ol500389t

10.3.4 Amine-Selective Bioconjugation Using Arene Diazonium Salts
Diethelm, S.; Schafroth, M. A.; Carreira, E. M.
Org. Lett.201416 (15), pp 3908-3911
DOI: 10.1021/ol5016509

10.3 5 Efficient and Facile Synthesis of Acrylamide Libraries for Protein-Guided Tethering
Allen, C. E.; Curran, P. R.; Brearley, A. S.; Boissel, V.; Sviridenko, L.; Press, N. J.; Stonehouse, J. P.; Armstrong, A.
Org. Lett.201517 (3), pp 458-460
DOI: 10.1021/ol503486t

10.4 Synthesis, Design and Molecular Function

This Special Issue on “Synthesis, Design and Molecular Function”, guest-edited by Paul Wender, is intended to explore the many exciting new advances and challenges associated with designing and making molecules in the 21st century. It features contributions from thought leaders in the field directed at new reactions, reagents and catalysts, process technologies and screening strategies.

See guest editorial by Paul Wender

10.4.1 Art, Architecture, and the Molecular Frontier
Paul A. Wender (Guest Editor)
DOI10.1021/acs.accounts.5b00332

10.4.2 From Synthesis to Function via Iterative Assembly of N-Methyliminodiacetic Acid Boronate Building Blocks
Junqi Li, Anthony S. Grillo, and Martin D. Burke *
DOI10.1021/acs.accounts.5b00128

10.4.3 Trimethylenemethane Diyl Mediated Tandem Cycloaddition Reactions: Mechanism Based Design of Synthetic Strategies
Hee-Yoon Lee *
DOI10.1021/acs.accounts.5b00178

10.4.4 Intermolecular Reaction Screening as a Tool for Reaction Evaluation
Karl D. Collins* and Frank Glorius*
DOI10.1021/ar500434f

10.4.5 Development of Globo-H Cancer Vaccine
Samuel J. Danishefsky*, Youe-Kong Shue, Michael N. Chang, and Chi-Huey Wong*
DOI10.1021/ar5004187

10.4.6 Total Synthesis of Vinblastine, Related Natural Products, and Key Analogues and Development of Inspired Methodology Suitable for the Systematic Study of Their Structure–Function Properties
Justin E. Sears and Dale L. Boger*
DOI10.1021/ar500400w

10.4.7 Reaction Design, Discovery, and Development as a Foundation to Function-Oriented Synthesis
Glenn C. Micalizio* and Sarah B. Hale
DOI10.1021/ar500408e

10.4.8 Copy, Edit, and Paste: Natural Product Approaches to Biomaterials and Neuroengineering
Karl Gademann*
DOI10.1021/ar500435b

10.4.9 Catalytic Enantioselective Construction of Quaternary Stereocenters: Assembly of Key Building Blocks for the Synthesis of Biologically Active Molecules
Yiyang Liu, Seo-Jung Han, Wen-Bo Liu, and Brian M. Stoltz*
DOI10.1021/ar5004658

10.4.10 Focused Library with a Core Structure Extracted from Natural Products and Modified: Application to Phosphatase Inhibitors and Several Biochemical Findings
Go Hirai* and Mikiko Sodeoka*
DOI10.1021/acs.accounts.5b00048

10.5 Ionization Methods in Mass Spectrometry

Mass spectrometry has undoubtedly boomed over the last two decades and has become a major analytical tool in many disciplines. The technique relies on the separation of ions of different m/z, and its success hinges on efficient ionization methods that furthermore should be tailored to the task at hand. Depending on the application, ionization should be soft, hard, selective, as efficient as possible, etc. This virtual issue pulls together publications from Analytical Chemistry that showcase the exemplary developments in ionization techniques.

10.5.1 From the editorial by Renato Zenobi
DOI 10.1021/acs.analchem.5b01062

10.5.2 Nanophotonic Ionization for Ultratrace and Single-Cell Analysis by Mass Spectrometry
Bennett N. Walker, Jessica A. Stolee, and Akos Vertes
DOI: 10.1021/ac301238k

10.5.3 Unraveling the Mechanism of Electrospray Ionization
Lars Konermann, Elias Ahadi, Antony D. Rodriguez, and Siavash Vahidi
DOI: 10.1021/ac302789c

10.5.4 Ambient Surface Mass Spectrometry Using Plasma-Assisted Desorption Ionization: Effects and Optimization of Analytical Parameters for Signal Intensities of Molecules and Polymers
T. L. Salter, I. S. Gilmore, A. Bowfield, O. T. Olabanji, and J. W. Bradley
DOI: 10.1021/ac302677m

10.5.5 Fast Surface Acoustic Wave-Matrix-Assisted Laser Desorption Ionization Mass Spectrometry of Cell Response from Islets of Langerhans
Loreta Bllaci, Sven Kjellström, Lena Eliasson, James R. Friend, Leslie Y. Yeo, and Staffan Nilsson
DOI: 10.1021/ac3019125

10.5.6 Electrospun Nanofibers as Substrates for Surface-Assisted Laser Desorption/Ionization and Matrix-Enhanced Surface-Assisted Laser Desorption/Ionization Mass Spectrometry
Tian Lu and Susan V. Olesik
DOI: 10.1021/ac303292e

10.5.7 Capillary Photoionization: A High Sensitivity Ionization Method for Mass Spectrometry
Markus Haapala, Tina Suominen, and Risto Kostiainen
DOI: 10.1021/ac4002673

10.5.8 High-Speed Tandem Mass Spectrometric in Situ Imaging by Nanospray Desorption Electrospray Ionization Mass Spectrometry
Ingela Lanekoff, Kristin Burnum-Johnson, Mathew Thomas, Joshua Short, James P. Carson, Jeeyeon Cha, Sudhansu K. Dey, Pengxiang Yang, Maria C. Prieto Conaway, and Julia Laskin
DOI: 10.1021/ac401760s

10.5.9 Atomic Force Microscope Controlled Topographical Imaging and Proximal Probe Thermal Desorption/Ionization Mass Spectrometry Imaging
Olga S. Ovchinnikova, Kevin Kjoller, Gregory B. Hurst, Dale A. Pelletier, and Gary J. Van Berkel
DOI: 10.1021/ac4026576

10.5.10 Droplet Electrospray Ionization Mass Spectrometry for High Throughput Screening for Enzyme Inhibitors
Shuwen Sun and Robert T. Kennedy
DOI: 10.1021/ac502542z

Read Full Post »

Eppendorf Award for Young European Investigators

Curator: Larry H. Bernstein, MD, FCAP

Article ID #184: Eppendorf Award for Young European Investigators. Published on 9/18/2015

WordCloud Image Produced by Adam Tubman

Series E. 2; 8.11

The independent Eppendorf Award Jury chaired by Prof. Reinhard Jahn selected Dr. Thomas Wollert (Research Group Leader at the Max Planck Institute of Biochemistry in Martinsried, Germany) as the 2015 winner of the Eppendorf Award for Young European Investigators.

Thomas receives the €20,000 prize for his groundbreaking work in reconstituting complex intracellular membrane events in the test tube using artificial membranes and purified components. His experiments have paved the way for understanding key steps in autophagy, a fundamental process required for the clearance of damaged cell parts in all eukaryotic cells.

Listen to a podcast with Thomas Wollert and learn more about his work, and read excerpts from the interview in a Q&A feature article.

Presented in partnership with Nature The Eppendorf Award for Young European Investigators was established in 1995 to recognize outstanding work in biomedical science. It also provides the opportunity for European researchers to showcase their work and communicate their research to a scientific audience. Nature is pleased to partner with Eppendorf to promote the award and celebrate the winner’s work in print and online. Nature’s Julie Gould talks to the 2015 winner Thomas Wollert (Max Planck Institute of Biochemistry, Germany) about his work — which looks at the complex molecular process that cells use to remove their waste — and how it felt to win the award.
To listen to the full interview, visit: go.nature.com/cszfl1

About the Award Thomas Wollert is the twentieth recipient of the Eppendorf Award for Young European Investigators, which recognizes talented young individuals working in the field of biomedical research in Europe. The Eppendorf Award is presented in partnership with Nature. The winner is selected by an independent jury of scientists under the chairmanship of Reinhard Jahn, Director at the Max Planck Institute for Biophysical Chemistry in Göttingen, Germany. Nature and Eppendorf do not influence the selection. For more information see: eppendorf.com/award

http://www.nature.com/nature/awards/eppendorf/eppendorf_award_2015.pdf?WT.mc_id=EMI_NATURE_1509_YOUNGINVESTIGATOR2015&spMailingID=49568192&spUserID=MTYxNjA5NDg5ODE3S0&spJobID=762344014&spReportId=NzYyMzQ0MDE0S0

Julie Gould: Congratulations on being awarded this year’s prize. How did it feel when you found out that you had won?

Thomas Wollert: That came as a big surprise to me. It’s a great honor and it’s of course a major recognition of our work; not only my work, but also the work that my laboratory has done over the past five years. So this is very important to me.

JG: Tell us a little bit about the research you are working on.

TW: The cells in our bodies recycle almost everything — they do not waste much. The question in the past has been: how is this achieved? The process needs to be highly regulated. You don’t want to degrade something that you still need, but you do want to get rid of dangerous material that accumulates in the cell. We became interested in one pathway that is involved in transporting this sort of trash, or unwanted material, to recycling stations in the cell. We are particularly interested in how the molecular mechanism is driven.

JG: What sort of molecular trash are we talking about?

TW: Everything that needs to be degraded in a cell has to end up at a recycling station, one of which is called the lysosome. What ends up there is chemically degraded, and the building blocks are reused by the cell to build material. Proteins that become aggregated, big material or composite structures, and everything else in the cell cytoplasm (such as mitochondria) need to be transported to the lysosome. There is a specialized pathway to do that — this has been called autophagy for self-digestion. During autophagy, crescent-shaped membranes are formed, which expand and capture cytoplasmic components. These structures become autophagosomes, which are like entire organelles and are the containers that transport the trash to the lysosomes for degradation.

JG: How do these autophagosomes form in the cell?

TW: In yeast the system is fairly well understood. Small membrane vesicles are recruited and fuse to form the crescents haped autophagic precursor membrane. This membrane then surrounds and captures material, and, after sealing, the full autophagosome is formed and finally fuses with the lysosome. There are 40 different proteins in yeast that have been identified as those that have an essential function in autophagy — they are specific to the autophagy pathway. The question was, what are they doing with the membrane and what is their molecular function? And that was the major interest of my lab.

JG: What did you discover? TW:

We analysed two important steps in autophagy. The first is initiation and the second is expansion.

An autophagosome is built from small vesicles, which come together and fuse. This process is driven by one big complex called the Atg1-kinase complex. This complex is known to be involved in recruiting the donor vesicles that create the autophagosome. We recently published work on the expansion step. This is an interesting step that involves a small ubiquitin-like molecule, Atg8. The unique feature of this particular molecule is that it becomes covalently attached to autophagic precursor membranes. Many Atg8 molecules get conjugated to these membranes, so the question has been: why is there so much Atg8 on the membrane and what is its job there? To answer this, we analyzed the proteins independently of the complex cellular environment. We produced recombinant molecular machines that drive the formation of autophagosomes and analyzed their function in the test tube. The test-tube components include the protein subunits of these molecular machines and model membranes that serve as the platform for proteins to assemble into large complexes. What we realized — and what came as a surprise to us — was that the molecular machine that drives conjugation of Atg8 stays with Atg8 at the membrane, rather than leaving after conjugation. We predicted that something needs to happen, some bigger structure needs to form on the membrane to keep the conjugation machine there. Using high-resolution approaches, we observed that Atg8 forms together with its conjugation machine, a protein shell on membranes. It’s like a meshwork that sits on top of the membrane and stabilizes the forming autophagosome. Presumably.

JG: Why presumably?

TW: Because the details of how this expansion is driven by the scaffold is something that we are investigating.

JG: Will you be following this up over the next few years?

TW: Yes. This is an interesting question, but not an easy one to answer. We need to understand the direct relationship of how this really works in vivo.

JG: How does the autophagosome capture material from cells?

TW: The selection of cargo comes in two flavours. Under normal conditions, when the cell is happy, it only wants to degrade unwanted material or something damaged. It chooses these materials quite selectively. For example, it might only want to degrade dysfunctional mitochondria, the cell’s power plants. The membrane then wraps tightly around these structures. However, if a cell becomes stressed or starved, it can use autophagy to degrade anything that’s around. That means bulk cytoplasm without any selectivity. Imagine a big happy cell that is starved and goes on a low-value nutritional diet. The cell will shrink, but it survives. If nutritional conditions improve, it can grow again.

JG: What big impacts will this research have?

TW: The research focus at the moment is neurodegenerative disease and cancer. In certain neurodegenerative diseases, some proteins can accumulate in cells. There are a couple of diseases, such as Huntington’s disease, in which particular genetic modifications lead to alterations in proteins, which then tend to aggregate. In other diseases, such as Alzheimer’s disease, proteins also accumulate, and those protein oligomers, or aggregates, are toxic to the cell. In some neurodegenerative diseases, it has been observed that increasing autophagy is beneficial for cells, and thus patients, because increasing autophagy increases the removal of the toxic material. Neurodegenerative disease is usually not observed until the later stages, when this material has already accumulated. If you could remove this harmful material from cells, you could maybe rescue some neurons from dying. This is one application where you would really want to increase autophagy. In cancer, it has already been shown that combining chemotherapy with an inhibitor of autophagy is beneficial because autophagy just counteracts chemotherapy.

JG: What is it about this field that you find so interesting?

TW: What excites me the most is that you can use a minimal system, combining a few components and then trying to get them to work in a test tube. Our major goal, and our holy grail in this research, is to have the full autophagy pathway in a test tube, combining the autophagy components, step by step, to produce an autophagosome from small membranes, and to have some material wrapped in the autophagosome.

Award Winners

2015 Winner

In 2015 Eppendorf AG is presenting the Eppendorf Award for Young European Investigators for the 20th time. The independent Eppendorf Award Jury chaired by Prof. Reinhard Jahn selected Dr. Thomas Wollert (Research Group Leader Molecular Membrane and Organelle Biology at the Max Planck Institute of Biochemistry in Martinsried, Germany) as the 2015 winner of the Eppendorf Award for Young European Investigators. Thomas Wollert, born 1979, receives the €20,000 prize for his groundbreaking work in reconstituting complex intracellular membrane events in the test tube using artificial membranes and purified components. Thomas talks about his work in this Award Feature

The official prize ceremony took place at the EMBL Advanced Training Centre in Heidelberg, Germany, on June 25, 2015.

To hear an interview with prize winner Thomas, listen here.

2014 Winner

The independent Eppendorf Award Jury chaired by Prof. Reinhard Jahn selected Madeline Lancaster, Ph.D., of the Institute of Molecular Biotechnology of the Austrian Academy of Sciences, Vienna, Austria, as the 2014 winner of the Eppendorf Award for Young European Investigators. Madeline Lancaster, born 1982, receives the € 15,000 research prize for her work showing that complex neuronal tissues resembling early states of fetal human brain can be created in vitro from pluripotent stem cells. Madeline talks about her work in this Award Feature

To hear an interview with prize winner Madeline, listen here or watch the video from the award ceremony.

2013 Winner

The independent Eppendorf Award Jury chaired by Prof. Reinhard Jahn selected Ben Lehner, Ph.D., of the Centre de Regulació Genòmica, Barcelona, Spain, as the 2013 winner of the Eppendorf Award for Young European Investigators. Ben, born 1978, receives the € 15,000 research prize for his discoveries concerning the fundamental question why mutations in the genome result in variable phenotypes. Ben talks about his work in this Award Feature.

To hear an interview with prize winner Ben, listen here or watch the video from the award ceremony.

2012 Winner

The 2012 prize was awarded to Elizabeth Murchison, Ph.D. (Wellcome Trust Sanger Institute, Cambridge, United Kingdom) for her discoveries concerning a deadly cancer that is spreading among the endemic population of Tasmanian devils in Tasmania and threatening the survival of the species. Elizabeth talks about her work in this Award Feature.

To hear an interview with prize winner Elizabeth, listen here or watch the video from the award ceremony in Heidelberg.

2011 Winner

The 2011 Eppendorf Young European Investigator Award goes to Suzan Rooijakkers for her contribution to discovering how Staphylococcus aureus evades immune attack. Suzan talks about her work on this Award Feature.

To hear an interview with prize winner Suzan, listen here.

Listen here to the podcast from the award ceremony in Heidelberg.

2009 Winner

In 2009 the prize was awarded to Óscar Fernández-Capetillo, head of the Genomic Instability Group at the Spanish National Cancer Center. Read the highlights of his interview with Nature in this Award Feature.

Listen here to learn about the impact the Award had on his career.

2008 Winner

The 2008 prize was awarded to Dr. Simon Boulton of the London Research Institute. Read the highlights of his interview with Nature in this Award Feature.

Listen here to learn about the impact the Award had on his career.

2007 Winner

Dr Mónica Bettencourt-Dias is the 2007 winner of the Eppendorf Young European Investigator Award. Monica gives a personal account of her research and the Eppendorf Award in an Award Feature forNature.

Listen here to learn more about the impact the award had on her career.

2006 Winner

Dr Luca Scorrano won the award in 2006. Read more about his research on the Eppendorf Young Investigator website.

Listen here to learn more about Dr Scorrano’s work and the impact the award has had on his career.

http://www.nature.com/multimedia/podcast/eppendorf/eppendorf-podcast-15.mp3   2015

https://www.youtube.com/watch?feature=player_embedded&v=N3SXLURTI_w   2014

https://www.youtube.com/watch?feature=player_embedded&v=ntU_Ve3x6oI     2013

https://www.youtube.com/watch?feature=player_embedded&v=E2mhX9ccEHs    2012

http://media.nature.com/download/nature/nature/podcast/eppendorf/eppendorf_2011_winner.mp3

http://media.nature.com/download/nature/nature/podcast/eppendorf/eppendorf_2011.mp3

http://media.nature.com/download/nature/nature/podcast/eppendorf/eppendorf_2010.mp3

http://media.nature.com/download/nature/nature/podcast/eppendorf/eppendorf-2009.mp3

Read Full Post »

Mature cells can be reprogrammed to become pluripotent – John Gurdon and Shinya Yamanaka

Larry H. Bernstein, MD, FCAP, Curator

Leaders in Pharmaceutical Innovation

Series E: 2; 7.1

In 1962, John B. Gurdon successfully cloned frogs. He took the nucleus of an adult frog cell – the part of the cell that holds the DNA – and put it into a frog egg cell. The egg was able to develop into a normal tadpole. These experiments showed that an adult, specialised cell still had the information needed to form a new tadpole. The same technique was later used to produce the famous cloned sheep, Dolly.

In 2006, Shinya Yamanaka’s work again took the scientific community by surprise and changed the way researchers think about how cells develop.Yamanaka showed that adult, fully specialised mouse cells could be reprogrammed to become cells that behave like embryonic stem cells – so-called induced pluripotent stem cells, which can develop into all types of cells in the body.

Gurdon and Yamanaka’s work is celebrated and explained in the award-winning documentary, Stem Cell Revolutions, by Clare Blackburn and Amy Hardie. The short clip above is taken from the film and links Gurdon and Yamanaka’s work (click the red button on the image above to watch the clip). Amy Hardie, who directed the film, commented: “So many scientists have said that Shinya Yamanaka has overturned our understanding of basic developmental biology. And he has – with the discovery of iPS cells. What Shinya Yamanaka himself points out and we were able to show in our film, Stem Cell Revolutions, is the lineage from John Gurdon who cloned frogs in Cambridge. Shinya’s groundbreaking discovery would not have been possible without Gurdon’s pioneering work.

Proc Natl Acad Sci U S A. 2013 Apr 9; 110(15): 5740–5741.

Published online 2013 Mar 28. doi:  10.1073/pnas.1221823110

Sir John Bertrand Gurdon, FRS, FMedSci (born 2 October 1933), is an English developmental biologist. He is best known for his pioneering research in nuclear transplantation[2][3][4] and cloning.[1][5][6][7] He was awarded the Lasker Award in 2009. In 2012, he and Shinya Yamanaka were awarded the Nobel Prize for Physiology or Medicine for the discovery that mature cells can be converted to stem cells.[8]

The Nobel Prize in Physiology or Medicine 2012
Sir John B. Gurdon, Shinya Yamanaka

ohn Bertrand Gurdon (JBG), born 2 October 1933, was brought up in a comfortable home by his parents (fig.1) on the Surrey/Hampshire border in a village, Frensham in South England, endowed with a large amount of National Trust heathland and ponds. His mother, Marjorie Byass, was from an East Yorkshire farming family. Brought up on a farm, and educated in that region, she became a physical training teacher working for some time in an American private school. When her son and daughter (Caroline, who trained as a nurse) had been raised, she gave much time to the regional administration of the “Women’s Institute,” a voluntary organisation for educating women.

His father, William Gurdon, was from a longstanding Suffolk family whose ancestors go back to 1199 (fig. 2; Muskett, 1900; Cunnington, 2008); with the family motto “virtus viget in arduis” [virtue flourishes in adversity].

Paternal lineage of JBG.

Many of them had distinguished careers in government and as regional administrators, including Sir Adam Gurdon [Muskett, 1900]. JBG’s ancestors lived in a stately home, Assington Hall, in West Suffolk (fig. 3).

His grandfather had to leave the family home through lack of money to maintain it, due to repeal of the Corn Laws (1846) so that tenant farmers could no longer pay their rent, because of foreign imports. Assington Hall was requisitioned by the army during World War II, and was burnt down in a supposedly accidental fire in 1957. The remaining part of the house was partly restored and part of the original home, including its minarets, is still present in Assington. One of JBG’s ancestors married again after his first wife died and the outcome of a second marriage yielded a distinguished lawyer who accepted the hereditary title of Baron Cranworth. JBG’s father left school at the age of 16 and took a position in a rice broking firm in Burma. He was an early volunteer in the First World War and was decorated with the Distinguished Conduct Medal (DCM) before being commissioned to an officer rank. After that he led a career in banking in Assam and East India. He retired, in his forties, and in retirement, he gave much time to the transcribing of professional textbooks (especially legal) into Braille for the blind as voluntary work.

World War II started in 1939 when JBG was aged six. It was a time of austerity. Limited rations of food were managed by his mother, and the garden was used to raise chickens. He did not see luxuries like a banana or an orange until well after the end of the war. At the age of eight he was sent to a local private school, Frensham Heights. In an intelligence test at that age, he was asked to draw an orange. He started drawing the stalk by which the orange would hang from a tree, reasoning that an orange would not exist in space. The teacher tore up the piece of paper and reported to his parents that he was mentally subnormal and would need special teaching. The teacher meant to say, draw a circle. He was moved to another private school in the village, namely Edgeborough, where he thrived. At that age he had an intense interest in plants and insects. In most of his spare time he collected butterflies and moths and raised their caterpillars.

At the age of 13, he started school at Eton as a boarder. He found life there intensely uncomfortable, because senior boys acted as despots, administering punishments for trivial misdemeanours. As a means of survival, he took up squash, and as a result of hard work rather than ability, he became eventually the school captain in this sport. While at school he continued his interest in Lepidoptera, raising large numbers of moths from their larval stage.

Gurdon attended Edgeborough and then Eton College, where he ranked last out of the 250 boys in his year group at biology, and was in the bottom set in every other science subject. A schoolmaster wrote a report stating “I believe he has ideas about becoming a scientist; on his present showing this is quite ridiculous.”[9] Gurdon explains it is the only document he ever framed; Gurdon also told a reporter “When you have problems like an experiment doesn’t work, which often happens, it’s nice to remind yourself that perhaps after all you are not so good at this job and the schoolmaster may have been right.”[10]

It was during his first term of being taught Science at the school, at the age of 15, that he received a totally damning report from the Biology master (fig. 4). This report resulted from JBG being placed in the bottom position of the lowest form in a group of 250 students of the same age. The report, sent to his housemaster, resulted in him being taken off any further study of Science of any kind at the school. For the rest of his school days, for the next three years, he was given no Science teaching and was placed in a class which studied Ancient Greek, Latin and a modern language, a course intended for those judged to be unsuited for studying any subject in depth.

Eton school report for JBG from Biology master, 1949.

 

Entrance to University was a problem: having sat the Entrance examination in Latin and Greek, the Admissions tutor at Christ Church Oxford University told JBG that he would be accepted for Entrance on condition that he did not plan to study the subject in which he took the Entrance (Classics). Later the Admissions tutor admitted that he had under-filled the college and had his mind on other things; he was Hugh Trevor-Roper, later Lord Dacre, and author of The Last Days of Hitler. In due course it emerged that JBG’s acceptance for Christ Church involved a complicated arrangement between JBG’s uncle, at that time a Fellow of Christ Church, JBG’s school housemaster and a friend of his uncle, Sir John Masterman, who was Master of Worcester College, Oxford and in charge of the wartime Enigma operation at Bletchley, agreeing to accept the housemaster’s son. Such a manoeuvre, and admission to Oxford on those terms, could never happen now. At that time, 1952, it was not very easy to fill a college with paying students. Before entering University, JBG had to take a year off to learn elementary Biology with a private tutor, generously funded by his parents who had already paid several years of Eton fees. He was told that he could formally enter the Department of Zoology course at Oxford if he passed the elementary exams in Physics, Chemistry and Biology in a preliminary year. He survived this and started the course in Zoology at Oxford in 1953. The course was extremely oldfashioned, by today’s standards. A major part of the teaching involved learning Palaeontology, and the names of skeletal parts of dinosaurs. JBG later became a personal friend of Sir Alister Hardy, the Head of that department, through his Oxford aunt (see later).

As the Zoology course came to an end, JBG enquired about the possibility of doing a PhD in Entomology, in accord with his continuing interest in insects. While still a student, he had got permission to go to Oxford University’s nature reserve, namely Wytham Woods, with his butterfly net. No butterflies were to be seen, but he caught the only moving thing, which was a kind of fly. He used the taxonomic reference works to try to identify this “fly.” Having realised that the fly was a Hymenopteron, he was still unable to identify it. He therefore went to the Natural History Museum in London for help. They pronounced that it was in fact a species of sawfly new to Britain. This must have been intensely irritating to the Professor of Entomology, whose main research project was to identify animals and plants in Wytham Woods. JBG was later rejected for PhD work in Entomology. This was a great blessing because the work he would have done in Entomology was not well regarded and had very little, if any, analytical component to it. By his immense good fortune, he was invited to do a PhD with the Oxford University lecturer who taught Developmental Biology, Dr Michael Fischberg.

Fischberg was born in St Petersburg, Russia, in 1919. He was educated in Switzerland and was a PhD student of E. Hadorn. Hadorn in turn was a student of F. Baltzer, who was a student of H. Spemann, himself a student of T. Boveri. This German-Swiss lineage of eminent Developmental Biologists turns out to be the background of a great many of the successful Developmental Biologists of the mid-1950s. Most of those that did not have this background can trace their own training back to R. G. Harrison (1870–1959) of the USA, who pioneered cell culture. Having finished his PhD with Hadorn, Fischberg took a position in the Institute of Animal Genetics under Waddington in Edinburgh, from where he accepted his appointment in the Oxford Zoology department, headed by Professor Sir Alister Hardy, an eminent marine biologist [Royal Society memoirs].

Starting his PhD work in 1956, Fischberg suggested to JBG that he should try to carry out somatic cell nuclear transfer in Xenopus, a procedure for this having been recently published by Briggs and King (1952). The advisability and technical problems that arose at this point are described in the accompanying papers (Gurdon 2013 a,b). Once these technical obstacles had been overcome, largely as a result of good luck, JBG’s work proceeded extraordinarily fast; strongly motivated by early success, he became an intensely hard worker. By the end of his PhD he had succeeded in obtaining normal development of intestinal epithelium cell nuclei transplanted to enucleated eggs of Xenopus. When these tadpoles had eventually reached sexual maturity, he was able to publish a paper entitled “Fertile intestine nuclei.”This was the first decisive evidence that all cells of the body contain the same complete set of genes. This answered a long-standing and important question in the field of Developmental Biology. However it also showed very clearly, as was commented on in JBG’s papers at the time, the remarkable ability of eggs to reprogram somatic cell nuclei back to an embryonic state. Eventually this phenomenon attracted increasingly large interest, and led to the idea of cell replacement using accessible adult cells, such as skin. A key future discovery was that of Martin Evans (Nobel Prize, 2006) that a permanently proliferating embryonic stem cell line could be established from mouse embryos. Under appropriate conditions these cells could be caused to differentiate into all different cell types. The combination of somatic cell nuclear transfer and the derivation of embryonic stem cells in mammals made it realistic to think of cell replacement for human diseases. A huge boost for this idea was later provided by Takahashi and Yamanaka (2006), with their discovery that the overexpression of certain transcription factors can also yield embryonic stem cells from adult somatic tissue. The accompanying Nobel lecture provides more detail of the later scientific part of JBG’s career.

A visit by the Nobel Laureate George Beadle to the Fischberg Group in the Oxford Zoology department in 1960 led to an offer from the California Institute of Technology (CalTech) (previous chairman George Beadle) for JBG to do postdoctoral work there. Fischberg very wisely advised JBG to accept the CalTech offer of postdoctoral work rather than offers from other nuclear transplant labs. Stimulated by his mother’s adventurous spirit, JBG decided to buy a secondhand Chevrolet in New York and drive across the USA to California, using the famous Route 66 (now replaced). He gave lectures as he travelled across the USA and stopped at laboratories of Briggs and King, Alexander Brink (paramutation) etc. He had hoped to become a post-doctoral student of R. Dulbecco at CalTech (Nobel Prize), but the chairman of that department advised against this because JBG had no training in virology. Therefore JBG did his postdoctoral work with Robert Edgar on Bacteriophage Genetics. JBG found he had no aptitude at all for Phage Genetics and decided to return to Britain after one year at CalTech. Nevertheless, that year at CalTech was extremely formative because it provided some acquaintance with Molecular Biology, which had so far entirely escaped his training. During that year he met Sturtevant, a student of Morgan, who pioneered the whole field of Drosophila Genetics. He also got to know Ed Lewis (future Nobel Laureate). Thanks to James Ebert (director of the Department of Embryology, Carnegie Institute of Washington, in Baltimore) JBG visited various labs in the USA at the end of his post-doctoral period and met Donald Brown in Baltimore on that visit. Meantime, the success of the nuclear transfer work in Oxford had led to Michael Fischberg being offered a head of department professorship in Geneva, Switzerland. JBG was offered the teaching position in Oxford vacated by M. Fischberg. JBG returned from California to England via Japan and many other countries over a two-month period. One month of that time he spent in Japan and met Tokindo Okada and made other friends in Japan, including M. Furusawa and subsequently Koichiro Shiokawa.

While doing graduate and postdoctoral work in Oxford, JBG made other contacts and friendships. His mother’s sister lived in Oxford, and he spent much time at her house and visiting famous gardens, fostering a lifelong interest in plants. Through that connection he met Miriam Rothschild, and became a lifelong friend of hers (Van Emden and Gurdon, 2006). This friendship contained, through Miriam Rothschild’s generosity, ski mountaineering holidays based in her house in Wengen. JBG had achieved the British ski club’s Gold standard ski medal, again through relentless practice rather than any natural ability. Also, in accord with his interest in the open air and dogged determination, he became a reasonably accomplished ice figure skater.

Nobel Lecture by Sir John B. Gurdon (42 minutes)

Sir John B. Gurdon delivered his Nobel Lecture on 7 December 2012 at Karolinska Institutet in Stockholm. He was introduced by Professor Urban Lendahl, Chairman of the Nobel Committee for Physiology or Medicine.
Credits: Sveriges Television AB (production)

Copyright © Nobel Media AB 2012

The Nobel Prize in Physiology or Medicine 2012    Lecture (pdf)

Nuclear transfer

In 1958, Gurdon, then at the University of Oxford, successfully cloned a frog using intact nuclei from the somatic cells of a Xenopus tadpole.[14][15] This work was an important extension of work of Briggs and King in 1952 on transplanting nuclei from embryonic blastula cells[16] and the successful induction of polyploidy in fish Stickleback, Gasterosteus aculatus, in 1956 by Har Swarup reported in Nature.[17] However, he could not yet conclusively show that the transplanted nuclei derived from a fully differentiated cell. This was finally shown in 1975 by a group working at the Basel Institute for Immunology in Switzerland.[18] They transplanted a nucleus from an antibody-producing lymphocyte (proof that it was fully differentiated) into an enucleated egg and obtained living tadpoles.

Gurdon’s experiments captured the attention of the scientific community and the tools and techniques he developed for nuclear transfer are still used today. The term clone[19] (from the ancient Greek word κλών (klōn, “twig”)) had already been in use since the beginning of the 20th century in reference to plants. In 1963 the British biologist J. B. S. Haldane, in describing Gurdon’s results, became one of the first to use the word “clone” in reference to animals.

Messenger RNA expression

Gurdon and colleagues also pioneered the use of Xenopus (genus of highly aquatic frog) eggs and oocytes to translate microinjected messenger RNA molecules,[20] a technique which has been widely used to identify the proteins encoded and to study their function.

Recent research

Gurdon’s recent research has focused on analysing intercellular signalling factors involved in cell differentiation, and on elucidating the mechanisms involved in reprogramming the nucleus in transplantation experiments, including the role of histone variants,[21][22] and demethylation of the transplanted DNA.[23]

Reprogramming of Mature Cells

Our lives begin when a fertilized egg divides and forms new cells that, in turn, also divide. These cells are identical in the beginning, but become increasingly varied over time. As a result of this process, our cells become specialized for their location in the body – perhaps in a nerve, a muscle, or a kidney. It was long thought that a mature or specialized cell could not return to an immature state, but this has been proven incorrect.

In 1962, John Gurdon removed the nucleus of a fertilized egg cell from a frog and replaced it with the nucleus of a mature cell taken from a tadpole’s intestine. This modified egg cell grew into a new frog, proving that the mature cell still contained the genetic information needed to form all types of cells. In 2006, Shinya Yamanaka succeeded in identifying a small number of genes within the genome of mice that proved decisive in this process. When activated, skin cells from mice could be reprogrammed to immature stem cells, which, in turn, can grow into all types of cells within the body. In the long-term, these discoveries may lead to new medical treatments.

Shinya Yamanaka

A winding road to pluripotency

http://www.nobelprize.org/nobel_prizes/medicine/laureates/2012/yamanaka-lecture.pdf

http://www.nobelprize.org/nobel_prizes/medicine/laureates/2012/ypdfamanaka-lecture_slides.

Nobel Lecture

46 min.
by Shinya Yamanaka Center for iPS Cell Research and Application (CiRA), Kyoto University, Kyoto 606-8507, Japan.
Gladstone Institute of Cardiovascular Disease, San Francisco, CA 94158, USA.
INTRODUC TION John Gurdon received recognition for his landmark achievement in 1962, which provided the first experimental evidence of reprogramming by the transplantation of amphibian somatic cell nuclei into enucleated oocytes [1]. This breakthrough in technology introduced a new paradigm; that each nucleus of a differentiated cell retains a complete set of blueprints for the whole body, while oocytes possess a certain potential for reprogramming. Inspired by this paradigm shift and subsequent research achievements, we identified four transcription factors that could induce pluripotency in somatic cells by their forced expression and successfully consolidated effective reprogramming methods in mouse cells in 2006 [2] and in human cells in 2007 [3]. The established reprogrammed cells were named “induced pluripotent stem (iPS) cells.” I would like to provide an overview focusing on the experimental background of the generation of iPS cells, and the future perspectives regarding iPS cell research, which has been developing rapidly.

Figure 1. My first experiment as a graduate student. Intravenous injection of a vasoactive molecule platelet activating factor (PAF) caused a transient decrease in blood pressure in dogs (upper panel). We hypothesized that this hypotension would be blocked by pretreatment with a thromboxane A2 inhibitor (lower left panel). Unexpectedly, we observed a profound hypotension (lower right panel).

In 1989, however, my life took a new turn from clinical medicine in orthopedic surgery to basic science research for two reasons. First, I found that I was not a very talented surgeon. Second, I saw many patients suffering from intractable diseases and injuries, which even highly talented surgeons and physicians were not able to cure. For example, I had encountered patients suffering from spinal cord injuries, amyotrophic lateral sclerosis and osteosarcomas. Furthermore, I lost my father due to liver cirrhosis during my residency. Basic medical research is the only way to find cures for these patients. For these reasons, I decided to go back to school. I became a Ph.D. student at Osaka City University Medical School in April of 1989.

Among the many departments at the school, I applied to the Department of Pharmacology, directed by Dr. Kenjiro Yamamoto.  Dr. Ikemoto repeatedly told me that we should not perform research that simply reproduced somebody else’s re-sults. Rather, we should do something unique and new. During my training as a scientist, I was very fortunate to have two types of teachers: namely, great men-tors and unexpected results from my experiments.
My direct mentor at the graduate school was Dr. Katsuyuki Miura. In my first few months as a Ph.D. student, Dr. Miura told me to read as many manuscripts as possible and propose new projects. I felt like I was given a blank canvas and told that I could draw whatever I wanted. This mentorship was very different from what I had experienced during my residency. At the hospital, I’d had little freedom, and had to follow instructions from senior physicians and textbooks. I thought “wow, I like this system!” Another thing that Dr. Miura often told me was that we were competing worldwide. Whatever project you chose, you will compete with other scientists throughout the world, mostly in the U.S. or Europe, on the same or similar projects. This was again very different from my experience at the hospital, where I was competing only with other residents at the same hospital. The idea of “worldwide” competition had never entered my mind when I was working at the hospital. For all of these reasons, I found that basic research was a more suitable career, based on my interests and temperament.
In the summer of 1989, I was still struggling to find my project. Dr. Miura proposed a simpler project to begin my research studies. He suggested that I examine the role of a vasoactive molecule, platelet activating factor (PAF), in dogs to study the regulation of blood pressure (Fig. 1). Because it was known that the intravenous injection of PAF into dogs caused a transient decrease in blood pressure (transient hypotension), Dr. Miura hypothesized that this decrease in blood pressure would be mediated by another vasoactive molecule, thromboxane A2. If that hypothesis was correct, then pretreatment with a thromboxane A2 inhibitor should block the PAF-induced transient decrease in blood pressure. My first experiment, where I treated dogs with an inhibitor of thromboxane A2, was performed based on his hypothesis, and I had expected no decrease in the blood pressure in the pretreated dogs. It should have been a simple experiment suitable for a beginner. However, the result was totally unexpected. In the beginning, the thromboxane A2 inhibitor did not seem to be effective, with subsequent PAF treatment inducing the normal transient decrease in the blood pressure. Surprisingly, however, a few minutes after the treatment, a profound and prolonged decrease in blood pressure was observed, which we had never observed following treatment with PAF alone (Fig. 1). I got so excited! I ran into Dr. Miura’s office to report this result excitedly. Although the result did not support his hypothesis, Dr. Miura responded with excitement, too, and encouraged me to explore the finding further. I spent another two years uncovering the mechanism responsible for this unexpected result [4, 5]. I was extremely lucky to obtain this kind of unexpected result in my very first experiment as a graduate student.

A scandal involving Japanese stem-cell research took a surprising turn Monday when the nation’s most revered researcher in the field, Nobel Prize laureate Shinya Yamanaka, apologized for what he described as poor record-keeping.

The apology came after months of soul-searching in Japan over research ethics. A researcher at the prestigious Riken institute, Haruko Obokata, apologized earlier this month after admitting errors in a paper in the journal Nature that described a possible new method of creating stem cells.

Last week, the head of the Riken panel investigating Dr. Obokata had to resign from the panel after admitting that a paper he co-authored used some of the same improper methods of cutting and pasting images that he had criticized in Dr. Obokata’s work.

On Monday evening, Dr. Yamanaka, a professor at Kyoto University, spoke at a news conference after questions arose about an image in a 2000 paper on which he was the lead author. In the paper, Dr. Yamanaka, then at Nara University, described a protein that played a role in turning embryo cells into cells specific to a part of the body.

The university said it conducted an investigation after Dr. Yamanaka informed administrators about allegations he discovered online that an image in the paper was doctored.

 

Read Full Post »

McEwen Award for Innovation: Irving Weissman, M.D., Stanford School of Medicine, and Hans Clevers, M.D., Ph.D., Hubrecht Institute

Larry H. Bernstein, MD, FCAP, Curator
Leaders in Pharmaceutical Innovation

Series E. 2; 7.3

Past winners include Azim Surani, James Thomson, Rudolf Jaenisch and Kazutoshi Takahashi with Shinya Yamanaka

The International Society for Stem Cell Research (ISSCR) has presented EuroStemCell partner Hans Clevers with the McEwen Award for Innovation at the opening of its annual meeting, today (24 June) in Stockholm, Sweden.

The prizes awarded by ISSCR in 2015 are:

McEwen Award for Innovation: Irving Weissman, M.D., Stanford School of Medicine, and Hans Clevers, M.D., Ph.D., Hubrecht Institute

ISSCR-BD Biosciences Outstanding Young Investigator Award: Paul Tesar, Ph.D., Case Western Reserve University School of Medicine

ISSCR Public Service Award: Alan Trounson, Ph.D., MIMR-PHI Institute of Medical Research

 

In 2015, the ISSCR recognizes long-standing contributors to the field, Weissman and Clevers, for the identification, prospective purification and characterization of somatic (adult) tissue-associated stem cells and advancement of their research findings toward clinical applications.

Award recipient Weissman’s many discoveries have helped map the direction of the stem cell field and have served as the basis for important research and work by scientists all over the world.  He was the first to isolate and characterize hematopoietic (blood) stem cells from mice and humans. He developed the approaches and technologies, now widely used within the field, for isolating blood stem and progenitor cells and defining their properties. Weissman pioneered the extension of his approaches to isolation of other stem cell types, including human nervous system cells and skeletal muscle myogenic stem/progenitor cells. Further, he discovered several independent leukemia stem cells and, more recently, bladder cancer stem cells, head and neck cancer stem cells and malignant melanoma stem cells. Weissman has pursued these discoveries to develop several promising means of cancer therapy.

Award recipient Clevers has been a leader in biomedical sciences and the area of Wnt signaling in colon cancer for more than three decades. He and his lab developed tools to identify and track an adult stem cell population able to give rise to the entire lining of the gut and later to demonstrate that these cells can be isolated and grown in culture as “miniguts,” recapitulating the normal structure and function of the gut. These discoveries are a move toward promising therapies for colon conditions, like ulcers, in which the lining of the intestine has been destroyed in patches, and provide a powerful resource for modeling disease pathology and for drug screening.

“Irv Weissman and Hans Clevers have made enormous contributions to stem cell science. Working in the blood and gut systems, respectively, and extending their findings in different tissues, they have defined the concepts and technologies that underpin many avenues of research,” Hans Schöler, chair of the ISSCR’s McEwen Awards selection committee, said. “Each has made pioneering conceptual advances in disease modeling and regenerative medicine.”

 

The ISSCR-BD Biosciences Outstanding Young Investigator Award recognizes exceptional achievements by an ISSCR member and investigator in the early part of their independent career in stem cell research.  The winner receives a $7,500 USD personal award and is invited to present at the ISSCR’s annual meeting. Past winners include Valentina Greco, Marius Wernig, Cédric Blanpain, Robert Blelloch, Joanna Wysocka and Konrad Hochedlinger.

Award recipient Tesar established his independent laboratory five years ago and has rapidly risen to his current position as the Dr. Donald and Ruth Weber Goodman Professor of Innovative Therapeutics and tenured Associate Professor in the Department of Genetics and Genome Sciences at Case Western Reserve University School of Medicine. Tesar’s studies have shaped the global understanding of both pluripotent stem cell and oligodendrocyte biology. His seminal and highly cited report on epiblast stem cells, published in Nature in 2007, along with similar findings by Pedersen, Vallier and colleagues, led to a complete shift in the understanding of how pluripotency is regulated in the mammalian embryo.  He has continued to provide high impact contributions to the field, pioneering new methods to generate and mature oligodendrocyte progenitor cells, and to use these to enhance repair in animal models of multiple sclerosis.

Stanford stem cell pioneer Irving Weissman wins international honors

by Krista Conger on Feb 10, 2015
http://news.stanford.edu/thedish/2015/02/10/stanford-stem-cell-pioneer-irving-weissman-wins-international-honors/

IRVING WEISSMAN, a professor of pathology and of developmental biology at Stanford Medical School, was recently awarded the Charles Rodolphe Brupbacher Prize for Cancer Research in Zurich.

Weissman, who directs the Stanford Institute for Stem Cell Biology and Regenerative Medicine, was honored for his role in identifying and isolating the first hematopoetic, or blood-forming, stem cell in mice in 1988, and then in humans in 1992. In 2000, he also isolated leukemia cancer stem cells from humans. Recently, he and his colleagues have devoted themselves to understanding how cancer cells escape destruction by the immune system by expressing a “don’t eat me” signal on their cell membranes.

“His discoveries on aging processes in stem-cell systems and ultimately his contribution toward understanding cancer stem cells and the way in which the immune system can control these cells are pioneering achievements with far-reaching clinical implications,” Markus Manz, director of the Department of Hematology at the University Hospital Zurich, said of Weissman at a symposium titled “Breakthroughs in Cancer Research and Therapy” where the prize was announced.

Weissman also is the director of Stanford’s Ludwig Center for Cancer Stem Cell Research and Medicine and holds the Virginia and Daniel K. Ludwig Professorship in Clinical Investigation in Cancer Research.

The prize, presented by the Charles Rodolphe Brupbacher Foundation, included 100,000 Swiss francs, or about $108,000.

The Charles Rodolphe Brupbacher Foundation was founded in 1991 by Brupbacher’s wife, Frederique, in honor of her late husband. This is the 12th time the prize, which is meant to recognize internationally acknowledged achievements in fundamental cancer research, has been awarded. Brupbacher was a Swiss banker, economist and international currency expert.

In addition to the Brupbacher Prize, it was recently announced that Weissman will receive theMcEwen Award for Innovation, supported by the McEwen Centre for Regenerative Medicine in Toronto. The award will be presented in June at the annual meeting of the International Society for Stem Cell Research in Stockholm. It recognizes the work of Weissman and Hans Clevers, of the Hubrecht Institute in the Netherlands, in the identification, purification and characterization of adult stem cells from a variety of human tissues and cancers. Weissman and Clevers will share a $100,000 award.

Anti-CD47 antibody may offer new route to successful cancer vaccination

Scientists at the School of Medicine have shown that their previously identified therapeutic approach to fight cancer via immune cells called macrophages also prompts the disease-fighting killer T cells to attack the cancer.

The research, published online May 20 in the Proceedings of the National Academy of Sciences, demonstrates that the approach may be a promising strategy for creating custom cancer vaccines.

Various researchers have been working over the years to create vaccines against cancer, but the resulting vaccines have not been highly effective. Current approaches to developing the vaccines rely on using immune cells called dendritic cells to introduce cancer protein fragments to T cells — a process known as antigen presentation. The hope has been that the process would stimulate the body’s T cells to identify cancer cells as diseased or damaged and target them for elimination. However, this process often only modestly activates the most potent cancer-fighting kind of T cell, called killer T cells or CD8+ T cells.

The Stanford team discovered that there was another viable vaccine approach, using the macrophage pathway to program killer T cells against cancer. Irving Weissman, MD, professor of pathology and of developmental biology, and his team previously showed that nearly all cancers use the molecule CD47 as a “don’t-eat-me” signal to escape from being eaten and eliminated by macrophages. The researchers found that anti-CD47 antibodies, which can block the “don’t-eat-me” signal and enable macrophages to engulf cancer cells, eliminated or inhibited the growth of various blood cancers and solid tumors.

In the new study, the Stanford team showed that after engulfing the cancer cells, the macrophages presented pieces of the cancer to CD8+ T cells, which, in addition to attacking cancer, are also potent attackers of virally infected or damaged cells. As a result, the CD8+ T cells were activated to attack the cancer cells on their own. “It was completely unexpected that CD8+ T cells would be mobilized when macrophages engulfed the cancer cells in the presence of CD47-blocking antibodies,” said MD/PhD student Diane Tseng, the lead author of the study. Following engulfment of cancer cells, macrophages activate T cells to mobilize their own immune attack against cancer, she said.

The Stanford group plans to start human clinical trials of the anti-CD47 cancer therapy in 2014. The new research provides hope that the therapy will cause the immune system to wage a two-pronged attack on cancer — through both macrophages and T cells. The approach may also give physicians early indicators of how the treatment is working in patients. “Monitoring T-cell parameters in patients receiving anti-CD47 antibody may help us identify the immunological signatures that tell us whether patients are responding to therapy,” said co-author Jens Volkmer, MD, an instructor at the Stanford Institute for Stem Cell Biology and Regenerative Medicine.

The research revives interest in an aspect of macrophages that has been neglected for decades: their role in presenting antigens to T cells. For many years, researchers have focused on the dendritic cell as the main antigen-presenting cell, and have generally believed that macrophages specialize in degrading antigens rather presenting them. This research shows that macrophages can be effective at antigen presentation and are powerful initiators of the CD8+T cell response.

The fact that T cells become involved in fighting cancer as a result of CD47-blocking antibody therapy could have important clinical implications. The antibody might be used as a personalized cancer vaccine allowing T cells to recognize the unique molecular markers on an individual patient’s cancer. “Because T cells are sensitized to attack a patient’s particular cancer, the administration of CD47-blocking antibodies in a sense could act as a personalized vaccination against that cancer,” Tseng added.

Weissman, who is senior author of the new study, is the director of the Stanford Institute for Stem Cell Biology and Regenerative Medicine and the director of the Stanford Ludwig Center for Cancer Stem Cell Research and Medicine.

Other Stanford investigators involved in the research were senior scientist Stephen Willingham, PhD; postdoctoral scholars John Fathman, PhD, Nathaniel Fernhoff, PhD, Matthew Inlay, PhD, and Masanori Miyanishi, MD, PhD; instructor Jun Seita, MD, PhD; graduate student Kipp Weisskopf, MPhil; and life sciences research associate Humberto Contreras-Trujillo.

The research was supported by the Virginia and D.K. Ludwig Fund for Cancer Research, the Joseph and Laurie Lacob Gynecologic/Ovarian Cancer Fund, the National Institutes of Health (grants R01CA86017, P01CA139490, P30CA124435 and F30CA168059), and the Student Training and Research in Tumor Immunology Program of the Cancer Research Institute.

Christopher Vaughan is communications manager at the Stanford Institute for Stem Cell Biology and Regenerative Medicine.

 

Clinical Investigation of a Humanized Anti-CD47 Antibody in Targeting Cancer Stem Cells in Hematologic Malignancies and Solid Tumors

Funding Type:

Disease Team Therapy Development III

Grant Number: DR3-06965

Investigator(s): Irving Weissman – PI

Institution: Stanford University

Disease Focus:
Cancer
Solid Tumor
Blood Cancer

Most normal tissues are maintained by a small number of stem cells that can both self-renew to maintain stem cell numbers, and also give rise to progenitors that make mature cells. We have shown that normal stem cells can accumulate mutations that cause progenitors to self-renew out of control, forming cancer stem cells (CSC). CSC make tumors composed of cancer cells, which are more sensitive to cancer drugs and radiation than the CSC. As a result, some CSC survive therapy, and grow and spread. We sought to find therapies that include all CSC as targets. We found that all cancers and their CSC protect themselves by expressing a ‘don’t eat me’ signal, called CD47, that prevents the innate immune system macrophages from eating and killing them. We have developed a novel therapy (anti-CD47 blocking antibody) that enables macrophages to eliminate both the CSC and the tumors they produce. This anti-CD47 antibody eliminates human cancer stem cells when patient cancers are grown in mice. At the time of funding of this proposal, we will have fulfilled FDA requirements to take this antibody into clinical trials, showing in animal models that the antibody is safe and well-tolerated, and that we can manufacture it to FDA specifications for administration to humans.

Here, we propose the initial clinical investigation of the anti-CD47 antibody with parallel first-in-human Phase 1 clinical trials in patients with either Acute Myelogenous Leukemia (AML) or separately a diversity of solid tumors, who are no longer candidates for conventional therapies or for whom there are no further standard therapies. The primary objectives of our Phase I clinical trials are to assess the safety and tolerability of anti-CD47 antibody. The trials are designed to determine the maximum tolerated dose and optimal dosing regimen of anti-CD47 antibody given to up to 42 patients with AML and up to 70 patients with solid tumors. While patients will be clinically evaluated for halting of disease progression, such clinical responses are rare in Phase I trials due to the advanced illness and small numbers of patients, and because it is not known how to optimally administer the antibody. Subsequent progression to Phase II clinical trials will involve administration of an optimal dosing regimen to larger numbers of patients. These Phase II trials will be critical for evaluating the ability of anti-CD47 antibody to either delay disease progression or cause clinical responses, including complete remission. In addition to its use as a stand-alone therapy, anti-CD47 antibody has shown promise in preclinical cancer models in combination with approved anti-cancer therapeutics to dramatically eradicate disease. Thus, our future clinical plans include testing anti-CD47 antibody in Phase IB studies with currently approved cancer therapeutics that produce partial responses. Ultimately, we hope anti-CD47 antibody therapy will provide durable clinical responses in the absence of significant toxicity.

New insights into the biology of cancer have provided a potential explanation for the challenge of treating cancer. An increasing number of scientific studies suggest that cancer is initiated and maintained by a small number of cancer stem cells that are relatively resistant to current treatment approaches. Cancer stem cells have the unique properties of continuous propagation, and the ability to give rise to all cell types found in that particular cancer. Such cells are proposed to persist in tumors as a distinct population, and because of their increased ability to survive existing anti-cancer therapies, they regenerate the tumor and cause relapse and metastasis. Cancer stem cells and their progeny produce a cell surface ‘invisibility cloak’ called CD47, a ‘don’t eat me signal’ for cells of the native immune system to counterbalance ‘eat me’ signals which appear during cancer development. Our anti-CD47 antibody counters the ‘cloak’, enabling the patient’s natural immune system to eliminate the cancer stem cells and cancer cells. Our preclinical data provide compelling support that anti-CD47 antibody might be a treatment strategy for many different cancer types, including breast, bladder, colon, ovarian, glioblastoma, leiomyosarcoma, squamous cell carcinoma, multiple myeloma, lymphoma, and acute myelogenous leukemia.

Development of specific therapies that target all cancer stem cells is necessary to achieve improved outcomes, especially for sufferers of metastatic disease. We hope our clinical trials proposed in this grant will indicate that anti-CD47 antibody is a safe and highly effective anti-ancer therapy that offers patients in California and throughout the world the possibility of increased survival and even complete cure.

We have previously developed a new therapeutic candidate, the anti-CD47 humanized antibody, Hu5F9-G4, which demonstrates potent anti-cancer activity in animal models of malignancy. The goal of CIRM DTIII Grant DR3-06965 is to conduct initial phase I clinical trials of this antibody in advanced cancer patients. We originally proposed to conduct two separate Phase I clinical trials: one in solid tumor patients with advanced malignancy (commenced in August 2014), the other in relapsed, refractory AML patients (anticipated to start in September 2015). The primary endpoints for these trials will be to assess safety and tolerability, and additional endpoints include obtaining information about the dosing regimen for subsequent clinical investigations, and initial efficacy assessments.

CD47 is a dominant anti-phagocytosis signal that is expressed on all types of human cancers assessed thus far. It binds to SIRPα, an inhibitory receptor on macrophages, and in so doing, blocks the ability of macrophages to engulf and eliminate cancer cells. Hu5F9-G4 blocks binding of CD47 to SIRPα, and restores the ability of macrophages to engulf or phagocytose cancer cells. In pre-clinical cancer models, treatment with Hu5F9-G4 shrunk tumors, eliminated metastases, and in some cases resulted in long-term protection from cancer recurrence. These results suggest that Hu5F9-G4 leads to elimination of cancer stem cells in addition to differentiated cancer cells.

We have developed Hu5F9-G4 for human clinical trials by demonstrating safety and tolerability in pre-clinical toxicology studies. These studies also indicated that we can achieve serum levels associated with potent efficacy in pre-clinical models. The regulatory agencies (FDA in the U.S., and MHRA in the U.K.) reviewed the large package of pre-clinical data describing Hu5F9-G4, and approved our requests to commence separate Phase I clinical trials in solid tumor and AML patients. The solid tumor trial commenced at Stanford in August 2014 and has been designed to assess patients in separate groups, or cohorts, treated with increasing doses of Hu5F9-G4. The trial is ongoing as primary endpoints have not been met. The acute myeloid leukemia trial has been given regulatory approval in the U.K., and will start enrolling patients in September 2015. In summary, during the last year, the Hu5F9-G4 clinical trials have made substantial progress and all milestones have been met.

Stem Cell Research: Promise and Progress

Hans Clevers: “Every day new research is showing us that many types of cancers are fed by tumour stem cells”

http://www.irbbarcelona.org/en/news/hans-clevers-every-day-new-research-is-showing-us-that-many-types-of-cancers-are-fed-by-tumour

The biggest challenge in designing new cancer therapies lies in successfully identifying and targeting tumour stem cells, which are responsible for the regrowth of the tumour.

The Barcelona BioMed Conference on “Normal and Tumour Stem Cells”, aims to analyze the function of stem cells in cancer. The conference, which begins today and runs until November 14 at the Institut d’Estudis Catalans, is co-organized by colon cancer research experts Eduard Batlle (IRB Barcelona) andHans Clevers (Hubrecht Institute, the Netherlands), with the support of the BBVA Foundation. During the three-day event, 21 world experts in the field will meet with a further 130 participants to share their latest research findings on tumour stem cells.

“In 2007 we held the first Barcelona BioMed Conference on this topic. At the time there was only very preliminary data on the relationship between stem cells and cancer. Five years on, many convincing data have emerged to indicate that the majority of tumours are indeed fed by tumour stem cells,” explains Hans Clevers, the scientist who first identified stem cells in the intestine and who today is one of the world leaders in research on normal stem cells and their potential for regenerative therapy.

A number of important studies have demonstrated that at the heart of cancers of the breast, colon, skin, brain, lung and leukemias lie a small group of malignant cells that have retained the properties of the stem cell that gave rise to the cancers in the first place. It is these cells that allow the tumour to grow and can regenerate it. The efforts of many research groups worldwide now focusses on unraveling this process, identifying the specific genes that allow it to occur, and finding ways to detect and eliminate these malignant stem cells.

Stem cells and the origin of tumours

One of the principal characteristics of stem cells is that they are able to copy themselves indefinitely, giving rise to one stem cell and one specialized cell. This capacity for unlimited replication ensures the constant renewal of healthy tissues, which is fundamental for survival and is the basis of regenerative medicine. When the stem cells undergo cancerous mutations or when normal tumour cells acquire stem cell properties, however, this can lead to the formation of tumours.

“This conference gives us a valuable opportunity to learn about the latest work on the two types of stem cells, normal and tumour, in different tissues. What we have been observing over recent years is that the tumour mimcs the hierarchies that exist in normal tissues. In order to understand the tumour, we need to understand the healthy tissue. Most of the scientists invited to the conference are working on both aspects,” explains Batlle. The list of speakers includes pioneers in the field, such as Irving L. Weissman, director of the Institute for Stem Cell Biology & Regenerative Medicine in Stanford, California. Weissman, known as the “father of haematopoiesis”, first identified stem cells in the blood and determined how they give rise to the different types of blood cells, making major contributions to our understanding of leukemias and other ‘liquid’ tumours.

Stem cells and metastasis

In addition to being at the root of the tumour and allowing it to grow, stem cells may also cause metastasis. In order for metastasis to occur, cells from the original tumour must escape into the blood stream and invade new organs to seed new tumours there. “Only cells with stem cell properties are able to make this happen, since they are the only type of cell that can generate all the cell types of the tumor,” explains Batlle. But in order to cause metastasis, these cells also need to be able to do other things. “We have discovered that in the case of colon cancer, stem cells must be able to trick the healthy tissue of the organ they have invaded into helping them survive in this hostile environment.” Batlle’s study, to be published tomorrow inCancer Cell, will be presented during the conference. This is the first piece of work to reveal a key role for the tumour microenvironment in fostering the process of metastasis, a discovery which will open doors to similar findings in other types of tumours.

Normal stem cells vs. tumour stem cells

One of the keys in the fight against cancer is the ability to identify tumour stem cells and differentiate them from healthy stem cells. The conference co-organizers maintain that “this is still a central question. We don’t yet know enough about normal stem cells, and technical issues make things difficult. We are making rapid progress, however, and in the next few years we expect to be able to make great strides both in figuring out the similarities and differences in the two types of cells, and in coming up with new strategies to fight the growth and spread of tumours.”

PROFILES OF CONFERENCE CO-ORGANIZERS

EDUARD BATLLE – Group Leader of the Colorectal Cancer Laboratory and Coordinator of the Oncology Programme at IRB Barcelona. ICREA Research Professor (Instituto Catalán para la Investigación y Estudios Avanzados).

Dr. Batlle’s research over the past decade has focused on the characterization of the mechanisms that cause the initiation, progression and metastasis of colon cancer. He has published studies in several high-impact journals such as Cell, Nature, Nature Genetics and Cancer Cell. His achievements include the discovery of the transcription factor Snail in tumour cells and the elucidation of the function of EphB membrane receptors in colorrectal cancer. During the Barcelona BioMed Conference, Dr. Batlle will present the results of a study to be published in Cancer Cell on a process indispensable for colon cancer metastasis.

Among his recognitions, Batlle has received the Banc Sabadell Prize for Biomedical Research (2010) and the “Debiopharm Life Sciences Award for Outstanding Research in Oncology” given by the Ecole Polytechnique Fédérale de Lausanne in Switzerland (2006). He is the recipient of an ERC Starting Grant awarded by the European Research Council in 2007.

 

HANS CLEVERS – Group leader at the Hubrecht Institute (director 2002-2012 ) and President of the Royal Netherlands Academy of Arts and Sciences. Dr. Clevers was the first scientist to identify intestinal stem cells and remains one of the leading researchers in this field. His discoveries have had significant impact in cancer as well as in regenerative therapy with stem cells and in vitro organ culture. Clevers’ work in developmental biology and cancer led him to discover the beta-catenin/Tcf4 transcriptional complex, which causes the majority of colorrectal cancer.

http://apoorvamandavilli.com/wp-content/uploads/2010/10/2010stem-cells-and-cancer.pdf

 

In 1991 Clevers became a professor of immunology at the University Medical Center in Utrecht. Since 2002 he has been a professor of molecular genetics at UMC Utrecht. Also in 2002 he became director of the Hubrecht Institute for Developmental Biology and Stem-Cell Research at the Royal Dutch Academy of Sciences, where until May 2012 he led the WNT Signaling and Cancer research group and was project leader of the Netherlands Proteomics Centre and Cancer Genomics Centre. Clevers discovered similarities between the normal renewal of intestinal tissue and the onset of colon cancer. In 2007 he received a grant of two million euros from the KWF Cancer Society to study the function of stem cells in the normal intestines and in colon cancer, and in 2008 he received an ERC Advanced Investigator Grant. In March 2012, Clevers, who since 2000 had been a member of the Royal Netherlands Academy of Arts and Sciences, was elected its president, a position he assumed on June 1 of that year, succeeding Robbert Dijkgraaf. In connection with his election to this position, he resigned from the Hubrecht Institute and began to carry out research two days a week at the UMC-U.[4][5][6][7][9]

Asked in a 2008 interview what had been the highlights of his research up to that point, Clevers said “there would probably be three. There was a first one, when I just started my lab, within the first few months we cloned the gene that they call TCF1, t-cell factor 1, I used to be a t-cell embryologist when we first started out. And that paper was published in EMBO in ’91, first author. So in that paper we described cloning of this vector, which at that time maybe on the world scale was not great but for my own lab to clone this gene was my first thing I ever did alone. This gene then in ’96 we found to be the crucial missing component of what’s called the Wnt signaling pathway, and this [was] generally seen as a major breakthrough we had. There were papers in ’96 and ’97 in Cell, and we had two papers in Science in the same two years.”

Clevers and his team thus showed that “there is that this TCF transcription factor, there is a small family of them, they occur in every animal on the planet, they are the end point of the signal transcription cascade, and they control virtually every decision in a developing animal. When we realized this we started changing our model systems, we used to work on lymphocytes, and we changed it, first to frogs and flies, drosophila, where the Wnt pathway had been studied by many other people that way we could use assays of those people. We then realized that in mammals Wnt signaling…was not only important in embryos but also crucial in adults, which is novel. And we switched to the gut, we found that one of our knockouts, the TCF4 knockout, one of the four members of that family had no stem cells in the gut. And this is the first link in the literature, this was also a ’97 paper in Nature Genetics, between Wnt signaling and stem cells in adults. And in that same year we found that colon cancer comes about by the disregulation of TCF4, and those two phenomena are really linked. So stem cells need TCF4, cancers disregulate TCF4 by mutating a gene upstream in that pathway called APC.”

After this Clevers’s team “continued to work on the intestine and on the physiology of the intestine, which was essentially an unstudied field, much to my surprise. May I emphasize, there are thousands of very competent embryologists, and they work on tiny details, and they fight over the smallest details, are extremely competent. In this intestinal field there are thousands of gastroentromologists that study cancer or colitis or Crohn’s Disease, but there are very few, if any, labs studying normal tissue, which is amazing because that is a tissue that we use every five days. It’s the most rapidly proliferating tissue in a normal body. So my lab actually build up a lot of mouse models and we learn a lot about how that’s being done, and then finally…last year we finally identified the stem cells in the gut. And we now can purify them in large numbers and study their characteristics.”[4]

A recent posting at the website of the Royal Netherlands Academy of Arts and Sciences provides a capsule summary of Clevers’s research to date: “His research deals with the intestine, in both its healthy and diseased state. He has discovered that there are numerous similarities between the normal process whereby intestinal tissue is renewed and the development of intestinal cancer. Improved understanding of these processes is crucial to developing new ways of treating cancer. Hans Clevers has described the molecular signalling pathways that are disrupted by cancer and has identified a protein that is specific to stem cells in the intestine. He has then been able to grow ‘mini-intestines’ from individual stem cells. These are the first steps on the road to regenerative medicine, in this case the regeneration of intestinal tissue.”[7]

Q&A: Hans Clevers

Eric Bender

Nature 521, S15 (14 May 2015) http://dx.doi.org://10.1038/521S15a

n 2009, Hans Clevers and Toshiro Sato (then a postdoc in Clevers’ lab) demonstrated a powerful new model to study development and disease: a three-dimensional ‘organoid’ derived from adult stem cells that replicates the structure of cells lining the intestine. More than 100 labs worldwide are now working with different types of organoid to study cancer and other diseases. Clevers, at the Hubrecht Institute in Utrecht, the Netherlands, discusses the potential of this approach.

Why might it be better to screen drugs in organoids rather than in cell lines?

We don’t currently understand why certain tumours are sensitive or resistant to particular drugs. With targeted therapies, you can make a prediction, but for classical chemotherapy drugs, such as cisplatin or 5-fluorouracil, it is totally unpredictable which tumours will respond. Tumours can be sequenced in great detail, but drugs against them cannot be tested effectively other than in clinical trials. Organoids are a very good genetic representation of the tumour, so they let us bridge the gap between deep-sequencing efforts and patient outcomes.

How do you see organoids contributing to the study of colorectal cancer?

We are collaborating with groups at the Broad Institute in Cambridge, Massachusetts, and the Sanger Institute in Hinxton, UK, to build a biobank of organoids from 20 or so people with colon cancer. We have organoids of the cancer and of normal cells from individual patients, as well as sequences of their protein-coding genes. We have established the non-profit Hubrecht Organoid Technology (HUB) to expand our organoid biobanks. The HUB shares these biobanks with academic groups around the world, and now works with about 15 companies on drug-development programmes. We can culture tumours from almost every person with colon cancer, sequence them and test them against drugs. Additionally, we can use research techniques that have been developed for cell lines, such as genetic tools, fluorescence-activated cell sorting and microarrays.

Is this research moving towards clinical trials?

Yes, my group and the HUB are collaborating with Emile Voest at the Netherlands Cancer Institute in Amsterdam on an observational trial. We already have some organoid models from people with colon cancer who receive chemotherapy. The organoids are screened against a panel of common colon-cancer drugs. The patients will be treated the same way the oncologists would normally treat them, but we’ll see if we could have predicted the response from our organoids. We’re also starting another trial in which we will enrol advanced-colon-cancer patients, for whom there is no standard treatment. We will make organoids, test drug sensitivity and resistance, and then advise the oncologists as to what drug to use for that particular patient. We will be looking at multiple drugs, so we need large numbers of patients — that’s the only way we will be able to produce enough data to help us match drugs to tumour types.

To benefit individual patients, won’t you need to test the drugs very quickly?

Yes — and that’s really where we want to take this technology. When you have pneumonia, your bacterial cultures are tested and you get answers in three days. With this technology, we can tell the oncologist the best odds for a combination of therapeutics, maybe not in three days, but in several weeks. We have an organoid-based test in cystic fibrosis that gives us a result in about two weeks.

How does the organoid approach differ from patient-derived xenografts, in which patients’ tumours are transplanted into immune-suppressed mice for testing drugs?

It’s the same principle — you get a functional readout of the patient’s tumour. But organoids can be tested against an unlimited amount of compounds and combinations. Furthermore, in contrast to xenografts, organoids can be established from almost all patients.

What are some of the next steps in your cancer research?

Organoids model the key component of the tumour but they lack some important elements. We want to combine organoids with other elements to make more-complete tools. For instance, we would like to introduce the immune system so that we can study the effects of the fantastic new immunotherapy drugs. We think that we can build it up in a reductionist way — take lymphocytes isolated from a tumour, bring these together with cancer organoids derived from the same tumour and watch what happens. And maybe we can also put microorganisms in these organoids. For example, we could add Helicobacter, a major cause of stomach cancer, to stomach organoids.

Can organoids also help to test drug combinations?

Yes, tumours are genetically heterogeneous, and there can be vast differences in drug sensitivity between clones for the same tumour. We can possibly advance sequence-based therapy by testing millions of drug combinations in organoids.

Single Lgr5 stem cells build crypt–villus structures in vitro without a mesenchymal niche

Toshiro Sato1, Robert G. Vries1, Hugo J. Snippert1, Marc van de Wetering1, Nick Barker1, Daniel E. Stange1, Johan H. van Es1, Arie Abo2, Pekka Kujala3, Peter J. Peters3 & Hans Clevers1
Nature 459, 262-265 (14 May 2009) |   http://dx.doi.org:/10.1038/nature07935    Received 16 July 2008; Accepted 24 February 2009

The intestinal epithelium is the most rapidly self-renewing tissue in adult mammals. We have recently demonstrated the presence of about six cycling Lgr5+ stem cells at the bottoms of small-intestinal crypts1. Here we describe the establishment of long-term culture conditions under which single crypts undergo multiple crypt fission events, while simultanously generating villus-like epithelial domains in which all differentiated cell types are present. Single sorted Lgr5+ stem cells can also initiate these crypt–villus organoids. Tracing experiments indicate that the Lgr5+ stem-cell hierarchy is maintained in organoids. We conclude that intestinal crypt–villus units are self-organizing structures, which can be built from a single stem cell in the absence of a non-epithelial cellular niche.

  • A Model for Life
Dis. Model. Mech. September 2013, doi: 10.1242/dmm.013367 vol. 6 no. 5 1053-1056

A gutsy approach to stem cells and signalling: an interview with Hans Clevers

Hans Clevers, Professor of Molecular Genetics at Utrecht University, began his career in immunology and developmental biology, but a shift towards intestinal research in the late 1990s led to his group’s pioneering discovery that Lgr5 is a marker of tissue stem cells – a finding that paved the way for a cascade of key insights into the molecular signalling pathways that are dysregulated in cancer. Interviewed here by Ross Cagan, Editor-in-Chief of Disease Models & Mechanisms, Hans recalls the mentors and discoveries that motivated his transition from basic to applied science, discusses his style of lab management and mentorship, and highlights the potential of organoid-based therapy for personalised medicine.

Johannes (Hans) Clevers was born in 1957 in Eindhoven, home to Philips Electronics, in the south of The Netherlands. From a young age he showed enthusiasm and a natural talent for science, and as an undergraduate became fascinated with molecular biology. He obtained his PhD in immunology from Utrecht University during the mid-1980s, and simultaneously studied medicine. Making the pivotal decision to move back into the lab after completing his clinical training, he undertook postdoctoral research in Cox Terhorst’s lab at the Dana-Farber Cancer Institute at Harvard University. He then returned to Utrecht to set up his own lab, and was a Professor of Immunology at the university between 1991 and 2002. From 2002 to 2012 he was Director of the nearby Hubrecht Institute for Stem Cell Research. During this time, Hans moved gradually into the gastroenterology field, and made groundbreaking discoveries regarding the role of Wnt signalling in stem cells and colon cancer. His unique contributions to cancer, stem cell research and regenerative medicine have been recognised in the form of numerous awards, and in 2013 he was one of the eleven winners of a $3 million award from the Breakthrough Prize in Life Sciences Foundation. Currently, he is Professor of Molecular Genetics at Utrecht University, and is also President of the Royal Netherlands Academy of Arts and Sciences (KNAW). Hans has also been involved in setting up several biotechnology companies.

Before we get to your background, I want to congratulate you on being, unsurprisingly, one of the Breakthrough Prize award winners. You have a long list of prizes now – is it something you’ve gotten used to?

This last one was unusual for me – prior to the Breakthrough award I had only ever received one American prize and that was in gastroenterology. To be the only researcher in Europe awarded, and to see my name on the list together with people like Robert Weinberg and Bert Vogelstein, who were the big shots when I was a postdoc, was a truly great honour. I went to the ceremony for the physics prize in Geneva, and it was like being at the Oscars – very surreal, as a scientist.

The first thing I did when I found out about my award was to invite the current and previous members of my lab to a huge party in Amsterdam, which will take place in September [2013]. There will be around 100 attendees – most of which are still in science. There will be good food and drink, stand-up comedy, and a small symposium.

Taking a step back into your past, why did you choose a career in science and medicine?

My high school system was very geared towards languages. I started learning biology at university in 1975 at the age of 18, and I was disappointed. Molecular biology was being developed in England, Switzerland and the US, but in Dutch universities there was no legal framework to do this, and so the courses – where available – focused only on technical details. Biology in general lacked charisma. At the time, my friends and brothers were junior medics, and as I had an interest in medicine I decided to take it on in addition to biology. I ended up spending a year in Nairobi and half a year at NIH for my biology rotations, and essentially I never went to any lectures (although this is something I never tell my students!). Anyway, I really started getting sucked into the clinical training, and found that working in a clinical environment is much more sociable than being in a lab. You’re part of a big organisation and there are lots of people to talk to, whereas in the lab there are only a few people, and small issues – such as somebody not cleaning up – can really cause friction. After medical school, I was picked, mainly because of my research background, for a training position in paediatrics. They suggested that I should start work for a PhD, so I went back into the lab. That’s when I realised that, despite the social attractiveness of working in a hospital, I was much more of a scientist than a doctor. I got my PhD – together with four published papers – in just 1 year. However, it was during my first postdoc position in Boston that I think I was really exposed to science for the first time. It was tough, but I knew I’d made the right decision.

Are there particular mentors who influenced your decision to choose the lab over clinics, and shaped your career moves?

When I received the Heineken Prize from the Royal Netherlands Academy of Arts and Sciences in 2012, I had to think deeply about my mentors and realised that there were two that I had almost forgotten. The first was my high school chemistry teacher, who sold laboratory chemicals to students from his home, during the evenings (in a well-regulated way). I had built a small lab in the attic of my parents’ house and I really had fun mixing things together and doing all the experiments that are possible to do at home. Because of this chemistry teacher, I learned the joy of being in a lab.

The second crucial mentor was my thesis advisor, who didn’t supervise me very much but did give me key advice that has stayed with me until now. He taught me that it’s important to trust everybody you work with, at least until they show you that they can’t be trusted. I emphasize this in my own lab – I encourage my students and postdocs to be open and transparent and to discuss their work. Some scientists are intuitively secretive and paranoid – cultural differences perhaps play a part in this. In my view, only when someone damages your trust can you justify being paranoid, and until then it is important to share information.

“…it’s important to trust everybody you work with, at least until they show you that they can’t be trusted”

There are many ways to run a lab; for example, you can micro-manage it or you can focus on the big picture and step back from the day-to-day issues. What is your style of running a lab?

When I first became a PI, I really liked doing experimental work. Even after 5 years as a postdoc, I enjoyed doing minipreps! As a consequence, I really micro-managed the few lab members I had, and I’m sure they were ultimately happy to get away from me. But when the lab grew a little bigger and I became Head of Department, it took me away from the lab much of the time. Nowadays, I informally talk with my lab colleagues as much as I can, preferably at the bench. As we speak, I know that there is someone in my group who will find out the results of a 3-month effort, today. I always insist on looking at the raw data, never the digested, analysed data. It could be 5 minutes or 2 hours, but when I’m needed in the lab I will always try to make time for it and be part of the troubleshooting process. When you can no longer troubleshoot in your own lab, you’re lost.

Well clearly success builds on success – some impressive scientists have come out of your lab. Do you encourage all of your group members to pursue academic positions?

I’ve had many ‘super postdocs’ in my lab but some of these individuals would not be happy as PIs. It’s not about capability, but about wanting to deal with the paperwork, the responsibility and the decision-making that come with being a PI. Such individuals can make a valuable contribution to a lab, given their years of experience, as well as acting as great mentors and role models for the newer group members. When, having gained experience in the pharmaceutical industry, Nick Barker re-joined my group in 2006 as Senior Staff Scientist, we spent 6–7 years looking for stem cell markers, and then broke open the field by identifying Lgr5 as a marker of cancer stem cell populations. Nick has now set up his own group in Singapore, but I have had several other very talented experimentalists in my lab for many years. Overall, I think that intermediate positions are fantastic for successful postdocs who might end up unhappy as PIs.

How did you get involved with intestinal stem cell research? You didn’t start in this field but somehow ended up there.

As an undergraduate student, I did a brief rotation project on T cells. This led to a PhD and postdoc focused on T cells. I learned molecular biology, which inspired me to clone a T-lymphocyte transcription factor, TCF-1, when I subsequently set up my own lab in Holland. We (Marc van der Wetering and I) cloned TCF-1 within a few months and showed that it binds DNA; but, despite trying all kinds of functional assays, we couldn’t show that it regulates transcription. It took 6 or 7 years to figure out that β-catenin, a signal transducer in the Wnt signalling pathway, was needed. We heard that Walter Birchmeier had made a complementary discovery in Berlin, and our papers came out at the same time.

Around that time, I was Clinical Professor in Immunology at Utrecht, and I started studying TCFs in mice, frogs, flies and worms. We soon established that TCFs are always the endpoint of the Wnt pathway. In 1996–1997, we knocked out TCF-4 in mice and, remarkably, observed a gut phenotype – the mice had no crypts. Simultaneously, we realised that the pathway is overactivated in colon cancer. That’s when I decided to move into studying the gut. It wasn’t easy as an immunologist, but I gradually got to know the gastroenterology field. At the time, this field was dominated by clinical research, and in fact our work didn’t really become known to gastroenterologists until around 3–4 years ago. They were totally unaware that mice could give clues about human disease, which surprised me, as in haematology and immunology, there is a good balance between basic and clinical science. There are other clinically well-developed fields, such as prostate and lung cancer research, that could really benefit from a stronger basic approach.

A key discovery for you was that Lgr5 is a marker of stem cells. When did you realise the implications of this discovery?

There were two ‘eureka’ moments with the stem cell story. The dogma at the time was the ‘+4’ stem cell model, which was pioneered by Chris Potten, who recently passed away. I tried to provide experimental support for this model, together with Nick Barker, but it never really went anywhere. Having realised that β-catenin and TCFs controlled crypts in the gut and cancer, we set out to determine the genetic programme controlled by this pathway. At the time (1997), there was no technology to do this properly, but in 2000 we performed one of the first microarrays with Pat Brown. Our array looked at expression in a colon cancer cell line. The array contained only two samples – plus or minus the Wnt pathway – but it opened the field for us by providing a list of markers to investigate further. This was the first, key step. From the list of markers, we picked a few that we thought were marking +4 cells, but these led us nowhere. Eventually, based on its unique expression pattern, we came up with Lgr5. We made numerous mouse strains, including Lgr5-GFP tagged mice. The moment we saw tiny cells lighting up under the microscope, I started writing our next ten big papers in my head. It was a remarkable moment – the cells exist, and we could visualise them using these mice.

And why exactly is Lgr5 so important, both from a basic and an applied standpoint?

Lgr5 is an exquisite protein. We and several other labs have shown that it is a marker for stem cells in many tissues. Originally, we saw it only in spontaneously dividing tissues, but we’ve recently found that it also appears in organs that have undergone damage. Lgr5 is unique in that it – on its own – it specifically marks homogenous populations of stem cells but not their progenitors, unlike most other markers. We now know that this is because it is a cell surface receptor protein in the Wnt pathway, and only stem cells require Wnts. In the gut, the stem cells are particularly active – in mice, they divide every day for 2.5 years, so they go through a thousand cell divisions.

Discovering Lgr5 led to another eureka moment: the generation of long-term culture systems that maintain crypt physiology. A Japanese gastroenterologist who I invited to my lab, Toshiro Sato, was the first to set up the right culture conditions, and now multiple labs are creating these systems, which are called organoids or ‘mini-guts’. Once the system was up and running, Toshiro showed that Paneth cells provide the niche for stem cells at crypt bottoms, and that stem cells produce their own daughters which then produce growth factors. With his former Japanese lab, we showed that normal tissue can be generated from a single stem cell, and it can survive in a mouse for as long as you want. Based on this finding, our lab evolved and now we’re culturing prostate, liver, pancreas, kidney, lung and breast tissue, all for prolonged periods of time, all from humans. There are no changes in chromosomal structure in the cultured cells, and deep sequencing reveals very few mutations. The next step will be to take single cells, genetically modify them like we do with embryonic stem cells, pick a safe clone, expand it and use it for therapy, particularly transplantation.

Do you think we will be able to take organoid-based therapy to the personalised level? Colorectal cancer, for example, only has a 3% success rate in clinical trials. Are organoids going to provide the answer?

We’re finalising a pilot sequencing study now involving 20 patients with normal crypts and colon cancer. With the wild-type and colon cancer organoids, we can potentially predict patient outcome and response to drugs. In the future, we hope to rapidly build large, living biobanks for other cancers, too. In line with this, we’re building up a ‘Stand Up 2 Cancer’ dream team involving several American labs and the Sanger Institute, with the aim of taking the organoid approach to the next level in cancer therapy. Sanger has robotised screening set-ups that allow thousands of compounds to be screened across hundreds of cell lines. We can now do this with patient-derived organoids. From these tests we could establish new effective drug combinations, and we could link genetics to function to help design smarter trials. The great thing about organoids is that they contain only epithelium – there is no immune system, no blood system, only the diseased tissue, making it a very clean system.

We’ve also recently collaborated with clinicians on a cystic fibrosis project. We can predict using cystic fibrosis ‘mini-guts’ that certain drugs that are currently in trials will work for one patient and not for another, and that certain drug combinations work better than others. From biopsy to drug response, it takes only 10 days. Industry is now very interested in using this assay to pre-screen and design trials.

“The great thing about organoids is that they contain only epithelium – there is no immune system, no blood system, only the diseased tissue, making it a very clean system”

In the past, you’ve suggested that classic hypothesis-driven science isn’t the right way to do science. Could you say a little bit more about this?

Now that I’m a bit older I’m more interested in how the process of science works. I always ask my colleagues: how do you run the lab and how do you make discoveries? In my lab, I try to establish a reproducible, quantitative system, like GFP mice and arrays. Then, I throw something at the system and look, without formulating a hypothesis. This is difficult because our brains like to produce causal relationships, even though these are often wrong. I’m constantly telling my group members that they should keep their minds open and make observations without assuming that they know what’s going on. In molecular biology, we can go anywhere we want and there are billions of effects to discover. You cannot do this in a hypothesis-driven way because you’re essentially retracing evolution. There are many solutions to a particular problem but evolution picked one – it’s very arrogant to think we can reconstruct this in our minds.

Some of my most elegant hypotheses have fallen by the wayside. The importance of establishing formal rules for innovation is a discussion worth having in biology. I understand that you have embraced movies to explain scientific concepts. What’s the story behind this?

I was inspired by Leonard Zon – I came across one of his movies about 8 years ago. I realised it’s much easier to convey messages visually than in words so I started working with a small company in Holland to produce science movies. The lab provides the idea and the images, and the company writes the script. We end up going back and forth a few times to make the message as accurate as possible, and it really shows us as scientists how ambiguous language can be. Often, feedback from the company sends us back into the lab to find out something we hadn’t looked into, for example how fast do the cells move, how many cells are there? Gradually, the movie comes together. Nowadays, I typically use the movies in my talks to explain a problem, and I’ve found that it’s much more effective to show the movie before explaining the experiments. People understand the experiments much better that way, and listen effortlessly. Now, whenever we have a story to write up I try to turn it into a 30-second movie before putting pen to paper. This really forces us to think about the core of the paper.

“In molecular biology, we can go anywhere we want and there are billions of effects to discover…There are many solutions to a particular problem but evolution picked one – it’s very arrogant to think we can reconstruct this in our minds”

In your view, is being a scientist a good career choice? What advice would you give to a young scientist thinking about this career?

Science is frustrating because things don’t work 90% of the time: ideas are wrong, experiments fail. You have to have the personality that thrives by those few fantastic moments of success that you have once a year or even once a career. Moving from being a clinician to being a scientist was one of the hardest decisions I ever made. A clinician gets rewards multiple times a day, so if you’re a person who needs that kind of reward and social interaction, then you shouldn’t be a scientist. Luckily there are now many alternative careers, such as pharma, government and teaching, that didn’t exist when I was a young scientist. However, there needs to be a radical change in the way we view these alternative routes. Maybe in the US it’s different, but here, if you step out of the system you are treated like a failure. I tell young scientists that failure comes with ending up as a miserable PI, with no funding and no papers.

PhD students and junior postdocs have to be aware that the people they see at meetings who give the great talks are in the minority – as scientists we have to be ready to do something else at any point during our career. I think the whole system has to realise that every other job can be as interesting as a job in science. That’s not what we always convey to young people – we describe academia as where it’s happening and everything else as dull or uncreative.

If you hadn’t chosen science as a career, what would you have done instead?

I would probably be a novelist. It’s even more competitive than being a scientist, but it’s also creative, so the perfect blend for me.

Read Full Post »

Ralph Brinster, ‘Father of Transgenesis’

 

Larry H. Bernstein, MD, FCAP, Curator
Leaders in Pharmaceutical Innovation
Series E. 2; 7.7

A candid conversation with veterinarian Ralph Brinster, ‘Father of Transgenesis’

For the past five decades, Ralph Brinster, VMD, PhD, Richard King Mellon Professor of Reproductive Physiology at the University of Pennsylvania’s School of Veterinary Medicine, has been working on furthering our understanding of the mammalian germ line. During that time, he helped forge the path that today’s biologists—including those working on transgenics and stem cell research—are following.

Brinster is often referred to as the “Father of Transgenesis,” the study of the experimental transfer of individual genes or DNA into the germ line of an animal, which then transmits the genetic alteration to offspring and successive generations. Many may remember the famous Nature cover story of 1982 that showed a normal-sized white mouse being dwarfed by his giant mouse sibling. That was Brinster’s work, along with his colleague Richard Palmiter of the University of Washington. Through painstaking experimentation, during which they inserted new genes into the germ line, Brinster and Palmiter demonstrated, in a dramatic and unequivocal manner, the true promise of transgenics. The “giant mouse” research was reported on the front page of most major newspapers around the globe.

For his groundbreaking work, Brinster was named one of seven scientists to win the National Medal of Science in 2010, a highly prestigious award that is given annually by the president of the United States. Brinster is the first veterinarian to be so honored and only the eighth from the University of Pennsylvania in the 50-year history of the medal.

 

Penn researcher shares insights of 50 years studying mammalian germ line.

source-image
Nov 01, 2012

For the past five decades, Ralph Brinster, VMD, PhD, Richard King Mellon Professor of Reproductive Physiology at the University of Pennsylvania’s School of Veterinary Medicine, has been working on furthering our understanding of the mammalian germ line. During that time, he helped forge the path that today’s biologists—including those working on transgenics and stem cell research—are following.


Ralph Brinster, VMD, PhD

Brinster was recently recognized for his 50 years of dedicated service as a faculty member in the Department of Animal Biology. The university and school held a two-day symposium in his honor, and research scientists from around the world participated. Michael Brown, a Nobel Laureate in Physiology or Medicine, presented the keynote lecture at the symposium.Brinster is often referred to as the “Father of Transgenesis,” the study of the experimental transfer of individual genes or DNA into the germ line of an animal, which then transmits the genetic alteration to offspring and successive generations. Many may remember the famous Nature cover story of 1982 that showed a normal-sized white mouse being dwarfed by his giant mouse sibling. That was Brinster’s work, along with his colleague Richard Palmiter of the University of Washington. Through painstaking experimentation, during which they inserted new genes into the germ line, Brinster and Palmiter demonstrated, in a dramatic and unequivocal manner, the true promise of transgenics. The “giant mouse” research was reported on the front page of most major newspapers around the globe.


An exceptional honor: Brinster is the only veterinarian to receive the National Medal of Science, presented last year by President Obama.

For his groundbreaking work, Brinster was named one of seven scientists to win the National Medal of Science in 2010, a highly prestigious award that is given annually by the president of the United States. Brinster is the first veterinarian to be so honored and only the eighth from the University of Pennsylvania in the 50-year history of the medal. He received his medal in October 2011 from President Obama himself during a ceremony held at the White House. In August of this year, the Theriogenology Foundation presented the 2012 Career Excellence in Theriogenology Award for his contributions to the field of reproductive veterinary medicine.DVM Newsmagazine recently caught up with Dr. Brinster in his office at the University of Pennsylvania School of Veterinary Medicine in Philadelphia.

DVM: How did you decide to work on the mammalian germ line?

Brinster: I grew up on a farm where we raised purebred animals. Genetics was fundamental on the farm in terms of breeding success and the potential profit gained from that endeavor. I learned at an early age that you must improve animal germ lines to succeed.

Three separate stages are important to consider in studying germ lines: Pedigree tells you what you think you should get. Performance is what you actually get. And progeny is what can be passed on to offspring. For example, a horse can have a great pedigree but never win a race, or be a great racer but never sire winners. So in the end you depend on progeny to ultimately prove the power, quality and characteristics of the germ line of an animal.

DVM: What excited you about work with germ cells?

Brinster: They are the only cells that biology really cares about. What is important to the biology of the species is actually the DNA in the gametes or germ cells. Therefore, on the basis of my background on the farm, my animal science training at Rutgers and my education in veterinary medicine, I felt they were the most important cells in any animal.

DVM: You started using stem cells in the 1970s, demonstrating that non-embryo-injected cells become part of the developing mouse. Why did you start that research?

Brinster: I believed that the introduction of stem cells early in development would allow them to take part in maturation of tissues. These are the studies that resulted in the teratocarcinoma cells being injected into blastocysts.

While we were trying to explore techniques to get better teratocarcinoma cells or similar cells to enter the germ line, I began developing techniques that might allow the introduction of genes directly into fertilized eggs. At first we worked with chromosomes, but they were difficult to handle. Fortunately, other scientists were developing recombinant DNA techniques, which made pure populations of specific genes available.

It was difficult to obtain funding for these studies because the probability of success appeared very low. To obtain funding for this type of study, injecting eggs with nucleic acids, I began studies putting messages for proteins into eggs to study the mechanisms by which the egg produced the specific proteins. One of the proteins I planned to study was ova albumin, and Richard Palmiter had done excellent studies with this protein. I contacted him to obtain the messenger RNA. However, he had stopped working on ova albumin and was working with metallothionein genes. Although I was already working with several molecular biologists and trying to introduce new genes into eggs, I was interested in other possible genes, but the metallothionein gene was present in mice, and there was no good assay to distinguish it from the endogenous protein.

However, I used the ova albumin messenger RNA for my protein studies, and later described these studies to Richard. At that time, he told me he was fusing the metallothionein promoter to the herpes simplex virus thymidine kinase gene, for which I had an assay. So I asked Richard to send me the fusion gene, and we began collaborating on microinjection of the gene into eggs. In the spring of 1981, we obtained transgenic mice expressing the metallothionein thymidine kinase fusion gene, and Richard and I then published the results of these studies in Cell several months later.

DVM: Tell us about the giant-mouse experiment of the early 1980s.

Brinster: I was very interested in making changes in the biology of the mouse using the transgenic technology, and one of the changes I envisioned was a correction of genetic defects. Richard and I discussed this project, which eventually led to the use of the metallothionein-growth hormone fusion gene in an attempt to correct the genetic defect in the “little” mice. The experiment was a success and was published in Nature 30 years ago this December. The effect was dramatic, and the experiment catalyzed interest in the transgenic technique among scientists as well as the general public. A picture of a large mouse next to its normal-sized sibling was published on the cover of Natureand appeared on the front page of most newspapers throughout the world.

DVM: I remember that photo. I was stunned by it and the research it represented. That must have been exciting for you, to get that much recognition for your work.

Brinster: Yes, I was surprised. The phone did not stop ringing for the entire day the picture appeared on the Nature cover. It brought a great deal of recognition to the scientific area and to our work, as well as the experiments of others working and contributing in this area.

DVM: What are your thoughts on the state of veterinary stem cell research today?

Brinster: It is critically important to understand how tissues develop, both normally and abnormally. I am not surprised that researchers are now studying the stem cell basis of cancer. I felt in the 1970s, when I was studying the teratocarcinoma cell, that all cancers must have a stem cell basis. It seemed logical that the cancer, like any self-perpetuating tissue, must have a stem cell basis, as well as a differentiation process, which is unregulated in cancer. The study of stem cells, including those of cancer, is an important area of investigation within veterinary medicine. Many veterinary schools are currently involved in innovative stem cell research.

DVM: What are you working on now?

Brinster: I am still studying the mammalian germ line and germ line cells. One area of investigation is related to human spermatogonial stem cells. About 80 percent of children with cancer are cured, but almost one-third of the prepubertal boys that recover become infertile or severely subfertile, which is a serious quality-of-life issue. About one in 5,000 reproductive-age men currently are cancer survivors with seriously impaired fertility. One method to alleviate this problem is to obtain a testicular biopsy before cancer treatment begins, and then use the stem cells from this cryopreserved biopsy at a later time to correct infertility. To be successful one must be able to expand the number of stem cells in the biopsy. Therefore, one of the main areas on which we have been working, in collaboration with researchers from the Children’s Hospital of Philadelphia, is the cultivation of human spermatogonial stem cells. This has proven to be very difficult, but I am sure we will be successful.

DVM: You are the only veterinarian to ever receive the National Medal of Science. What was that day like for you, meeting President Obama in the White House?

Brinster: It was extremely rewarding to be recognized by such a distinguished jury as the one that selects National Medal of Science winners. The ceremony itself was exceptional, and winning the Medal of Science brought well-deserved recognition to the School of Veterinary Medicine, my department and Penn.

DVM: What do you think your legacy in the veterinary and the broader scientific community will be?

Brinster: I think I will be recognized for my work on transgenics, in part because it has been tremendously important as a scientific breakthrough. However, many believe that it represents more, because it provides a method by which man can experimentally modify the germ line of species and thus change the “program of life.” This ability is a major change in man’s relationship to other species.

DVM: What changes have you seen in your 50 years teaching in veterinary school?

Brinster: The diversity of opportunities for students in their veterinary education and the many areas in which they can use their training following graduation is now enormous. They can contribute to many aspects of society now, and veterinary medicine has become critical to a wide range of problems. One particular area in which veterinary medicine will be especially important is related to zoonotic diseases. Approximately 70 percent of new infectious diseases affecting humans currently arise from animals, which represent the reservoir. This is just one example of an area in which veterinarians are critically important to societal health.

Donna Loyle, MS, is a freelance writer in Philadelphia who specializes in medicine and veterinary science.

 

If you ask Ralph L. Brinster, VMD, PhD the secret to his success, he will say it is luck. But if you ask anyone else — including colleagues with whom he has worked for more than five decades — they will tell you it is much more than that — it is brilliance and unyielding curiosity. Dr. Brinster, the Richard King Mellon Professor of Reproductive Physiology at Penn Vet, was one of seven scientists to be honored by President Barack Obama in October 2011 with a 2010 National Medal of Science, the highest accolade bestowed by the United States government on scientists and engineers. Since the award was first established 50 years ago, Dr. Brinster is the first veterinarian and the eighth scientist from Penn to win the National Medal of Science. The reason for this highest of honors? Dr. Brinster is often regarded as the father of transgenesis, and it was his research on the manipulation of the mammalian germ line, the cells that give rise to sperm and eggs, for which he was honored. By inserting new genes into the germ line of a developing organism — the process known as transgenesis — researchers can produce animals with selected traits that are indispensible models in understanding life processes and disease. Penn President Amy Gutmann said, “Ralph Brinster is a trailblazer in the field of reproductive biology and genetics whose work has had inestimable influence in science and medicine. His early findings helped usher in the era of transgenic research and represent foundational aspects of techniques used in genetic engineering, in vitro fertilization and cloning. We are extraordinarily proud that he has received the National Medal of Science in recognition of more than five decades of scientific achievement.” Clearly, it took something more than simple luck. The Path to Discovery “I grew up on a small farm in northern New Jersey, and from my experiences there, I became interested in animal development and breeding, including fertility and transmission of genetic characteristics to progeny,” said Dr. Brinster. “Growing up on a farm was a good environment. You work hard and there are no vacations.” That environment and value system paved the way for Dr. Brinster’s long academic career and continued quest for understanding animal development. After earning a bachelor’s degree in animal science from Rutgers University in 1953, Dr. Brinster planned to continue his education, but the Korean War was underway.

Dr. Brinster became a second lieutenant in the United States Air Force and served a year in Korea, after which he finished his military commitment in Texas. Still, he did not lose sight of his intention to attend veterinary school. He started Penn Vet in 1956, putting the GI Bill benefits to good use financing his education. “I was not a great student as an undergraduate; therefore, I was fortunate to be accepted at Penn Vet,” recalled Dr. Brinster. “My intent was to work with large animals, but I became more interested in fertility of animals and germ cell biology; thus, following graduation I began PhD training in physiology at Penn Medicine.” Dr. Brinster earned his PhD in 1964, and made nearimmediate and long-lasting impacts in science.

Dr. Brinster’s first major breakthrough came from research leading to his PhD. It was this research in the early 1960s that led to the development of an effective and reliable system in which to observe and experiment on eggs and embryos outside of the body. By using a culture method that consisted of placing mouse embryos in culture medium under an oil layer, Dr. Brinster created a system that would be adopted by the scientific community almost immediately. The system is still used today – virtually unchanged – as the go-to technique for experiments involving mammalian eggs and embryos, including all transgenic work, embryonic stem cell research, in vitro fertilization in humans, cloning and knockout technology. But creating this system was just a first step for Dr. Brinster. Next he planned to manipulate the germ line and germ cells to further understand their development and regulation. Thinking back to his childhood on the farm and appreciating the need for producing quality livestock, Dr. Brinster said, “I never lost interest in animal breeding and eventually became more and more interested in fertility, specifically the germ line. I wanted to modify the germ line and germ cells to understand how they function.” Using a mouse model, a standard species in the field of genetics because of their short reproductive time of three weeks and their well-defined genetic background, Dr. Brinster in the early 1970s began his work towards transgenesis. By taking stem cells from mouse teratocarcinomas and injecting them into mouse blastocysts, Dr. Brinster was able to demonstrate, through a series of experiments, that the non-embryo injected cells amazingly became part of the developing mouse tissues and were present in the adult.

This series of experiments illustrated that donor cells, which could be cultured in vitro and modified genetically, would become part of the adult mouse. Therefore, such cells could carry genetic change into the mouse and into its germ cells, thus permanently altering the germ line of the animal. “The germ cells are critical cells,” said Dr. Brinster. “They are the only cells in the body that will pass DNA to the next generation.” While he and other scientists continued to develop and perfect this approach with stem cells to alter the germ cells and germ line, Dr. Brinster began to explore and perfect another approach to germ line modification. He initiated these experiments by demonstrating in 1980 that fertilized one-cell mouse eggs could be injected with nucleic acids and survive. He and others then used this approach to introduce new genes into the adult mouse by injecting them into the fertilized egg. He and Richard Palmiter of the University of Washington published a foundation paper in 1981 demonstrating the integration and expression of a transgene in mice. The following year, they published the famous giant mouse experiment, which appeared as the cover story in the journal Nature in 1982 and was reported on the front page of newspapers throughout the world. In this transformational experiment, they demonstrated that the growth hormone transgene produced rapid growth and large size in the mouse, and the results catalyzed interest in transgenesis. A picture of the mice appears in most textbooks as representing the beginning of the transgenic revolution. “When we saw the giant mouse,” said Dr. Brinster, “we were surprised and delighted. The giant mouse experiment was a fantastic experiment. That is the experiment that made everybody, including us, stop and say, ‘This is incredibly powerful.’ That you could enter the germ line and make a change like that. It’s the first time man was able to experimentally modify the genetic code that will make the next individual.” The implications of this success are far-reaching and include the possibility of understanding the origin of animal and human diseases, as well as studying the mechanisms by which a single cell, the fertilized egg, develops into a complex animal.

Dr. Brinster has recently turned his attention to spermatogonial stem cells (SSCs), the foundation stem cells of the male germ line and spermatogenesis. SSCs self-renew and generate daughter cells to differentiate into spermatozoa throughout the entire lifespan of the male. “I started thinking about the male germ line, and I reasoned that if you took cells from a fertile testis and injected them into the seminiferous tubules of an infertile testis, they should be able to restore fertility to the animal,” said Dr. Brinster. Of all the testis cells transplanted, only the spermatogonial stem cells would colonize the testis and be able to regenerate complete spermatogenesis. “It was a simple concept; I am surprised no one did it before.” This transplantation system is now used worldwide to study and experiment on male germ line stem cells and spermatogenesis in all species. Dr. Brinster has used the transplantation system to develop cryopreservation and culture methods for spermatogonial stem cells of rodents and higher species, including primates. These techniques make individual male germ lines and their genetic content biologically immortal for all mammalian species. Clearly, the approaches Dr. Brinster has developed in the male mirror those that he introduced for the female back in the 1960s. They will be useful to preserve and genetically modify the germ lines of farm animals to increase productivity and health.

 

Stephen Williams, PhD, LPBI

Nice story and interview by Penn Vet. It’s good to read about the history, timeline of discovery, and important works that led to breakthroughs in biology.

Don’t forget about the “Mother of Transgenics” Dr. Bea Mintz, a brilliant developmental biologist in the same city of Philadelphia and discoverer of seminal findings in developmental biology. I have a posting which gives more of her bio at

Heroes in Medical Research: Developing Models for Cancer Research

“Heroes in Medical Research: Developing Models for Cancer Research”

 

Richard Palmiter
Professor of Biochemistry, Investigator, HHMI
PhD 1968 Stanford University
AB 1964 Duke University

Honors

  • 2004 Vern Chapman Lecture, 18th International Mouse Genome Meeting
  • 2004 Recipient of Julius Axelrod Medal
  • 1999 Tyner Eminent Scholar, Florida State University, Tallahassee, FL
  • 1999 Wallace Rowe Lecture, American Association of Laboratory Animal Sciences 50th Annual Meeting
  • 1998 Fourteenth von Euler Lecture, Karolinska Institute, Stockholm, Sweden
  • 1998 Second International Fellow of the Garvan Institute, Sydney, Australia
  • 1994 Charles-Leopold Mayer Award, French Academy of Sciences (shared with Dr. R. Brinster)
  • 1989 Distinguished Service Award of US Department of Agriculture.
  • 1988 Elected to National Academy of Sciences
  • 1988 Elected to American Academy of Arts and Sciences
  • 1987 Elected Fellow of American Association for the Advancement of Science
  • 1983 New York Academy of Sciences Award in Biological and Medical Sciences
  • 1982 George Thorn Award, Howard Hughes Medical Institute
  • 1988-1991 Co-Chairman of Four Mouse Molecular Genetics Meetings, Cold Spring Harbor & Heidelberg

Our group uses genetic techniques to study the role of neuromodulators in the development and function of the mammalian nervous system. Most neuromodulators are polypeptides or amino acid derivatives. They are packaged in synaptic vesicles and released into the synaptic cleft upon neuronal stimulation where they modulate the activity of neurons by binding to membrane receptors coupled to G-protein-linked signaling pathways. Our group has been studying the role of the catecholamines, norepinephrine and dopamine, by making mice in which enzymes required for their biosynthesis have been inactivated.Mice that cannot synthesize dopamine develop normally but they become hypoactive and die of starvation a few weeks after birth. Treatment with L-dopa restores dopamine and restores locomotion and feeding and most other behaviors for about 8 hours. Thus, it is possible to study the same mice in either a dopamine replete and dopamine depleted state. Using this model, we have been examining the roles of dopamine in motivation, reward and learning. We also use viral gene therapy strategies to restore dopamine signaling to particular brain regions to ask where dopamine is needed for particular behaviors. We have begun using genetic techniques to manipulate the activity of dopamine neurons. For example, we have removed NMDA receptors from dopamine neurons to reduce excitatory glutamatergic input and discovered that those mice cannot remember where pleasurable events occur. Next, we will be expressing genes into dopamine neurons that will allow pharmacological activation or inactivation of dopamine neuron activity to allow us more directly assess the role of dopamine neurons in various behaviors.

Another area of interest involves the role of hypothalamic neurons that express a neuropeptide called agouti-related protein (AgRP). This small population of neurons is involved in the regulation of appetite and metabolism. We devised a method to selectively kill these neurons and discovered that mice die of starvation. A few days after killing AgRP neurons, the mice neither initiate feeding voluntarily nor swallow much liquid diet even if it is introduced directly into their mouth. Thus, we believe sudden loss of these AgRP neurons disrupts the normal motivational and consummatory systems that control feeding behavior. In addition to AgRP, these neurons make neuropeptide Y and gamma-amino butyric acid (GABA). We have eliminated AgRP and NPY as being critical players in the starvation phenotype and are currently concentrating on the role of GABA.

Publications:

Showing 5 most recent results. [Show All]

  1. Kim HW, Choi WS, Sorscher N, Park HJ, Tronche F, Palmiter RD, Xia Z. Genetic reduction of mitochondrial complex I function does not lead to loss of dopamine neurons in vivo. Neurobiol. Aging 2015 Sep; 36(9):2617-27. [PMID:26070241] [PMCID:PMC4523431]
  2. Denis RG, Joly-Amado A, Webber E, Langlet F, Schaeffer M, Padilla SL, Cansell C, Dehouck B, Castel J, Delbès AS, Martinez S, Lacombe A, Rouch C, Kassis N, Fehrentz JA, Martinez J, Verdié P, Hnasko TS, Palmiter RD, Krashes MJ, Güler AD, Magnan C, Luquet S. Palatability Can Drive Feeding Independent of AgRP Neurons. Cell Metab. 2015 Aug; [PMID:26278050]
  3. Han S, Soleiman MT, Soden ME, Zweifel LS, Palmiter RD. Elucidating an Affective Pain Circuit that Creates a Threat Memory. Cell 2015 Jul; 162(2):363-74. [PMID:26186190] [PMCID:PMC4512641]
  4. Garrett Morgan R, Gibbs JT, Melief EJ, Postupna NO, Sherfield EE, Wilson A, Dirk Keene C, Montine TJ, Palmiter RD, Darvas M. Relative contributions of severe dopaminergic neuron ablation and dopamine depletion to cognitive impairment. Exp. Neurol. 2015 Jun; 271:205-214. [PMID:26079646]
  5. Tong L, Strong MK, Kaur T, Juiz JM, Oesterle EC, Hume C, Warchol ME, Palmiter RD, Rubel EW. Selective deletion of cochlear hair cells causes rapid age-dependent changes in spiral ganglion and cochlear nucleus neurons. J. Neurosci. 2015 May; 35(20):7878-91. [PMID:25995473][PMCID:PMC4438131]

Richard Palmiter uses genetic and viral transduction techniques to discern neural circuits that control mouse behavior. He is particularly interested in neural circuits that control appetite.

 The central nervous system (CNS) integrates environmental sensory information (sight, sound, smell, taste, and touch) with signals from the body (sensory information from internal organs and hormones) to generate appropriate movements. The CNS can learn to associate particular sensory cues with subsequent events to facilitate appropriate responses—either approach or avoidance behaviors. Our laboratory uses genetic manipulations in the mouse to examine the neural circuits (the wiring diagrams) involved in these responses and the signaling molecules (neurotransmitters/neuromodulators) that are used by the neurons in the circuit. The neural circuits that mediate essential behaviors that do not require thought are likely to be hardwired, although still subject to modulation. Complete neural circuits have not been defined for most basic behaviors in mammals. However, genetic and viral tools are being developed that are promoting rapid progress. We are using these techniques to decipher neural circuits that promote or inhibit feeding behavior.

Neurons express agouti-related protein (AgRP) in the arcuate hypothalamus...

Neurons that express agouti-related protein in the arcuate hypothalamus…

Neurons in an area of the brain called the arcuate region of the hypothalamus (ARC) integrate hormonal (insulin, leptin, and ghrelin) and neuronal inputs to modulate food intake and metabolism as a means of maintaining adequate energy supplies for bodily needs. One population of neurons in the ARC that has received considerable attention expresses γ-aminobutyric acid (GABA), neuropeptide Y, and agouti-related protein (AgRP) as neurotransmitters/neuromodulators. Because AgRP is expressed exclusively in these neurons, we refer to them as AgRP neurons. These neurons become active when an animal is hungry and promote feeding behaviors by releasing their transmitters in various regions of the brain to activate the next neurons in the circuit. Genetic manipulation of AGRP neurons is relatively easy because one can target the expression of new genes to the Agrp gene locus by homologous recombination in embryonic stem cells and then derive mice carrying that genetic modification. If Cre recombinase is targeted to these AgRP neurons, then a virus carrying a Cre-dependent effector gene can be injected into the ARC and the effector protein will be expressed only in AgRP neurons. One useful effector gene is channelrhodopsin (ChR2),a light-activated ion channel that causes neurons to release transmitters when activated by a laser connected to an optic fiber inserted just above the ARC. Photo activation of AgRP neurons during the day when mice are usually sleeping stimulates robust feeding behaviors. Scott Sternson, a group leader HHMI’s Janelia Farm Research Campus, has exploited this clever technique. We performed a converse experiment by making mice that expressed the human diphtheria toxin receptor from the Agrp locus and then administered diphtheria toxin, which killed the AgRP neurons. As might be expected, if these neurons are important for feeding, the demise of AgRP neurons in adult mice led to starvation.

To understand why the mice starve after ablation of AgRP neurons, we assumed that loss of inhibitory signaling by these AgRP neurons resulted in hyperactivity of postsynaptic neurons elsewhere in the brain, which then promoted anorexia. Through a series of experiments, we discovered that hyperactivity of neurons in a brain region called the parabrachial nucleus (PBN) was responsible for the anorexia. We exploited the location of the hyperactive neurons in the PBN and coincidence with the expression pattern of the Calca gene encoding calcitonin gene–related protein (CGRP) to make a mouse that expresses Cre recombinase from the Calca locus. Viral delivery of Cre-dependent ChR2 to the PBN of the Calca-Cre mice followed by photoactivation revealed that excitation of these CGRP-expressing neurons inhibited feeding by hungry mice. Furthermore, we used another strategy to chronically inhibit these neurons and prevented starvation after ablation of AgRP neurons, providing strong evidence that loss of AgRP neurons promotes starvation by activating the CGRP neurons.

These CGRP neurons are known to relay sensory information to the forebrain. They are normally activated by visceral malaise (e.g., food poisoning), nausea (e.g., motion sickness), satiety, and probably many other conditions that lead to anorexia. Thus, activation of these neurons provides a brake on normal feeding activity and presumably protects mice from dangerous environmental events. The phenomenon of conditioned taste aversion, in which ingestion of a novel food is followed by visceral illness and consequent aversion to consuming that food in the future, depends on this circuit. This is a long-lasting, one-trial learning experience that is of obvious value to a foraging animal. Photoactivation of CGRP neurons coincident with presentation of a novel food is sufficient to establish an aversion to eating that food. The CGRP neurons also mediate the aversive effects of a foot shock: blockade of CGRP neuron function attenuates the ability of a mouse to associate the foot shock with the location in the environment where it occurred.

By selective expression of ChR2-mCherry in CGRP neurons, we visualized axon projections to the bed nucleus of the stria terminalis (BNST) and to the lateral capsule region of the central nucleus of the amygdala (lcCeA). Photoactivation of the terminals in the lcCeA inhibited feeding by hungry mice, whereas activation of terminals in the BNST had no effect. Current efforts are directed toward identifying the target neurons in the lcCeA and determining where they project their axons. We also intend to identify neurons in the hindbrain that directly activate CGRP neurons. These efforts should help to define the neural circuit that leads from the viscera to the amygdala and beyond.

Ablation of AgRP neurons in adult mice results in starvation by activating the CGRP neurons. We have discovered numerous ways to prevent the hyperactivation of CGRP neurons and thus prevent starvation, including genetic downregulation of glutamatergic signaling onto CGRP neurons, pharmacological activation of GABA signaling onto CGRP neurons, and prior treatment with lithium chloride. Remarkably, after a week or so of these interventions, the mice survive without their AgRP neurons, suggesting that some form of adaptation has taken place such that the appetite-enhancing role of the AgRP neurons is no longer necessary for adequate feeding. We suspect that adaptation involves synaptic plasticity within the CGRP neurons and plan to use electrophysiological techniques to discern the mechanisms.

Read Full Post »

CRISPR/Cas-mediated Genome Engineering

Curator: Larry H. Bernstein, MD, FCAP

UPDATED on 10/9/2015

2.1.5.27

2.1.5.27   CRISPR/Cas-mediated Genome Engineering, Volume 2 (Volume Two: Latest in Genomics Methodologies for Therapeutics: Gene Editing, NGS and BioInformatics, Simulations and the Genome Ontology), Part 2: CRISPR for Gene Editing and DNA Repair

Cpf1 Is a Single RNA-Guided Endonuclease of a Class 2 CRISPR-Cas System

Bernd Zetsche10

,

Jonathan S. Gootenberg10

,

Omar O. Abudayyeh

,

Ian M. Slaymaker

,

Kira S. Makarova

,

Patrick Essletzbichler

,

Sara E. Volz

,

Julia Joung

,

John van der Oost

,

Aviv Regev

,

Eugene V. Koonin

,

Feng Zhangcorrespondence
10Co-first author
Publication stage: In Press Corrected Proof

Highlights

  • CRISPR-Cpf1 is a class 2 CRISPR system
  • Cpf1 is a CRISPR-associated two-component RNA-programmable DNA nuclease
  • Targeted DNA is cleaved as a 5-nt staggered cut distal to a 5′ T-rich PAM
  • Two Cpf1 orthologs exhibit robust nuclease activity in human cells

Summary

The microbial adaptive immune system CRISPR mediates defense against foreign genetic elements through two classes of RNA-guided nuclease effectors. Class 1 effectors utilize multi-protein complexes, whereas class 2 effectors rely on single-component effector proteins such as the well-characterized Cas9. Here, we report characterization of Cpf1, a putative class 2 CRISPR effector. We demonstrate that Cpf1 mediates robust DNA interference with features distinct from Cas9. Cpf1 is a single RNA-guided endonuclease lacking tracrRNA, and it utilizes a T-rich protospacer-adjacent motif. Moreover, Cpf1 cleaves DNA via a staggered DNA double-stranded break. Out of 16 Cpf1-family proteins, we identified two candidate enzymes from Acidaminococcus and Lachnospiraceae, with efficient genome-editing activity in human cells. Identifying this mechanism of interference broadens our understanding of CRISPR-Cas systems and advances their genome editing applications.

VIEW IMAGE and SOURCE

http://www.cell.com/cell/abstract/S0092-8674%2815%2901200-3

SOURCE

https://www.broadinstitute.org/news/7272

Series E. 2: 7.5

Rudolf Jaenisch

One-Step Generation of Mice Carrying Mutations in Multiple Genes by CRISPR/Cas-Mediated Genome Engineering

Haoyi Wang6, Hui Yang6, Chikdu S. Shivalila6, Meelad M. Dawlaty, Albert W. Cheng, Feng Zhang, Rudolf Jaenisch
Cell May 2013; 153: 4(9), p910–918  http://dx.doi.org/10.1016/j.cell.2013.04.025

Highlights

  • •CRISPR/Cas9-mediated simultaneous targeting of five genes in mES cells
  • •Generation of Tet1/Tet2 double-mutant mice in one step
  • •Generation of Tet1/Tet2 double-mutant mice with predefined mutations in one step

Summary

Mice carrying mutations in multiple genes are traditionally generated by sequential recombination in embryonic stem cells and/or time-consuming intercrossing of mice with a single mutation. The CRISPR/Cas system has been adapted as an efficient gene-targeting technology with the potential for multiplexed genome editing. We demonstrate that CRISPR/Cas-mediated gene editing allows the simultaneous disruption of five genes (Tet123SryUty – 8 alleles) in mouse embryonic stem (ES) cells with high efficiency. Coinjection of Cas9 mRNA and single-guide RNAs (sgRNAs) targeting Tet1 and Tet2 into zygotes generated mice with biallelic mutations in both genes with an efficiency of 80%. Finally, we show that coinjection of Cas9 mRNA/sgRNAs with mutant oligos generated precise point mutations simultaneously in two target genes. Thus, the CRISPR/Cas system allows the one-step generation of animals carrying mutations in multiple genes, an approach that will greatly accelerate the in vivo study of functionally redundant genes and of epistatic gene interactions.

Generating genetically modified mice using CRISPR/Cas-mediated genome engineering

Hui Yang, Haoyi WangRudolf Jaenisch
Nature Protocols  2014; 9, 1956–1968.   http://dx.doi.org:/10.1038/nprot.2014.134

Mice with specific gene modifications are valuable tools for studying development and disease. Traditional gene targeting in mice using embryonic stem (ES) cells, although suitable for generating sophisticated genetic modifications in endogenous genes, is complex and time-consuming. We have recently described CRISPR/Cas-mediated genome engineering for the generation of mice carrying mutations in multiple genes, endogenous reporters, conditional alleles or defined deletions. Here we provide a detailed protocol for embryo manipulation by piezo-driven injection of nucleic acids into the cytoplasm to create gene-modified mice. Beginning with target design, the generation of gene-modified mice can be achieved in as little as 4 weeks. We also describe the application of the CRISPR/Cas technology for the simultaneous editing of multiple genes (five genes or more) after a single transfection of ES cells. The principles described in this protocol have already been applied in rats and primates, and they are applicable to sophisticated genome engineering in species in which ES cells are not available.

Our long-range goals are to understand epigenetic regulation of gene expression in mammalian development and disease. An important question is to understand the different epigenetic conformations that distinguish differentiated cell states and to define strategies to transdifferentiate one differentiated cell type into another. Embryonic stem cells are of major significance because they have the potential to generate any cell type in the body and, therefore, are of great interest for regenerative medicine. A major focus of our work is to understand the molecular mechanisms that allow the reprogramming of somatic cells to an embryonic pluripotent state and to use the potential of patient specific pluripotent cells to study complex human diseases.

One-Step Generation of Mice Carrying Mutations in Multiple Genes by CRISPR/Cas-Mediated Genome Engineering

Haoyi Wang16Hui Yang16Chikdu S. Shivalila126Meelad M. Dawlaty1Albert W. Cheng13Feng Zhang45Rudolf Jaenisch13,

Cell  May 2013; 153(4): 910–918  http://dx.doi.org:/10.1016/j.cell.2013.04.025

Highlights

  • CRISPR/Cas9-mediated simultaneous targeting of five genes in mES cells
  • Generation of Tet1/Tet2 double-mutant mice in one step
  • Generation of Tet1/Tet2 double-mutant mice with predefined mutations in one step

Mice carrying mutations in multiple genes are traditionally generated by sequential recombination in embryonic stem cells and/or time-consuming intercrossing of mice with a single mutation. The CRISPR/Cas system has been adapted as an efficient gene-targeting technology with the potential for multiplexed genome editing. We demonstrate that CRISPR/Cas-mediated gene editing allows the simultaneous disruption of five genes (Tet1, 2, 3, Sry, Uty – 8 alleles) in mouse embryonic stem (ES) cells with high efficiency. Coinjection of Cas9 mRNA and single-guide RNAs (sgRNAs) targeting Tet1 and Tet2 into zygotes generated mice with biallelic mutations in both genes with an efficiency of 80%. Finally, we show that coinjection of Cas9 mRNA/sgRNAs with mutant oligos generated precise point mutations simultaneously in two target genes. Thus, the CRISPR/Cas system allows the one-step generation of animals carrying mutations in multiple genes, an approach that will greatly accelerate the in vivo study of functionally redundant genes and of epistatic gene interactions.

Genetically modified mice represent a crucial tool for understanding gene function in development and disease. Mutant mice are conventionally generated by insertional mutagenesis (Copeland and Jenkins, 2010Kool and Berns, 2009) or by gene-targeting methods (Capecchi, 2005). In conventional gene-targeting methods, mutations are introduced through homologous recombination in mouse embryonic stem (ES) cells. Targeted ES cells injected into wild-type (WT) blastocysts can contribute to the germline of chimeric animals, generating mice containing the targeted gene modification (Capecchi, 2005). It is costly and time consuming to produce single-gene knockout mice and even more so to make double-mutant mice. Moreover, in most other mammalian species, no established ES cell lines are available that contribute efficiently to chimeric animals, which greatly limits the genetic studies in many species.

Alternative methods have been developed to accelerate the process of genome modification by directly injecting DNA or mRNA of site-specific nucleases into the one-cell embryo to generate DNA double-strand break (DSB) at a specified locus in various species (Bogdanove and Voytas, 2011Carroll et al., 2008Urnov et al., 2010). DSBs induced by these site-specific nucleases can then be repaired by error-prone nonhomologous end joining (NHEJ) resulting in mutant mice and rats carrying deletions or insertions at the cut site (Carbery et al., 2010Geurts et al., 2009Sung et al., 2013;Tesson et al., 2011). If a donor plasmid with homology to the ends flanking the DSB is coinjected, high-fidelity homologous recombination can produce animals with targeted integrations (Cui et al., 2011Meyer et al., 2010). Because these methods require the complex designs of zinc finger nucleases (ZNFs) or Transcription activator-like effector nucleases (TALENs) for each target gene and because the efficiency of targeting may vary substantially, no multiplexed gene targeting in animals has been reported to date. To dissect the functions of gene family members with redundant functions or to analyze epistatic relationships in genetic pathways, mice with two or more mutated genes are required, prompting the development of efficient technology for the generation of animals carrying multiple mutated genes.

Recently, the type II bacterial CRISPR/Cas system has been demonstrated as an efficient gene-targeting technology with the potential for multiplexed genome editing. Bacteria and archaea have evolved an RNA-based adaptive immune system that uses CRISPR (clustered regularly interspaced short palindromic repeat) and Cas (CRISPR-associated) proteins to detect and destroy invading viruses and plasmids (Horvath and Barrangou, 2010Wiedenheft et al., 2012). Cas proteins, CRISPR RNAs (crRNAs), andtrans-activating crRNA (tracrRNA) form ribonucleoprotein complexes, which target and degrade foreign nucleic acids, guided by crRNAs ( Gasiunas et al., 2012Jinek et al., 2012). It was shown that the Cas9 endonuclease from Streptococcus pyogenes type II CRISPR/Cas system can be programmed to produce sequence-specific DSB in vitro by providing a synthetic single-guide RNA (sgRNA) consisting of a fusion of crRNA and tracrRNA ( Jinek et al., 2012). More intriguingly, Cas9 and sgRNA are the only components necessary and sufficient for induction of targeted DNA cleavage in cultured human cells ( Cho et al., 2013Cong et al., 2013Mali et al., 2013) as well as in zebrafish (Chang et al., 2013Hwang et al., 2013). A recent report also demonstrated disruption of a GFP transgene in mice using the CRISPR/Cas system ( Shen et al., 2013). The ease of design, construction, and delivery of multiple sgRNAs suggest the possibility of multiplexed genome editing in mammals. Indeed, one study demonstrated that two loci separated by 119 bp could be cleaved simultaneously in cultured human cells at a low efficiency ( Cong et al., 2013). The extent of achievable multiplexed genome editing has yet to be demonstrated in stem cells as well as in animals. Here, we use the CRISPR/Cas system to drive both NHEJ-based gene disruption and homology directed repair (HDR)-based precise gene editing to achieve highly efficient and simultaneous targeting of multiple genes in stem cells and mice.

Simultaneous Targeting up to Five Genes in ES Cells

To test whether the CRISPR/Cas system could produce targeted cleavage in the mouse genome, we transfected plasmids expressing both the mammalian-codon-optimized Cas9 and a sgRNA targeting each gene ( Cong et al., 2013Mali et al., 2013) into mouse ES cells and determined the targeted cleavage efficiency by the Surveyor assay ( Guschin et al., 2010). All three Cas9-sgRNA transfections produced cleavage at target loci with high efficiency of 36% at Tet1, 48% atTet2, and 36% at Tet3 ( Figure 1B). Because each target locus contains a restriction enzyme recognition site ( Figure 1A), we PCR amplified an ∼500 bp fragment around each target site and digested the PCR products with the respective enzyme. A correctly targeted allele will lose the restriction site, which can be detected by failure to cleave upon enzyme treatment. Using this restriction fragment length polymorphism (RFLP) assay, we screened 48 ES cell clones from each single-targeting experiment. Consistent with the Surveyor analysis, a high percentage of ES cell clones were targeted, with a high probability of having both alleles mutated ( Figure S1A available online). The results summarized in Table 1 demonstrate that between 65% and 81% of the tested ES cell clones carried mutations in the Tet genes with up to 77% having mutations in both alleles.

Figure 1.

Multiplexed Gene Targeting in mouse ES cells

(A) Schematic of the Cas9/sgRNA-targeting sites in Tet12, and 3. The sgRNA-targeting sequence is underlined, and the protospacer-adjacent motif (PAM) sequence is labeled in green. The restriction sites at the target regions are bold and capitalized. Restriction enzymes used for RFLP and Southern blot analysis are shown, and the Southern blot probes are shown as orange boxes.

(B) Surveyor assay for Cas9-mediated cleavage at Tet12, and 3 loci in ES cells.

(C) Genotyping of triple-targeted ES cells, clones 51, 52, and 53 are shown. Upper: RFLP analysis. Tet1PCR products were digested with SacI, Tet2 PCR products were digested with EcoRV, and Tet3 PCR products were digested with XhoI. Lower: Southern blot analysis. For the Tet1 locus, SacI digested genomic DNA was hybridized with a 5′ probe. Expected fragment size: WT = 5.8 kb, TM (targeted mutation) = 6.4 kb. For the Tet2 locus, SacI, and EcoRV double-digested genomic DNA was hybridized with a 3′ probe. Expected fragment size: WT = 4.3 kb, TM = 5.6 kb. For the Tet3 locus, BamHI and XhoI double-digested genomic DNA was hybridized with a 5′ probe. Expected fragment size: WT = 3.2 kb, TM = 8.1 kb.

(D) The sequence of six mutant alleles in triple-targeted ES cell clone 14 and 41. PAM sequence is labeled in red.

(E) Analysis of 5hmC levels in DNA isolated from triple-targeted ES cell clones by dot blot assay using anti-5hmC antibody. A previously characterized DKO clone derived using traditional method is used as a control. See also Figure S1.

Figure options

Figure S1.

Single-, Triple-, and Quintuple-Gene Targeting in mES Cells, Related to Figure 1

(A) RFLP analysis of clones from each single-targeting experiment (1 to 17 are shown).

(B) RFLP analysis of triple-gene-targeted clones (37 to 53 are shown). Tet1 PCR products were digested with SacI, Tet2 PCR products were digested with EcoRV, and Tet3 PCR products were digested with XhoI. WT control is shown in the last lane. Genotyping of clone 51, 52, and 53 are also shown in Figure 1C.

(C) Schematic of the Cas9/sgRNA-targeting sites in Sry and Uty. The sgRNA-targeting sequence is underlined, and the protospacer-adjacent motif (PAM) sequence is labeled in green. The restriction sites at the target regions are bold and capitalized. Restriction enzymes used for RFLP analysis are shown.

(D) RFLP analysis of quintuple-gene-targeted clones (1 to 10 are shown). Sry PCR products were digested with BsaJI, Uty PCR products were digested with AvrII. WT control is shown in the last lane. RFLP analysis of Tet123 loci are not shown.

Figure options

Table 1.

CRISPR/Cas-Mediated Gene Targeting in V6.5 ES Cells

Mutant Alleles per Clone / Total Clones Tested
Gene 6 5 4 3 2 1 0
Tet1 N/A 27/48 4/48 17/48
Tet2 37/48 2/48 9/48
Tet3 32/48 3/48 13/48
Tet1Tet2 + Tet3 20/96 16/96 2/96 2/96 1/96 0/96 55/96

Plasmids encoding Cas9 and sgRNAs targeting Tet1Tet2, and Tet3 were transfected separately (single targeting) or in a pool (triple targeting) into ES cells. The number of total alleles mutated in each ES cell clone is listed from 0 to 2 for single-targeting experiment, and 0 to 6 for triple-targeting experiment. The number of clones containing each specific number of mutated alleles is shown in relation to the total number of clones screened in each experiment. See also Table S1.

Table options

The high efficiency of single-gene modification prompted us to test the possibility of targeting all three genes simultaneously. For this we cotransfected ES cells with the constructs expressing Cas9 and three sgRNAs targeting Tet12, and 3. Of 96 clones screened using the RFLP assay, 20 clones were identified as having mutations in all six alleles of the three genes ( Figures 1C and S1B and Table 1). To exclude that a PCR bias could give false positive results, we performed Southern blot analysis and confirmed complete agreement with the RFLP results ( Figure 1C). We subcloned and sequenced the PCR products of Tet1-, Tet2-, and Tet3-targeted regions to verify that all of eight tested clones carried biallelic mutations in all three genes with most clones displaying two mutant alleles for each gene with small insertions or deletions (indels) at the target site ( Figure 1D). To test whether these mutant alleles would abolish the function of Tet proteins, we compared the 5hmC level of targeted clones to WT ES cells. Previously, we reported a depletion of 5hmC in Tet1/Tet2 double-knockout ES cells derived using traditional gene-targeting methods ( Dawlaty et al., 2013). As expected from loss of function alleles, we found a significant reduction of 5hmC levels in all clones carrying biallelic mutations in the three genes ( Figure 1E).

To further test the potential of multiplexed gene targeting by CRISPR/Cas system, we designed sgRNAs targeting two Y-linked genes, Sry and Uty ( Figure S1C). Short PCR products encoding sgRNAs targeting all five genes (Tet1Tet2Tet3Sry, and Uty) were pooled and cotransfected with a Cas9 expressing plasmid and the PGK puroR cassette into ES cells. Of 96 clones that were screened using the RFLP assay, 10% carried mutations in all eight alleles of the five genes ( Figure S1D and Table S1), demonstrating the capacity of the CRISP/Cas9 system for highly efficient multiplexed gene targeting.

One-Step Generation of Single-Gene Mutant Mice by Zygote Injection

We tested whether mutant mice could be generated in vivo by direct embryo manipulation. Capped polyadenylated Cas9 mRNA was produced by in vitro transcription and coinjected with sgRNAs. Initially, to determine the optimal concentration of Cas9 mRNA for targeting in vivo, we microinjected varying amounts of Cas9-encoding mRNA with Tet1 targeting sgRNA at constant concentration (20 ng/μl) into pronuclear (PN) stage one-cell mouse embryos and assessed the frequency of altered alleles at the blastocyst stage using the RFLP assay. As expected, higher concentration of Cas9 mRNA led to more efficient gene disruption ( Figure S2A). Nevertheless, even embryos injected with the highest amount of Cas9 mRNA (200 ng/μl) showed normal blastocyst development, suggesting low toxicity.

Figure S2.

One-Step Generation of Single-Gene Mutant Mice by Zygote Injection, Related to Figure 2

(A) RFLP analysis of blastocysts injected with different concentration of Cas9 mRNA and Tet1 sgRNA at 20 ng/μl. Tet1 PCR products were digested with SacI.

(B) Commonly recovered Tet1 and Tet2 alleles resulted from MMEJ. PAM sequence of each targeting sequence is labeled in green. Microhomology flanking the DSB is bold and underlined in WT sequence.

(C) RFLP analysis of eight Tet3-targeted blastocysts demonstrated high targeting efficiency (embryo 3 and 5 failed to amplify). Tet3 PCR products were digested with XhoI.

(D) Some Tet3-targeted mice show smaller size and all homozygous mutants died within 1 day after birth.

(E) RFLP analysis of Tet3 single-targeted newborn mice. Mouse 8 and 14 survived after birth. Sample 2 and 6 failed to amplify.

(F) Sequences of both Tet3 alleles of surviving Tet3-targeted mouse 14. PAM sequences are labeled in red.

Figure options

To investigate whether postnatal mice carrying targeted mutations could be generated, we coinjected sgRNAs targeting Tet1or Tet2 with different concentrations of Cas9 mRNA. Blastocysts derived from the injected embryos were transplanted into foster mothers and newborn pups were obtained. As summarized in Table 2, about 10% of the transferred blastocysts developed to birth independent of the RNA concentrations used for injection suggesting low fetal toxicity of the Cas9 mRNA and sgRNA. RFLP, Southern blot, and sequencing analysis demonstrated that between 50 and 90% of the postnatal mice carried biallelic mutations in either target gene ( Figures 2A, 2B, and 2C and Table 2).

Table 2.

CRISPR/Cas-Mediated Single-Gene Targeting in BDF2 Mice

Gene Cas9/sg RNA (ng/μl) Blastocysts/Injected Zygotes Transferred Embryos (Recipients) Newborns (Dead) Mutant Alleles per Mouse/Total Mice Testeda
2 1 0
Tet1 200/20 38/50 19 (1) 2 (0) 2/2 0/2 0/2
100/20 50/60 25 (1) 3 (0) 2/3 0/3 1/3
50/20 40/50 40 (2) 8 (3) 4/7 2/7 1/7
100/50 167/198 60 (3) 12 (2) 9/11 1/11 1/11
Tet2 100/50 176/203 108 (5) 22 (3) 19/20 0/20 1/20
Tet3 100/50 85/112 64 (4) 15 (13) 9/13 2/13 2/13

Cas9 mRNA and sgRNAs targeting Tet1Tet2, or Tet3 were injected into fertilized eggs. The blastocysts derived from injected embryos were transplanted into foster mothers and newborn pups were obtained and genotyped. The number of total alleles mutated in each mouse is listed from 0 to 2. The number of mice containing each specific number of mutated alleles is shown in relation to the total number of mice screened in each experiment. See also Table S2. A Some of the pups were cannibalized.

Table options

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413004674-gr2.jpg

Surprisingly, specific Δ9 Tet1 and specific Δ8 and Δ15 Tet2 mutant alleles were repeatedly recovered in independently derived mice. Preferential generation of these alleles is likely caused by a short sequence repeat flanking the DSB (see Figure S2B) consistent with previous reports demonstrating that perfect microhomology sequences flanking the cleavage sites can generate microhomology-mediated precise deletions by end repair mechanism (MMEJ) ( McVey and Lee, 2008Symington and Gautier, 2011) (Figure S2B). A similar observation was also made when TALEN mRNA was injected into one-cell rat embryos ( Tesson et al., 2011).

We also derived blastocysts from zygotes injected with Cas9 mRNA and Tet3 sgRNA. Genotyping of the blastocysts demonstrated that of eight embryos three were homozygous and three were heterozygous Tet3 mutants (two failed to amplify) (Figure S2C). Some blastocysts were implanted into foster mothers and, upon C section, we readily identified multiple mice of smaller size ( Figure S2D), many of which died soon after delivery. Genotyping shown in Figure S2E indicated that all pups with mutations in both Tet3 alleles died neonatally. Only 2 out of 15 mice survived that were either Tet3heterozygous mutants or WT ( Figure S2F). These results are consistent with the lethal neonatal phenotype of Tet3 knockout mice generated using traditional methods ( Gu et al., 2011), although we have not yet established which of the Tet3 mutations produced loss of function rather than hypomorphic alleles.

One-Step Generation of Double-Gene Mutant Mice by Zygote Injection

To test whether Tet1/Tet2 double-mutant mice could be produced from single embryos, we coinjected Tet1 and Tet2 sgRNAs with 20 or 100 ng/μl Cas9 mRNA into zygotes. A total of 28 pups were born from 144 embryos transferred into foster mothers (21% live-birth rate) that had been injected at the zygote stage with high concentrations of RNA (Cas9 mRNA at 100 ng/μl, sgRNAs at 50 ng/μl), consistent with low or no toxicity of the Cas9 mRNA and sgRNAs ( Table 3). RFLP, Southern blot analysis, and sequencing identified 22 mice carrying targeted mutations at all four alleles of the Tet1 and Tet2genes ( Figures 2D and 2E) with the remaining mice carrying mutations in a subset of alleles ( Table 3). Injection of zygotes with low concentration of RNA (Cas9 mRNA at 20 ng/μl, sgRNAs at 20 ng/μl) yielded 19 pups from 75 transferred embryos (25% live-birth rate), which is a higher survival rate than from embryos injected with 100 ng/μl of Cas9 RNA. Nevertheless, more than 50% of the pups were biallelic Tet1/Tet2 double mutants ( Table 3). These results demonstrate that postnatal mice carrying biallelic mutations in two different genes can be generated within one month with high efficiency (Figure 2F).

Table 3.

CRISPR/Cas-Mediated Double-Gene Targeting in BDF2 Mice

Gene Cas9/sgRNA (ng/μl) Blastocyst/Injected Zygotes Transferred Embryos (Recipients) Newborns (Dead) Mutant Alleles per Mouse/Total Mice Testeda
4 3 2 1 0
Tet1 +Tet2 100 / 50 194/229 144(7) 31(8) 22/28 4/28 1/28 1/28 0/28
20 / 20 92/109 75(5) 19(3) 11/19 1/19 2/19 3/19 2/19

Cas9 mRNA and sgRNAs targeting Tet1and Tet2 were coinjected into fertilized eggs. The blastocysts derived from the injected embryos were transplanted into foster mothers and newborn pups were obtained and genotyped. The number of total alleles mutated in each mouse is listed from 0 to 4 for Tet1 and Tet2. The number of mice containing each specific number of mutated alleles is shown in relation to the number of total mice screened in each experiment. A Some of the pups were cannibalized.

Table options

Although the high live-birth rate and normal development of mutant mice suggest low toxicity of CRISPR/Cas9 system, we sought to determine the off-target effects in vivo. Previous work in vitro, in bacteria, and in cultured human cells suggested that the protospacer-adjacent motif (PAM) sequence NGG and the 8 to 12 base “seed sequence” at the 3′ end of the sgRNA are most important for determining the DNA cleavage specificity (Cong et al., 2013Jiang et al., 2013Jinek et al., 2012). Based on this rule, only three and four potential off targets exist in mouse genome for Tet1 and Tet2 sgRNA, respectively ( Table S2 and Experimental Procedures), with each of them perfectly matching the 12 bp seed sequence at the 3′ end and the NGG PAM sequence of the sgRNA (there is no potential off-target site for Tet3 sgRNA using this prediction rule). From seven double-mutant mice produced from injection with high RNA concentration we PCR amplified 400 to 500 bp fragments from all seven potential off-target loci and found no cleavage in the Surveyor assay ( Figure S3), suggesting a high specificity of CRISPR/Cas system.

Figure S3.

Off-Target Analysis of Double-Mutant Mice, Related to Figure 2

(A) Three potential off targets of Tet1 sgRNA and four potential off targets of Tet2 sgRNA are shown. The 12 bp perfect matching seed sequence is labeled in blue, and NGG PAM sequence is labeled in red.

(B) Surveyor assay of all seven potential off-target loci in seven double-mutant mice derived with high concentration of Cas9 mRNA (100 ng/μl) injection. WT control is included as the eighth sample. The weak cleavage activity at Ubr1 locus is not due to off-target effect because sequences of these PCR products show no mutations.

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413004674-figs3.jpg

Multiplexed Precise HDR-Mediated Genome Editing In Vivo

The NHEJ-mediated gene mutations described above produced mutant alleles with different and unpredictable insertions and deletions of variable size. We explored the possibility of precise homology directed repair (HDR)-mediated genome editing by coinjecting Cas9 mRNA, sgRNAs, and single-stranded DNA oligos into one-cell embryos. For this we designed an oligo targeting Tet1 so as to change two base pairs of a SacI restriction site and creating instead an EcoRI site and a second oligo targetingTet2 with two base pair changes that would convert an EcoRV site into an EcoRI site (Figure 3A). Blastocysts were derived from zygotes injected with Cas9 mRNA and sgRNAs and oligos targeting Tet1 or Tet2, respectively. DNA was isolated, amplified, and digested with EcoRI to detect oligo-mediated HDR events. Six out of nine Tet1-targeted embryos and 9 out of 15 Tet2-targeted embryos incorporated an EcoRI site at the respective target locus, with several embryos having both alleles modified (Figure S4A). When Cas9 mRNA, sgRNAs, and single-stranded DNA oligos targeting both Tet1 and Tet2 were coinjected into zygotes, out of 14 embryos, four were identified that were targeted with the oligo at the Tet1 locus, seven that were targeted with the oligo at the Tet2 locus and one embryo (2) that had one allele of each gene correctly modified (Figure S4B). All four alleles of embryo 2 were sequenced, confirming that one allele of each gene contained the 2 bp changes directed by the oligo, whereas the other alleles were disrupted by NHEJ-mediated deletion and insertion ( Figure S4C).

Figure 3.

Multiplexed HDR-Mediated Genome Editing In Vivo

(A) Schematic of the oligo-targeting sites at Tet1 and Tet2 loci. The sgRNA-targeting sequence is underlined, and the PAM sequence is labeled in green. Oligo targeting each gene is shown under the target site, with 2 bp changes labeled in red. Restriction enzyme sites used for RFLP analysis are bold and capitalized.

(B) RFLP analysis of double oligo injection mice with HDR-mediated targeting at the Tet1 and Tet2 loci.

(C) The sequences of both alleles of Tet1 and Tet2 in mouse 5 and 7 show simultaneously HDR-mediated targeting at one allele or two alleles of each gene, and NHEJ-mediated disruption at the other alleles. See also Figure S4.

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413004674-gr3.jpg

Figure S4.

Multiplexed Precise HDR-Mediated Genome Editing In Vivo, Related to Figure 3

(A) RFLP analysis of single oligo injection embryos with HDR-mediated targeting at Tet1 and Tet2 locus.

(B) RFLP analysis of double oligo injection embryos with multiplexed HDR-mediated targeting at both Tet1and Tet2 loci.

(C) Sequences of both alleles of Tet1 and Tet2 in embryo 2 show simultaneously HDR-mediated targeting at one allele of both genes, and NHEJ-mediated gene disruption at the other allele of each gene.

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413004674-figs4.jpg

Blastocysts with double oligo injections were implanted into foster mothers and a total of 10 pups were born from 48 embryos transferred (21% live-birth rate). Upon RFLP analysis using EcoRI, we identified seven mice containing EcoRI sites at the Tet1 locus and eight mice containing EcoRI sites at the Tet2 locus, with six mice containing EcoRI sites at both Tet1 and Tet2 loci ( Figure 3B). We also applied RFLP analysis using SacI and EcoRV to Tet1 and Tet2 loci, respectively, showing that all alleles not targeted by oligos contained disruptions, which is in consistent with the high biallelic mutation rate by Cas9 mRNA and sgRNAs injection. These results were confirmed by sequencing demonstrating mutations in all four alleles of mouse 5 and 7 ( Figure 3C). Our results demonstrate that mice with HDR-mediated precise mutations in multiple genes can be generated in one step by CRISPR/Cas-mediated genome editing.

Discussion

The genetic manipulation of mice is a crucial approach for the study of development and disease. However, the generation of mice with specific mutations is labor intensive and involves gene targeting by homologous recombination in ES cells, the production of chimeric mice, and, after germline transmission of the targeted ES cells, the interbreeding of heterozygous mice to produce the homozygous experimental animals, a process that may take 6 to 12 months or longer (Capecchi, 2005). To produce mice carrying mutations in several genes requires time-consuming intercrossing of single-mutant mice. Similarly, the generation of ES cells carrying homozygous mutations in several genes is usually achieved by sequential targeting, a process that is labor intensive, necessitating multiple consecutive cloning steps to target the genes and to delete the selectable markers.

As summarized in Figure 4, we have established three different approaches for the generation of mice carrying multiple genetic alterations. We demonstrate that CRISPR/Cas-mediated genome editing in ES cells can generate the simultaneous mutations of several genes with high efficiency, a single-step approach allowing the production of cells with mutations in five different genes (Figure 4A). We chose the threeTet genes as targets because the respective mutant phenotypes have been well defined previously ( Dawlaty et al., 20112013Gu et al., 2011). Cells mutant for Tet12 and 3were depleted of 5hmC as would be expected for loss of function mutations of the genes (Dawlaty et al., 2013). However, we have not as yet established, which of the Cas9-mediated gene mutations produced loss of function rather than hypomorphic alleles.

Figure 4.

Mutiplexed Genome Editing in ES Cells and Mouse

(A) Multiple gene targeting in ES cells.

(B) One-step generation of mice with multiple mutations. Upper: multiple targeted mutations with random indels introduced through NHEJ. Lower: multiple predefined mutations introduced through HDR-mediated repair.

Figure options

We also show that mouse embryos can be directly modified by injection of Cas9 mRNA and sgRNA into the fertilized egg resulting in the efficient production of mice carrying biallelic mutations in a given gene. More significantly, coinjection of Cas9 with Tet1 andTet2 sgRNAs into zygotes produced mice that carried mutations in both genes (Figure 4B, upper). We found that up to 95% of newborn mice were biallelic mutant in the targeted gene when single sgRNA was injected and when coinjected with two different sgRNAs, up to 80% carried biallelic mutations in both targeted genes. Thus, mice carrying multiple mutations can be generated within 4 weeks, which is a much shorter time frame than can be achieved by conventional consecutive targeting of genes in ES cells and avoids time-consuming intercrossing of single-mutant mice.

The introduction of DSBs by CRISPR/Cas generates mutant alleles with varying deletions or insertions in contrast to designed precise mutations created by homologous recombination. The introduction of point mutations into human ES cells, cancer cell lines, and mouse by ZNF or TALEN along with DNA oligo has been demonstrated previously (Chen et al., 2011Soldner et al., 2011Wefers et al., 2013). We demonstrate that CRISPR/Cas-mediated targeting is useful to generate mutant alleles with predetermined alterations, and coinjection of single-stranded oligos can introduce designed point mutations into two target genes in one step, allowing for multiplexed gene editing in a strictly controlled manner (Figure 4B, lower). It will be of great interest to assess whether this targeting system allows for the production of conditional alleles, or precise insertion of larger DNA fragments such as GFP markers so as to generate conditional knockout and reporter mice for specific genes.

There are several potential limitations of the CRISPR/Cas technology. First, the requirement for a NGG PAM sequence of S. pyogenes Cas9 limits the target space in the mouse genome. It has been shown that the Streptococcus thermophilus LMD-9 Cas9 using different PAM sequence can also induce targeted DNA cleavage in mammalian cells ( Cong et al., 2013). Therefore, exploiting different Cas9 proteins may enable to target most of the mouse genome. Second, although the sgRNAs used here showed high targeting efficiency, much work is needed to elucidate the rules for designing sgRNAs with consistent high targeting efficiency, which is essential for multiplexed genome engineering. Third, although our off-target analysis for the seven most likely off targets of Tet1 and Tet2 sgRNAs failed to detect mutations in these loci, it is possible that other mutations were induced following as yet unidentified rules. A more thorough sequencing analysis for a large number of sgRNAs will provide more information about the potential off-target cleavage of the CRISPR/Cas system and lead to a better prediction of potential off-target sites. Last, oligo-mediated repair allows for precise genome editing, but the other allele is often mutated through NHEJ ( Figures 3B, 3C, andS4C). We have shown that using lower Cas9 mRNA concentration generates more mice with heterozygous mutations. Therefore, it may be possible to optimize the system for more efficient generation of mice with only one oligo -modified allele. In addition, employment of Cas9 nickase will likely avoid this complication because it mainly induces DNA single-strand break, which is typically repaired through HDR ( Cong et al., 2013;Mali et al., 2013).

It is likely that a much larger number of genomic loci than targeted in the present work can be modified simultaneously when pooled sgRNAs are introduced. The methods presented here open up the possibility of systematic genome engineering in mice, facilitating the investigation of entire signaling pathways, of synthetic lethal phenotypes or of genes that have redundant functions. A particularly interesting application is the possibility to produce mice carrying multiple alterations in candidate loci that have been identified in GWAS studies to play a role in the genesis of multigenic diseases. In summary, CRISPR/Cas-mediated genome editing makes possible the generation of ES cells and mice carrying multiple genetic alterations and will facilitate the genetic dissection of development and complex diseases.

One-Step Generation of Mice Carrying Reporter and Conditional Alleles by CRISPR/Cas-Mediated Genome Engineering

Hui Yang14Haoyi Wang14Chikdu S. Shivalila124Albert W. Cheng13Linyu Shi1, Rudolf Jaenisch13

Cell Sep 2013; 154(6):1370-1379   http://dx.doi.org:/10.1016/j.cell.2013.08.022

Highlights

  • One-step generation of mice with reporters in endogenous genes
  • One-step generation of conditional mutant mice
  • Off-target analysis suggests high specificity of the CRISPR/Cas9 system

The type II bacterial CRISPR/Cas system is a novel genome-engineering technology with the ease of multiplexed gene targeting. Here, we created reporter and conditional mutant mice by coinjection of zygotes with Cas9 mRNA and different guide RNAs (sgRNAs) as well as DNA vectors of different sizes. Using this one-step procedure we generated mice carrying a tag or a fluorescent reporter construct in the Nanog, the Sox2, and the Oct4 gene as well as Mecp2 conditional mutant mice. In addition, using sgRNAs targeting two separate sites in the Mecp2 gene, we produced mice harboring the predicted deletions of about 700 bps. Finally, we analyzed potential off-targets of five sgRNAs in gene-modified mice and ESC lines and identified off-target mutations in only rare instances.

Mice with specific gene modification are valuable tools for studying development and disease. Traditional gene targeting in embryonic stem (ES) cells, although suitable for generating sophisticated genetic modifications in endogenous genes, is complex and time-consuming (Capecchi, 2005). The production of genetically modified mice and rats has been greatly accelerated by novel approaches using direct injection of DNA or mRNA of site-specific nucleases into the one-cell-stage embryo, generating DNA double-strand breaks (DSB) at specified sequences leading to targeted mutations (Carbery et al., 2010Geurts et al., 2009Shen et al., 2013Sung et al., 2013Tesson et al., 2011 and Wang et al., 2013). Coinjection of a single-stranded or double-stranded DNA template containing homology to the sequences flanking the DSB can produce mutant alleles with precise point mutations or DNA inserts (Brown et al., 2013Cui et al., 2011Meyer et al., 2010Wang et al., 2013 and Wefers et al., 2013). Recently, pronuclear injection of two pairs of ZFNs and two double-stranded donor vectors into rat fertilized eggs produced rat containing loxP-flanked (floxed) alleles (Brown et al., 2013). However, the complex and time-consuming design and generation of ZFNs and double-stranded donor vectors limit the application of this method.

CRISPR (clustered regularly interspaced short palindromic repeat) and Cas (CRISPR-associated) proteins function as the RNA-based adaptive immune system in bacteria and archaea (Horvath and Barrangou, 2010 and Wiedenheft et al., 2012). The type II bacterial CRISPR/Cas system has been demonstrated as an efficient gene-targeting technology that facilitates multiplexed gene targeting (Cong et al., 2013 and Wang et al., 2013). Because the binding of Cas9 is guided by the simple base-pair complementarities between the engineered single-guide RNA (sgRNA) and a target genomic DNA sequence, it is possible to direct Cas9 to any genomic locus by providing the engineered sgRNA (Cho et al., 2013Cong et al., 2013Gilbert et al., 2013Hwang et al., 2013Jinek et al., 2012Jinek et al., 2013Mali et al., 2013bQi et al., 2013 and Wang et al., 2013).

Previously, we used the type II bacterial CRISPR/Cas system as an efficient tool to generate mice carrying mutations in multiple genes in one step (Wang et al., 2013). However, this study left a number of issues unresolved. For example, neither the efficiency of using the CRISPR/Cas gene-editing approach for the insertion of DNA constructs into endogenous genes nor its utility to create conditional mutant mice was clarified. Here, we report the one-step generation of mice carrying reporter constructs in three different genes as well as the derivation of conditional mutant mice. In addition, we performed an extensive off-target cleavage analysis and show that off-target mutations are rare in targeted mice and ES cells derived from CRISPR/Cas zygote injection.

Results

Targeted Insertion of Short DNA Fragments

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413010167-figs1.jpg

Mice with Reporters in the Endogenous Nanog, Sox2, and Oct4 Genes

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413010167-gr1.jpg

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413010167-gr2.jpg

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413010167-figs2.jpg

Finally, we designed sgRNA targeting the Oct4 3′ UTR, which was coinjected with a published donor vector designed to integrate the 3 kb transgene cassette (IRES-eGFP-loxP-Neo-loxP; Figure 2D) at the 3′ end of the Oct4 gene ( Lengner et al., 2007). Blastocysts were derived from injected zygotes, inspected for GFP expression, and explanted to derive ES cells. About 20% (47/254) of the blastocysts displayed uniform GFP expression in the ICM region. Three of nine derived ES cell lines expressed GFP (Figure 2E), including one showed mosaic expression ( Table S2). Three out of ten live-born mice contained the targeted allele ( Table 1). Correct targeting in mice and ES cell lines was confirmed by Southern blot analysis ( Figure 2F).

Conventionally, transgenic mice are generated by pronuclear instead of cytoplasmic injection of DNA. To optimize the generation of CRISPR/Cas9-targeted embryos, we compared different concentrations of RNA and the Nanog-mCherry or the Oct4-GFP DNA vectors as well as three different delivery modes: (1) simultaneous injection of all constructs into the cytoplasm, (2) simultaneous injection of the RNA and the DNA into the pronucleus, and (3) injection of Cas9/sgRNA into the cytoplasm followed 2 hr later by pronuclear injection of the DNA vector. Table S1 shows that simultaneous injection of all constructs into the cytoplasm at a concentration of 100 ng/μl Cas9 RNA, 50 ng/μl of sgRNA and 200 ng/μl of vector DNA was optimal, resulting in 9% (86/936) to 19% (47/254) of targeted blastocysts. Similarly, the simultaneous injection of 5 ng/μl Cas9 RNA, 2.5 ng/μl of sgRNA, and 10 ng/μl of DNA vector into the pronucleus yielded between 9% (7/75) and 18% (13/72) targeted blastocysts. In contrast, the two-step procedure with Cas9 and sgRNA simultaneous injected into the cytoplasm followed 2 hr later by pronuclear injection of different concentrations of DNA vector yielded no or at most 3% (1/34) positive blastocysts. Thus, our results suggest that simultaneous injection of RNA and DNA into the cytoplasm or nucleus is the most efficient procedure to achieve targeted insertion.

Conditional Mecp2 Mutant Mice

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413010167-figs3.jpg

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413010167-gr3.jpg

A total of 98 E13.5 embryos and mice were generated from zygotes injected with Cas9 mRNA, sgRNAs, and DNA oligos targeting the L2 and R1 sites. Genomic DNA was digested with both NheI and EcoRI, and analyzed by Southern blot using exon 3 and exon 4 probes (Figures 3A and 3B). The L2 and R1 oligos contained, in addition to the loxP site, different restriction sites (NheI or EcoRI). Thus, single loxP site integration at L2 or R1 will produce either a 3.9 kb or a 2 kb band, respectively, when hybridized with the exon3 probe (Figures 3A and B). We found that about 50% (45/98) of the embryos and mice carried a loxP site at the L2 site and about 25% (25/98) at the R1 site. Importantly, integration of both loxP sites on the same DNA molecule, generating a floxed allele, produces a 700 bp band as detected by exon 3 probe hybridization (Figures 3A and 3B). RFLP analysis, sequencing (Figures S4A and S4B) and Southern blot analysis (Figure 3B) showed that 16 out of the 98 mice tested contained two loxP sites flanking exon 3 on the same allele. Table 2 summarizes the frequency of all alleles and shows that the overall insertion frequency of an L2 or R1 insertion was slightly higher in females (21/38) than in males (28/60) consistent with the higher copy number of the X-linkedMecp2 gene in females. To confirm that the floxed allele was functional, we used genomic DNA for in vitro Cre-mediated recombination. Upon Cre treatment, both the deletion and circular products were detected by PCR in targeted mice, but not in DNA from wild-type mice ( Figure 3C). The PCR products were sequenced and confirmed the precise Cre-loxP-mediated recombination ( Figure S4C).

http://ars.els-cdn.com/content/image/1-s2.0-S0092867413010167-figs4.jpg

Mosaicism

Off-Target Analysis

In this study, we demonstrate that CRISPR/Cas technology can be used for efficient one-step insertions of a short epitope or longer fluorescent tags into precise genomic locations, which will facilitate the generation of mice carrying reporters in endogenous genes. Mice and embryos carrying reporter constructs in the Sox2, the Nanog and the Oct4 gene were derived from zygotes injected with Cas9 mRNA, sgRNAs, and DNA oligos or vectors encoding a tag or a fluorescent marker. Moreover, microinjection of two Mecp2-specific sgRNAs, Cas9 mRNA, and two different oligos encoding loxP sites into fertilized eggs allowed for the one-step generation of conditional mutant mice. In addition, we show that the introduction of two spaced sgRNAs targeting the Mecp2 gene can produce mice carrying defined deletions of about 700 bp. Though all RNA and DNA constructs were injected into the cytoplasm or nucleus of zygotes, the gene modification events could happen at the one-cell stage or later. Indeed, Southern analyses revealed mosaicism in 17% (1/6) to 40% (20/49) of the targeted mice and ES cell lines indicating that the insertion of the transgenes had occurred after the zygote stage ( Table S2).

More…

In summary, CRISPR/Cas-mediated genome editing represents an efficient and simple method of generating sophisticated genetic modifications in mice such as conditional alleles and endogenous reporters in one step. The principles described in this study could be directly adapted to other mammalian species, opening the possibility of sophisticated genome engineering in many species where ES cells are not available.

Multiplexed activation of endogenous genes by CRISPR-on, an RNA-guided transcriptional activator system

Albert W Cheng1,2,*, Haoyi Wang1,*, Hui Yang1, Linyu Shi1, Yarden Katz1,3, Thorold W Theunissen1, Sudharshan Rangarajan1, Chikdu S Shivalila1,4, Daniel B Dadon1,4 and Rudolf Jaenisch1,4
Cell Research (2013) 23:1163–1171. http://dx.doi.org:/10.1038/cr.2013.122

Technologies allowing for specific regulation of endogenous genes are valuable for the study of gene functions and have great potential in therapeutics. We created the CRISPR-on system, a two-component transcriptional activator consisting of a nuclease-dead Cas9 (dCas9) protein fused with a transcriptional activation domain and single guide RNAs (sgRNAs) with complementary sequence to gene promoters. We demonstrate that CRISPR-on can efficiently activate exogenous reporter genes in both human and mouse cells in a tunable manner. In addition, we show that robust reporter gene activation in vivo can be achieved by injecting the system components into mouse zygotes. Furthermore, we show that CRISPR-on can activate the endogenous IL1RNSOX2, and OCT4genes. The most efficient gene activation was achieved by clusters of 3-4 sgRNAs binding to the proximal promoters, suggesting their synergistic action in gene induction. Significantly, when sgRNAs targeting multiple genes were simultaneously introduced into cells, robust multiplexed endogenous gene activation was achieved. Genome-wide expression profiling demonstrated high specificity of the system.

Gene expression is strictly controlled in many biol-ogical processes, such as development and diseases. Transcription factors regulate gene expression by binding to specific DNA sequences at the enhancer and promoter regions of target genes, and modulate transcription through their effector domains1. Based on the same principle, artificial transcription factors (ATFs) have been generated by fusing various functional domains to a DNA binding domain engineered to bind to the genes of interest, thereby modulating their expression2,3. The capability of regulating endogenous gene expression using ATFs may facilitate the study of the transcriptional network underlying complex biological processes and provide new therapeutic options for diseases. Significant efforts and progress have been made to engineer DNA binding domains with defined specificities. The decipherment of the “code” of DNA binding specificity of zinc finger proteins and transcription activator-like effectors (TALE) has led to the rational design of DNA binding domains to recognize specific nucleotides with certain probability4,5,6,7,8,9,10. However, binding specificity of these ATFs is usually degenerate, can be difficult to predict and the complex and time-consuming design and generation limits their applications. To study the transcriptional network in a systematic manner, regulating multiple endogenous genes is required, prompting the development of efficient technology for simultaneous regulation of multiple endogenous genes.

CRISPR (clustered regularly interspaced short palin-dromic repeat) and Cas (CRISPR-associated) proteins are utilized by bacteria and archea to defend against viral pathogens11,12. Because the binding of Cas protein is guided by the simple base-pair complementarities between the engineered single guide RNA (sgRNA) and a target genomic DNA sequence, Cas9 could be directed to specific genomic locus or multiple loci simultaneously, by providing the engineered sgRNAs13,14,15,16,17,18,19,20. A recent study described the CRISPRi (CRISPR interference) system, in which the nuclease-deficient dCas9 (D10A; H840A) proteins blocked the transcription apparatus when directed to promoters or gene bodies in bacteria21. A subsequent study demonstrated a more efficient gene repression in eukaryotes by dCas9 fused with a transcription repression domain or exogenous transgene activation when fused with an activation domain22. Two most recent studies showed single endogenous gene activation using dCas9-based activators9,10. To what extent multiple endogenous genes could be regulated simultaneously has not been explored. In this study we report the generation of an RNA-programmable CRISPR-on system, which enables the simultaneous activation of multiple endogenous genes with a defined stoichiometry.

We show here that the CRISPR-on system can be used for the simultaneous induction of at least three different endogenous genes. More significantly, we demonstrated that the stoichiometry of gene induction of multiple genes can be tuned by adjusting the relative amount of their cognate sgRNAs. Simultaneous activation of multiple endogenous genes with defined stoichiometry opens up novel opportunities for systems biology as it allows for the predictable manipulation of transcriptional networks.

Finally, with the ease of design and synthesis, a library of sgRNAs could be generated. When introduced into a cell line constitutively expressing dCas9 activator, gene activation screens mediated by RNA (RNAa) could be achieved. As the specificity components (sgRNA) can be separately designed and constructed from the effector component (Cas fusion proteins), the same library of sgRNAs could be used with different dCas9 fusions (e.g., VP160 domain for transactivation, KRAB domain for transcriptional repression, chromatin modifier domains for specific histone modification) to exert different functions at particular genomic loci.

  1. Spitz F, Furlong EE. Transcription factors: from enhancer binding to developmental control. Nat Rev Genet 2012; 13:613–626. | Article | PubMed | CAS |
  2. Blancafort P, Segal DJ, Barbas CF 3rd. Designing transcription factor architectures for drug discovery. Mol Pharmacol 2004; 66:1361–1371. | Article | PubMed | ISI | CAS |
  3. Sera T. Zinc-finger-based artificial transcription factors and their applications. Adv Drug Deliv Rev 2009; 61:513–526. | Article | PubMed | ISI | CAS |
  4. Beerli RR, Segal DJ, Dreier B, Barbas CF 3rd. Toward controlling gene expression at will: specific regulation of the erbB-2/HER-2 promoter by using polydactyl zinc finger proteins constructed from modular building blocks. Proc Natl Acad Sci USA 1998; 95:14628–14633. | Article | PubMed | CAS |
  5. Beerli RR, Dreier B, Barbas CF 3rd. Positive and negative regulation of endogenous genes by designed transcription factors. Proc Natl Acad Sci USA 2000; 97:1495–1500. | Article | PubMed | CAS |
  6. Zhang F, Cong L, Lodato S, Kosuri S, Church GM, Arlotta P. Efficient construction of sequence-specific TAL effectors for modulating mammalian transcription. Nat Biotechnol 2011; 29:149–153. | Article | PubMed | ISI | CAS |
  7. Moscou MJ, Bogdanove AJ. A simple cipher governs DNA recognition by TAL effectors. Science 2009; 326:1501. | Article | PubMed | ISI | CAS |
  8. Boch J, Scholze H, Schornack S, et al. Breaking the code of DNA binding specificity of TAL-type III effectors. Science 2009; 326:1509–1512. | Article | PubMed | ISI | CAS |
  9. Maeder ML, Linder SJ, Reyon D, et al. Robust, synergistic regulation of human gene expression using TALE activators. Nat Methods 2013; 10:243–245. | Article | PubMed | CAS |
  10. Perez-Pinera P, Ousterout DG, Brunger JM, et al. Synergistic and tunable human gene activation by combinations of synthetic transcription factors.Nat Methods 2013; 10:239–242. | Article | PubMed | CAS |
  11. Bhaya D, Davison M, Barrangou R. CRISPR-Cas systems in bacteria and archaea: versatile small RNAs for adaptive defense and regulation. Annu Rev Genet 2011; 45:273–297. | Article | PubMed | CAS |
  12. Wiedenheft B, Sternberg SH, Doudna JA. RNA-guided genetic silencing systems in bacteria and archaea. Nature 2012; 482:331–338. | Article | PubMed | CAS |

….

Our long-range goals are to understand epigenetic regulation of gene expression in mammalian development and disease. An important question is to understand the different epigenetic conformations that distinguish differentiated cell states and to define strategies to transdifferentiate one differentiated cell type into another. Embryonic stem cells are of major significance because they have the potential to generate any cell type in the body and, therefore, are of great interest for regenerative medicine. A major focus of our work is to understand the molecular mechanisms that allow the reprogramming of somatic cells to an embryonic pluripotent state and to use the potential of patient specific pluripotent cells to study complex human diseases.

http://www.fiercebiotech.com/press-releases/fiercebiotech-names-crispr-therapeutics-one-its-fierce-15-biotech-companies?

Elizabeth Pennisi

Three years ago, no one knew or cared about much about a protein called Cpf1 produced by a bacterial gene. Now, it shows potential for making a fast-developing genome editing technique called CRISPR easier and more accurate. Bioinformaticians identified this protein and its potential connection to CRISPR by scanning the public database of genome sequences. Their colleagues now show that two of 16 versions of this protein tested can delete a gene in a human cell. Cpf1 has other advantages as well-being smaller than one of the popular Cas9 proteins used and depending on a smaller piece of RNA to find its target DNA. But its utility for editing genomes of human and other cells needs further testing.

Read Full Post »

Lonely Receptors: RXR – Jensen, Chambon, and Evans

Larry H. Bernstein, MD, FCAP, Curator

Leaders in Pharmaceutical Intelligence

Series E. 2; 7.2

 

Nuclear receptors provoke RNA production in response to steroid hormones

Albert Lasker Basic Medical Research Award

Pierre Chambon, Ronald Evans and Elwood Jensen

For the discovery of the superfamily of nuclear hormone receptors and elucidation of a unifying mechanism that regulates embryonic development and diverse metabolic pathways.

Hormones control a vast array of biological processes, including embryonic development, growth rate, and body weight. Scientists had known since the early 1900s that tiny hormone doses dramatically alter physiology, but they had no idea that these signaling molecules did so by prodding genes. The 1950s, when Jensen began his work, was the great era of enzymology. Conventional wisdom held that estradiol—the female sex hormone that instigates growth of immature reproductive tissue such as the uterus—entered the cell and underwent a series of chemical reactions that produced a particular compound as a byproduct. This compound—NADPH—is essential for many enzymes’ operations but its small quantities normally limit their productivity. A spike in NADPH concentrations would stimulate growth or other activities by unleashing the enzymes, the reasoning went.

In 1956, Jensen (at the University of Chicago) decided to scrutinize what happened to estradiol within its target tissues, but he had a problem: The hormone is physiologically active in minute quantities, so he needed an extremely sensitive way to track it. He devised an apparatus that tagged it with tritium—a radioactive form of hydrogen—at an efficiency level that had not previously been achieved. This innovation allowed him to detect a trillionth of a gram of estradiol.

When he injected this radioactive substance into immature rats, he noticed that most tissues—skeletal muscle, kidneys and liver, for example—started expelling it within 15 minutes. In contrast, tissues known to respond to the hormone—those of the reproductive tract—held onto it tightly. Furthermore, the hormone showed up in the nuclei of cells, where genes reside. Something there was apparently grabbing the estradiol.

Jensen subsequently showed that his radioactive hormone remained chemically unchanged once inside the cell. Estrogen did not act by being metabolized and producing NADPH, but presumably by performing some job in the nucleus. Subsequent work by Jensen and Jack Gorski established that estradiol converts a protein in the cytoplasm, its receptor, into a form that can migrate to the nucleus, embrace DNA, and turn on specific genes.

From 1962 to 1980, molecular endocrinologists built on Jensen’s work to discover the receptors for the other major steroid hormones—testosterone, progesterone, glucocorticoids, aldosterone, and the steroid-like vitamin D. In addition to Jensen and Gorski, many scientists—notably Bert O’Malley, Jan-Ake Gustafsson, Keith Yamamoto, and the late Gordon Tompkins—made crucial observations during the early days of steroid receptor research.

Clinical Applications of Estrogen-Receptor Detection

Clinicians knew that removing the ovaries or adrenal glands of women with breast cancer would stop tumor growth in one out of three patients, but the molecular basis for this phenomenon was mysterious. Jensen showed that breast cancers with low estrogen-receptor content do not respond to surgical treatment. Receptor status could therefore indicate who would benefit from the procedure and who should skip an unnecessary operation. In the mid-1970s, Jensen and his colleague Craig Jordan found that women with cancers that contain large amounts of estrogen receptor are also likely to benefit from tamoxifen, an anti-estrogen compound that mimics the effect of removing the ovaries or adrenal glands. The other patients—those with small numbers of receptors—could immediately move on to chemotherapy that might combat their disease rather than waiting months to find out that the tumors were growing despite tamoxifen treatment. By 1980, Jensen’s test had become a standard part of care for breast cancer patients.

In the meantime, Jensen set about generating antibodies that bound the receptor—a tool that provided a more reliable way to measure receptor quantities in excised breast tumor specimens. His work has transformed the treatment of breast cancer patients and saves or prolongs more than 100,000 lives annually.

Long-Lost Relatives

By the early 1980s, interest in molecular endocrinology had shifted toward the rapidly developing area of gene control. Chambon and Evans had long wondered how genes turn on and off, and recognized nuclear hormone signaling as the best system for studying regulated gene transcription. They wanted to know exactly how nuclear receptors provoke RNA production in response to steroid hormones. To manipulate and analyze the receptors, they would need to isolate the genes for them.

By late 1985 and early 1986, Evans (at the Salk Institute in La Jolla) and Chambon (at the Institute of Genetics and Molecular and Cellular Biology in Strasbourg, France) had pieced together the glucocorticoid and estrogen receptor genes, respectively. They noticed that the sequences resembled that of v-erbA, a miscreant viral protein that fosters uncontrolled cell growth. This observation raised the possibility that v-erbA and its well-behaved cellular counterpart, c-erbA, would also bind DNA and control gene activity in response to some chemical activator, or ligand. In 1986, Evans and Björn Vennström simultaneously reported that c-erbA was a thyroid hormone receptor that was related to the steroid hormone receptors, thus uniting the fields of thyroid and steroid biology.

Chambon and Evans set to work deconstructing the glucocorticoid and estrogen receptors. By creating mutations at different spots and probing which activities the resulting proteins lost, they dissected the receptor into three domains: one bound hormone, one bound DNA, and one activated target genes. The structure of each domain strongly resembled the analogous one in the other receptor.

Chambon and Evans wanted to match other members of the growing receptor gene family with their chemical triggers. Because the DNA- and ligand-binding regions functioned independently, it was possible to hook the DNA-binding domain of, say, the glucocorticoid receptor to the ligand-binding domain of another receptor whose ligand was unknown. The ligand for that receptor would then activate a glucocorticoid-responsive test gene.

Evans would use this method to identify ligands for several novel members of the nuclear receptor family, and both he and Chambon exploited it to discover a physiologically crucial receptor. In the late 1970s, scientists had suggested that the physiologically active derivative of vitamin A, retinoic acid, could exert its effects by binding to a nuclear receptor. This nutrient is essential from fertilization through adulthood, and researchers were eager to understand its activities on a molecular level. During embryonic development, deficiency of retinoic acid impairs formation of most organs, and the compound can hinder cancer cell proliferation. So Chambon set out to find a receptor that responded to retinoic acid. He isolated a member of the nuclear receptor gene family whose production increased in breast cancer cells that slowed their growth upon exposure to the chemical. Simultaneously, Evans identified the same protein. He tested whether more than a dozen compounds activated an unknown receptor and one passed: retinoic acid.

Remarkably, in 1986, the two scientists had independently—and unbeknownst to each other—identified the same retinoic acid receptor, a molecule of tremendous significance. The discovery of this molecule provided an entry point for detailing vitamin A biology.

Rx for Lonely Receptors: RXR

The list of presumptive nuclear receptors was growing quickly as scientists realized that the common DNA sequences provided a handle with which to grab these molecules from the genome. Because their chemical activators weren’t known, they were called “orphan” receptors, and researchers were keen on “adopting” them to ligands. Some of these ligands, they reasoned, would represent previously unknown classes of gene activators. The test system that Chambon and Evans used to match up retinoic acid with its receptor, in which they stitched an unknown ligand-binding domain to a DNA-binding domain for a receptor with known target sequences, could be harnessed to accomplish this task.

Evans had identified some potential nuclear receptors from fruit flies. He decided to pursue a human orphan receptor that closely resembled one of these receptor genes, reasoning that a protein that functioned in both flies and mammals was likely to perform an important job.

This receptor responded to retinoic acid in intact cells but did not bind it in the test tube, so Evans called it the Retinoid X Receptor (RXR), thinking that its ligand was some retinoic acid derivative. In cells, enzymes convert retinoic acid to metabolites and it seemed possible that one of these compounds was RXR’s ligand. In 1992, Evans’s group and one at Hoffmann-La Roche discovered that 9-cis-retinoic acid, a stereoisomer of retinoic acid, could activate RXR, identifying the first new receptor ligand in 25 years. This finding launched the orphan receptor field because it provided strong evidence that the strategy could unearth previously unknown ligands.

In the meantime, Chambon had found that the purified retinoic acid receptor, in contrast to the estrogen receptor, did not bind efficiently to its target DNA. Other nuclear receptors, too, needed help grasping genes. In the test tube, the retinoic acid, thyroid hormone, and vitamin D3 receptors could attach well to their target DNA only when supplemented with cellular material, which presumably contained some crucial substance. Chambon and Michael Rosenfeld independently purified a single protein that performed this feat, and it turned out to be none other than RXR. This ability of RXR to pair with other receptors—forming so-called heterodimers—would turn out to be key for switching on many orphan receptors. These heterodimeric couplings yield large numbers of distinct gene-controlling entities.

Chambon revealed the power of mixing and matching in these molecular duos through his thorough and extensive genetic manipulations in mice. He has shown that vitamin A exerts its wide-ranging effects on organ development in the embryo through the action of eight different forms of the retinoic acid receptor and six different forms of RXR, interacting with each other in a multitude of combinations.

Clinical Applications of the Superfamily Work

The concept of RXR as a promiscuous heterodimeric partner for certain nuclear receptors led to the unexpected identification of a number of clinically relevant receptors. These proteins include the peroxisome proliferator-activated receptor (PPAR), which stimulates fat-cell maturation and sits at the center of Type 2 diabetes and a number of lipid-related disorders; the liver X receptors (LXRs) and bile acid receptor (FXR), which help manage cholesterol homeostasis; and the steroid and xenobiotic receptor (PXR), which turns on enzymes that dispose of chemicals that need to be detoxified, such as drugs.

Because the nuclear receptors wield such physiological power, they have provided excellent targets for disease treatment. The anti-diabetes compounds glitazones, for example, work by stimulating PPAR, and the clinically used lipid-lowering medications called fibrates work by binding a closely related receptor, PPAR. Retinoic acid therapy has dramatically altered the prognosis of people with acute promyelocytic leukemia by triggering specialization of the immature white blood cells that accumulate in these individuals. The three-dimensional structure of nuclear receptors with and without their ligands, which Chambon and his colleagues first solved, promises to accelerate drug discovery in the whole field.

Nuclear hormone receptors have touched on human health in other ways as well. Genetic perturbations in the genes for these proteins cause a variety of illnesses. For example, certain forms of rickets arise from mutations in the vitamin D receptor and several disorders of male sexual differentiation stem from defects in the androgen receptor.

The discoveries of Jensen, Chambon, and Evans revealed an unimagined superfamily of proteins. At the start of this work almost 50 years ago, no one would have anticipated that steroids, thyroid hormone, retinoids, vitamin D, fatty acids, bile acids, and many lipid-based drugs transmit their signal through similar pathways. Four dozen human nuclear receptors are now known, and scientists are working out the roles of these proteins in normal and aberrant physiology. These discoveries have revolutionized the fields of endocrinology and metabolism, and pointed toward new tactics for drug discovery.

by Evelyn Strauss, Ph.D.

 

The 2004 Lasker Award for Basic Medical Research will be presented to Elwood Jensen, Ph.D., the Charles B. Huggins Distinguished Service Professor Emeritus in the Ben May Institute for Cancer Research at the University of Chicago, one of three scientists whose discoveries “revolutionized the fields of endocrinology and metabolism,” according to the award citation. Jensen’s work had a rapid, direct and lasting impact on treatment and prevention of breast cancer.

The Lasker Awards are the nation’s most distinguished honor for outstanding contributions to basic and clinical medical research. Often called “America’s Nobels,” the Lasker Award has been awarded to 68 scientists who subsequently went on to receive the Nobel Prize, including 15 in the last 10 years.

Jensen will share the basic medical research award with two colleagues, Pierre Chambon, of the Institute of Genetics and Molecular and Cellular Biology (Strasbourg, France), and Ronald M. Evans of the Salk Institute for Biological Studies (La Jolla, California) and the Howard Hughes Medical Institute.

They were selected for their discovery of the “superfamily of nuclear hormone receptors and the elucidation of a unifying mechanism that regulates embryonic development and diverse metabolic pathways.” The implications of this research for understanding human disease and accelerating drug discovery “have been profound and hold much promise for the future,” notes the announcement from the Lasker Foundation.

Jensen is being honored for his pioneering research on how steroid hormones, such as estrogen, exert their influence. His discoveries explained how these hormones work, which has led to the development of drugs that can enhance or inhibit the process.

Hormones control a vast array of biological processes, including embryonic development, growth rate and body weight. Before Jensen, however, the way which hormones cause these effects was “a complete mystery,” recalled Gene DeSombre, Ph.D., professor emeritus at the University of Chicago, who worked with Jensen in the Ben May Institute as a post-doctoral fellow and then as a colleague.

In the 1950s, biochemists thought a hormone entered a cell, where a series of oxidation and reductions reactions with the estrogen provided needed energy for the growth stimulation and other specific actions shown by estrogens.

From the late 1950s to the 1970s Jensen entirely overturned that notion. Working with estrogen, he proved that hormones do not undergo chemical change. Instead, they bind to a receptor protein within the cell. This hormone-receptor complex then travels to the cell nucleus, where it regulates gene expression.

At the time, this idea was heresy. “That really got him into some hot water,” recalled DeSombre. “Jensen struggled quite a lot,” echoes Shutsung Liao, Ph.D., another Ben May colleague, who subsequently found a similar system for testosterone action. But for Jensen, just getting into hot water was a struggle. When he first presented preliminary data at a 1958 meeting in Vienna, only five people attended, three of whom were the other speakers. More than 1,000 attended a simultaneous symposium on the metabolic processing of estrogen.

In the next 20 years, Jensen convinced his colleagues by publishing a series of major and highly original discoveries in four related areas of hormone research:

  • Jensen discovered the estrogen receptor, the first receptor found for any hormone. In 1958, using a radioactive marker, he showed that only the tissues that respond to estrogen, such as those of the female reproductive tract, were able to concentrate injected estrogen from the blood. This specific uptake suggested that these cells must contain binding proteins, which he called “estrogen receptors.”
  • In 1967, Jensen and Jack Gorski of the University of Wisconsin showed that these putative receptors were macromolecules that could be extracted from these tissues. With this method, Jensen showed that when estrogen bound to this receptor, the compound then migrated to the nucleus where it bound avidly and activated specific genes, stimulating new RNA synthesis.
  • By 1968, Jensen had devised a reliable test for the presence of estrogen receptors in breast cancer cells. It had been known for decades that about one-third of premenopausal women who had advanced breast cancer would respond to estrogen blockade brought about by removing their ovaries, the source of estrogen, but there was no way to predict which women would respond. In 1971, Jensen showed that women with receptor-rich breast cancers often have remissions following removal of the sources of estrogen, but cancers that contain few or no estrogen receptors do not respond to estrogen-blocking therapy.
  • By 1977, Jensen and Geoffrey Greene, Ph.D., also in the University of Chicago’s Ben May Institute, had developed monoclonal antibodies directed against estrogen receptors, which enabled then to quickly and accurately detect and count estrogen receptors in breast and other tumors. By 1980, this test had become a standard part of care for breast cancer patients

This work “transformed the treatment of breast cancer patients,” notes the Lasker Foundation, “and saves or prolongs more than a 100,000 lives annually.”

”Jensen’s revolutionary discovery of estrogen receptors is beyond doubt one of the major achievements in biochemical endocrinology of our time,” said DeSombre. “His work is hallmarked by great technical ingenuity and conceptual novelty. His promulgation of simple yet profound ideas concerning the role of receptors in estrogen action have been of the greatest importance for research on the basic and clinical physiology not only of estrogens but also of all other categories of steroid hormones.”

By the early 1970s, Jensen was searching for chemical, rather than surgical, ways to shield estrogen-dependent tumors from circulating hormones. He and colleague Craig Jordan (then at the Worcester Foundation for Experimental Biology in Massachusetts) subsequently found that women with cancers that contain large amounts of estrogen receptor are also likely to benefit from tamoxifen, a compound that blocks some of the effects of estrogen. Patients with few or no receptors could immediately move on to chemotherapy rather than waiting months to find out that the tumors were growing despite tamoxifen treatment.

Following Jensen’s lead, researchers soon found that the receptors for the other major steroid hormones, such as testosterone, progesterone, and cortisone, worked essentially the same way.

In 1986, Pierre Chambon and Ronald Evans separately but simultaneously discovered that the steroid hormone receptors were merely the tip of the iceberg of what would turn out to be a large family of structurally related nuclear receptors, now known to consist of 48 members. Evans and Chambon unearthed a number of these receptors, which revealed new regulatory systems that control the body’s response to essential nutrients (such as Vitamin A), fat-soluble signaling molecules (such as fatty acids and bile acids), and drugs (such as the glitazones used to treat Type 2 diabetes and retinoic acid for certain forms of acute leukemia).

These three individuals “created the field of nuclear hormone receptor research, which now occupies a large area of biological and medical investigation,” said Dr. Joseph L. Goldstein, chairman of the international jury of researchers that selects recipients of the Lasker Awards, and recipient of the Lasker Award for Basic Medical Research and the Nobel Prize in Medicine in 1985.

They revealed the “unexpected and unifying mechanism by which many signaling molecules regulate a plethora of key physiological pathways that operate from embryonic development through adulthood. They discovered a family of proteins that allows chemicals as diverse as steroid hormones, Vitamin A, and thyroid hormone to perform in the body.”

Jensen, known for concluding his lectures in verse, neatly summed up what his extraordinary series of discoveries might mean to a woman who has been diagnosed with breast cancer:

“A lady with growth neoplastic
Thought surgical ablation too drastic.
She preferred that her ill
Could be cured with a pill,
Which today is no longer fantastic.”

JBC THEMATIC MINIREVIEW SERIES 2011

Nuclear Receptors in Biology and Diseases

Thematic Minireview Series on Nuclear Receptors in Biology and Diseases

Sohaib Khan and Jerry B Lingrel

Although a connection between breast cancer and the ovary was made by Sir George Beatson in 1896 and estrogen was purified in 1920, it remained puzzling as to how the hormone exerted its biological effects. In the late 1950s, when Elwood Jensen delved into this problem by asking, essentially, “What does tissue do with this hormone?” little did he know that his quest would lead to the establishment of the nuclear receptor field. The late 1950s was the era of intermediary metabolism and enzymology, when steroid hormones were considered likely substrates in the formation of metabolites that functioned as cofactors in an essential metabolic pathway. The biological responses to estrogens and other steroids were thought to be mediated by enzymes. Against this background and prevailing dogma, Jensen and colleagues defined the biochemical mechanisms by which steroid hormones exert their effects. While working at the University of Chicago’s Ben May Institute for Cancer Research, they synthesized tritium-labeled estradiol and concurrently developed a new method to measure its uptake in biological material. These tools enabled them to determine the biochemical fate of physiological amounts of hormone. They discovered that the reproductive tissues of the immature rat contain characteristic hormone-binding components with which estradiol reacts to induce uterine growth without itself being chemically changed. From the close correlation between the inhibition of binding and inhibition of growth response, Jensen established that the binding substances were receptors. Thus, we saw the birth of the first member of the nuclear receptor family (known as the estrogen receptor). These findings stimulated the search for other physiological receptors, and the pioneering works by Pierre Chambon, Ronald Evans, Jan-Åke Gustafsson, Bert W. O’Malley, and Keith Yamamoto led to the discoveries of the glucocorticoid receptor (GR),2 progesterone receptor, retinoic acid receptor, and orphan receptors. In a rather short span of time, the nuclear receptor family has grown into a 49-member-strong “superfamily.” This is a family whose members, functioning as sequence-specific transcription factors, have defined the many intricacies of the mechanism of transcription. These ligand-dependent transcription factors generally possess similar “domain organizations,” of which the DNA-binding domain and the ligand-binding domain are critical in amplifying the hormonal signals via the receptor target genes. The nuclear receptor family is divided into four groups: (i) Group 1 is composed of steroid hormone receptors that control target gene transcription by binding as homodimers to response element (RE) palindromes; (ii) in Group 2, the nuclear receptors heterodimerize with retinoid X receptor and generally bind to direct repeat REs; (iii) Group 3 consists of those orphan receptors that function as homodimers and bind to direct repeat REs; and (iv) orphan receptors in Group 4 function as monomers and bind to single REs.

Since the early demonstration by Jack Gorski and Jensen that the estrogen receptor (ER) activates transcription, the nuclear receptor field has come a long way. In addition to the first cloning of the polymerase II transcription factors (GR and ER cDNAs), of note is the discovery of steroid receptor coactivators (SRCs), a truly major piece of the transcriptional jigsaw puzzle, described by the laboratories of O’Malley and Myles Brown. The induction of coactivators and corepressors in the transcriptional machinery has expanded tremendously our understanding of this complex process. We now know that ligand binding to the respective receptors triggers a fascinating chain of events, including the translocation of the receptors to the nucleus, ligand-induced changes in the receptor conformations, receptor dimerization, interaction with the target gene promoter elements, recruitment of coactivators (or corepressors), chromatin remodeling, and subsequent interaction with the polymerase II complex to initiate transcription.

By virtue of their abilities to regulate a myriad of human developmental and physiological functions (reproduction, development, metabolism), nuclear receptors have been implicated in a wide range of diseases, such as cancer, diabetes, obesity, etc. Not surprisingly, drug companies are spending billions of dollars to develop medicines for cancer and metabolic disorders that involve nuclear receptors. More than 50 years after the discovery of the ER, the scientific community owes Jensen and other founding members of the nuclear receptor family much gratitude, for they have taken us through a remarkable expedition filled with eureka moments to understand how hormones and other ligands function!

This thematic minireview series will cover a range of topics in the nuclear receptor field. The minireviews include the current studies of identifying subtypes of the GR. Different receptors arise from alternative mRNA splicing and from the use of different promoter start sites and post-translational modifications, such as phosphorylation. The series covers the physiological roles of the different GRs. The field of orphan nuclear receptors and the search for possible ligands also are reviewed. One minireview concentrates largely on the following nuclear receptors: peroxisome proliferator-activated receptor (PPAR) α, PPARγ, Rev-erbα, and retinoic acid receptor-related orphan receptor α. ERα was the first identified and has been studied the most, whereas ERβ has not been studied in the same detail. ERβ is very important, and one of the minireviews provides a summary of the new biological functions that are being ascribed to it. Also, the development of small molecule inhibitors for the ER will be considered. An important aspect of nuclear receptor function is how these receptors function in transcription. The role of transcriptional coactivators in nuclear receptor gene regulation will be reviewed as well as how signal amplification and interaction are involved in transcription regulation by steroids. The SRC/p160 family of coregulators includes SRC-1, SRC-2, and SRC-3, and the latter has been shown to act as an oncogene, particularly in breast cancer. Molecular analysis of its role in breast cancer progression and metastasis will be the focus of one of the minireviews. In addition, interactions of nuclear receptors with the genome will be reviewed, as will the role of the homeodomain protein HoxB13 in specifying the cellular response to androgens. Mining nuclear receptor cistromes and how nuclear receptors reset metabolism also will be considered. The association of nuclear receptors (e.g. PPARδ) with physiological functions, such as circadian rhythm and muscle functions, will also be addressed. Finally, the role of nuclear receptors in disease using the retinoid X receptor α/β knock-out and transgenic mouse model skin syndromes and asthma will be reviewed. These are diverse and important topics that are critical in understanding the regulation of nuclear receptors and the biological roles they play in normal function and disease.

The Nuclear Receptor Superfamily: A Rosetta Stone for Physiology

Ronald M. Evans
Howard Hughes Medical Institute, Gene Expression Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037
Molecular Endocrinology 19(6):1429–143   http://dx.doi.org:/10.1210/me.2005-0046

In the December 1985 issue of Nature, we described the cloning of the first nuclear receptor cDNA encoding the human glucocorticoid receptor (GR) (1). In the 20 yr since that event, our field has witnessed a quantum leap by the subsequent discovery and functional elaboration of the nuclear receptor superfamily (2)—a family whose history is linked to the evolution of the entire animal kingdom and whose actions, by decoding the genome, span the vast diversity of biological functions from development to physiology, pathology, and treatment. A messenger is an envoy or courier charged with transmitting a communication or message. In one sense, the cloning of that first messenger (the GR) represented the completion of a prediction that began with Elwood Jensen’s characterization of the first steroid receptor protein (3) and continued with the pioneering work of others in the steroid receptor field (including Gorski, O’Malley, Gustafsson, and Yamamoto). Yet, like the discovery of the Rosetta stone in 1799, the revelation of the GR sequence heralded a completely unpredictable demarcation in the field, helping to solve mysteries unearthed nearly 100 yr ago as well as opening a portal to the future. The beginnings of the adventure lie in disciplines such as medicine and nutrition, which gave rise to the emergent field of endocrinology in the first half of the last century. The purification of chemical messengers ultimately known as hormones from organs and vitamins from foods spurred the study of these compounds and their physiologic effects on the body. At about the same time, the field of molecular biology was emerging from the disciplines of chemistry, physics, and their application to biological problems such as the structure of DNA and the molecular events surrounding its replication and transcription. It would not be until the late 1960s and 1970s that endocrinology and molecular biology would begin to intersect as the link between receptors and transcriptional control were being laid down. During this time, the work of Jensen (4) and Gorski (5) identified a high-affinity estrogen receptor (ER) that suggested an action in the nucleus. Gordon Tomkins and his associates (J. Baxter, G. Ringold, E. B. Thompson, H. Samuels, H. Bourne, and others) were one of the most creative forces studying glucocorticoid action (6). Concurrent work by O’Malley, Gustafsson, and Yamamoto provided further, important evidence supporting a link between steroid receptor action and transcription (see accompanying perspective articles in this issue of Molecular Endocrinology). But whereas the steroid hormone field continued to evolve in this direction, it is of interest to note that the mechanism of action of thyroid hormone and retinoids remained clouded and controversial until the eventual cloning of their receptors in the late 1980s. Likewise, no one had foreseen the possibility that other lipophilic molecules (like oxysterols, bile acids, and fatty acids) would also function through a similar mechanism, or that other steroid receptor-like proteins existed that would play an important role in transcriptional regulation of so many diverse pathways. Thus, the GR isolation in 1985 led to the concept of a hidden superfamily of receptors that in a very real way provided the needed molecular code to unravel the puzzle of physiologic homeostasis.

Unconventional Gene-Ology

The study of RNA tumor viruses was ascendant, and the concept that they evolved by pirating key signaling pathways greatly influenced my future studies. With this training, I went on to work with Jim Darnell at the Rockefeller University on adenovirus transcription, a model brought to the lab by Lennart Philipson. At the time, adenovirus was one of the best tools to study programmed gene expression in an animal cell. My sole focus was to localize the elusive major late promoter, which provided my first Nature paper (7). Ed Ziff, a newly hired assistant professor from Cambridge, brought innovative unpublished DNA and RNA sequencing techniques that, after much technical angst, allowed us to sequence the major late promoter and derive the structure of the first eukaryotic polymerase II promoter (8). This thrilling result convinced me that the problem of gene control could be solved at the molecular level. Our next goal, which I shared with Michael Harpold in the Darnell lab, was to translate the concepts developed around adenovirus into cellular systems. My model was to analyze the glucocorticoid and thyroid hormone regulation of the GH gene. Under the strict federal guidelines for newly approved recombinant DNA research, we cloned the GH cDNA in 1977 and the first genomic clones in 1978 (9) after I moved on to The Salk Institute. However, to fully address the hormone signaling problem, I realized that it would be necessary to clone the GR and thyroid hormone receptors (TRs), which began in earnest in 1981. Up until that time, the purification and cloning of any polymerase II transcription factor had eluded researchers because of their low abundance. Four years later, the GR would be the first transcription factor for a defined response element to be cloned, sequenced, and functionally identified.

A Rock and A Hard Place

A key question was whether the GR protein encoded by the receptor was sufficient, when expressed in a heterologous cell, to convey the hormonal message. Before the publication, a new postdoc, Vincent Giguere, began tinkering with the isolated GR, trying to address this question. The rate of development of any field is limited by the existing techniques and depends on the development of new ones. Vincent devised a revolutionary technique—the cotransfection assay that required two plasmids to be taken up in the same cell, the expression vector to be transcribed, the encoded protein to be functional and an inducible promoter linked to a chloramphenicol acetyltransferase reporter in the nucleus ready to flicker on (10, 12). With so many variables and unknowns, I was stunned and expressionless when it worked the very first time. Cotransfection was an easy, fast, and quantitative technique. It would become (and still remains) the dominant assay to characterize receptor function. It would also become the mainstay for drug discovery in the pharmaceutical industry. The development of this technique proved a great advantage because existing technology involved creating stable cell lines, a tedious process prone to integration artifacts that ultimately could not match the explosive pace of the field. Indeed, within 4 months Stan and Vincent had fully characterized 27 insertional mutants delineating the DBD, LBD, and two activation domains (12). The route to understanding the signaling mechanism now had a solid structural foundation. A serendipitous gift to my retroviral origins was the homology of the GR sequence to the v-erbA oncogene product of the avian erythroblastosis virus genome (13). With this discovery, erbA advanced to a candidate nuclear transcription factor potentially involved in a signal transduction pathway. Thus, while Stan concentrated on the GR, Cary began to delve into the erbA discovery. Within months of the GR publication, the human c-erbA gene was in hand (14). Unbeknownst to us, Bjorn Vennstrom, one of the first to characterize the avian erythroblastosis virus genome, had also isolated c-erbA and was searching for a function. Based on the low homology of the LBD region to the GR and ER, both groups deduced that the imaginary erbA ligand would be nonsteroidal.

The work of our two groups (15, 16), published in December of 1986, broadened the principles of the signal transduction pathway by demonstrating that thyroid and steroid hormone receptor signaling had a common evolutionary origin and provided an entree to understand how mutations within a receptor could activate it to an oncogene. Although we did not know it at the time, this work would also lead us to the concept of the corepressor. In the meantime, my student, Catherine Thompson, zeroed in on an erb-A-related gene and soon identified a second TR expressed at high levels in the central nervous system (17). Thus came into existence the and forms of the TR. Jeff Arriza, the third graduate student in the lab, purified a genomic fragment that had weakly hybridized to the GR resulting in the isolation of the human mineralocorticoid receptor (MR) (18). MR proved to have an at least 10-fold higher affinity for glucocorticoids than the GR itself and was further distinguished by its ability to bind and be activated by aldosterone. This enabled the development of GR- and MR-selective drugs such as the recent MR antagonist eplerenone. Thus, in a 2-yr time span our lab had progressed on three distinct, albeit related, receptor systems, and in doing so molecular biology and endocrinology were irrevocably linked. The field of molecular endocrinology (and coincidentally the eponymous journal) was born.

Ligands From Stone

I have often been asked how we could handle so many divergent systems. Indeed, from a medical perspective, these systems seem widely unrelated. Studies of ER, progesterone receptor, and androgen receptor (AR) fall under reproductive physiology, vitamin D under bone and mineral metabolism, with vitamin A part of nutritional science. Medical fields are naturally idiosyncratic because of the specialized knowledge required to conduct experiments. With my training as a molecular biologist, physiology was the complex output of genes and thus control of gene expression was the overriding problem. This conceptual approach had a great unifying effect because all receptors transduce their signaling through the gene. As an “outsider,” my goal was to exploit multiple receptor systems to seek general principles. This philosophical approach afforded us a freedom to redefine the signaling problem from the nucleus outward and thus even poorly characterized, even unknown, physiologic systems fell into the crosshairs of our molecular gun.

Vincent, while screening a testes Fig. 1. Models of Nuclear Receptor Structure Top, Original hand-shaped wire model (circa 1992) of the nuclear receptor DBD. Bottom, Schematic representation of the GR DBD. Conserved residues in zinc fingers, P-box and D-box are indicated isolated what would become the vitamin A or retinoic acid receptor (RAR) (19). Initially, Vincent thought he had isolated the AR, although this later proved not to be the case. By that stage, the lab had perfected a new technique—the domain swap—by which the GR DBD could be introduced into any receptor and confers on the chimeric protein the ability to activate a mouse mammary tumor virus reporter. This clever technique, independently developed in the Chambon lab, would prove to be essential. Effectively, the domain swap would enable us to screen for ligands without any knowledge of their physiologic function. Activation of a target gene was all that was needed! By creating this GR chimera, Vincent was able to screen the new receptor against a ligand cocktail including androgens, steroids, thyroid hormone, cholesterol, and the vitamin A metabolite retinoic acid. From the first assay, it was clear that he had isolated a high-affinity selective RAR that had no response to any other test ligand. Thus, without knowing any true direct target gene for retinoic acid, we were nonetheless able to isolate and characterize its receptor. Remarkably, Martin Petkovich in the Chambon lab isolated the same gene. Once again, this is an example where a new technique offered an entirely new approach to a problem. Both papers were published in the December 1987 issue of Nature (19, 20). With the combination of steroids, thyroid hormones, and vitamin A, the three elemental components of the nuclear receptor superfamily were in hand. By the time the RAR papers were published, Vincent with Na Yang, had already isolated two estrogen-related receptors termed ERR1 and 2 that would represent the first true orphan receptors in the evolving superfamily (21). A third receptor (ERR3) would be isolated 10 yr later (22). The three ERRs are distinguished by their ability to activate through ER response elements, but required no ligand. However, of potential major medical relevance, estrogen antagonists such as 4-hydroxy-tamoxifen silences ERR constitutive activity (23). The superfamily was growing exponentially, transforming into a new field, driven by a new breed of exceptional students and fellows attracted by the mechanics of transcription and its emerging link to physiology. For example, the RAR and TR offered an unprecedented look at understanding the action of vitamin A as a morphogen and the role of thyroxin in setting the basal metabolic rate of the body. We were a relatively small group, and our decision to work on multiple different receptor systems created a unique environment. Because there was so little overlap between projects, postdocs and students readily discussed all results, exchanged reagents and freely collaborated, resulting in a tremendous acceleration of progress. The high level of camaraderie was powered by the joie de vivre of the exciting discoveries and the ability of our family of students and postdocs to each adopt their own receptors. We all felt we were in a golden age and even more was to come.

In 1989, Jan Sap in Vennstrom’s group and Klaus Damm in our group demonstrated that the TR becomes oncogenic by mutation in the LBD (24, 25). Although we expected ligand-independent activation, it was clearly a constituitive repressor becoming the first example of a dominant-negative oncogene. The concept of the dominant-negative oncogene had been proposed one year earlier by Ira Herskowitz (26). This discovery changed our thinking on hormone action, and repression soon would be shown to be a common feature of receptor antagonists. David Mangelsdorf, who had arrived in the lab the year before was captivated by the glow of weakly hybridizing DNA bands and, in 1989, had amassed his own collection of orphan receptors, among which was the future retinoid X receptor (RXR) (27). In search for biological activity, a candidate ligand was found in lipid extracts from outdated human blood. However, the key test came from demonstrating that addition of all-trans retinoic acid to cultured cells would lead to its rapid metabolism coupled with the release of an inducing activity for RXR, which we termed retinoid X. David and his benchmate, Rich Heyman, began working on the chemistry of this inducer along with Gregor Eichele and Christine Thaller, then at Baylor College of Medicine (Houston, TX). This work led to the identification of 9-cis retinoic acid by our lab and a group at Hoffman LaRoche (Nutley, NJ) (28, 29). Like the retinal molecule in rhodopsin, 9-cis-retinoic acid represents the exploitation of retinoid isomerization by nature to control a key signaling pathway. More importantly, in the 39 yr since the discovery of aldosterone in 1953, this revelation would reawaken and reinvent the single most defining but dormant tool of endocrinology—ligand discovery. Indeed, the discovery that new receptors could lead to new ligands opened up an entirely new avenue of research. Like the puzzle of the structure of the benzene ring, which was solved in 1890 when Fredrick Kekule dreamed of a snake biting its own tail, the physiologic head of the “endocrine snake” and the molecular biology tail had come full circle. The era of reverse endocrinology was now upon us.

Response Elements: Deciphering The Scripts

One problem in addressing the downstream effects of our newly discovered receptors was that their response elements and target genes were by definition unknown. Kaz Umesono delved into this mystery and would produce a paradigm shift that would both solve the problem and further unify the field. With the view that the DBD functioned as a molecular receptor for its cognate hormone response element, meticulous mutational studies revealed two key DBD sequences, termed the P-box and D-box, that controlled the process (30).

The D-box was shown to direct dimerization, a feature previously thought to be unique to the LBD. One perplexing point was that the P-boxes of the nonsteroidal receptors were conserved, leading to the improbable prediction that many different receptors would recognize the same target sequence. By manual compilation and comparison of all known response elements, Kaz proposed a core hexamer— AGGTCA—as the prototypic common target sequence. By requiring the half-site to be an obligate hexamer an underlying pattern—the direct repeat—emerged. In the direct repeat paradigm, we proposed that half-site spacing, not sequence difference, was the key ingredient to distinguishing the response elements. The metric was referred to as the 3-4-5 rule (31). According to the rule, direct repeats of AGGTCA spaced by three nucleotides, would be a vitamin D response element (DR-3), the same repeat spaced by four nucleotides a thyroid hormone response element (DR-4), and the same repeat spaced by five nucleotides a vitamin A response element (DR-5). Eventually, all steps from 0–5 on the DR ladder would be filled (Fig. 2). The validity of this paradigm was ensured by a crystal structure solved in collaboration with Paul Sigler’s group at Yale (32). Indeed, of the remaining 40 nonsteroidal receptors, all but three can be demonstrated to have a preferred binding site within some component of the direct repeat ladder. Exceptions include SHP and DAX, which lack DBDs, and farnesoid X receptor (FXR) that binds to the ecdysone response element as a palindrome with zero spacing. Kaz’s insight, by drawing commonality from diversity, came to solve a problem that impacted on virtually every receptor. Remarkably, each new receptor in the superfamily could immediately be assigned a place on the ladder. The ladder also provided a simple means to conduct a ligand screening assay in absence of any knowledge of an endogenous target gene. Kaz’s ladder was a turbo charge for the field. The next major advance in the field was the discovery of the RXR heterodimer. Although we knew that retinoid and thyroid receptors required a nuclear competence factor for DNA binding, its identity was unknown. We tested RXR, but our initial experiments were flawed. Of the first four papers describing the discovery, that from Chambon’s lab was most elegant because they simply purified an activity to homogeneity to find RXR (33)! Rosenfeld was first to publish, and Ozato, Pfahl and Kliewer all concurred (34–37). Tony Oro and Pang Yao in our lab soon published that the ecdysone receptor functions as a heterodimer with ultraspiracle, the insect homolog of RXR (38, 39), revealing that the ancient origins of the heterodimer which arose before the divergence of vertebrates and invertebrates.

Reverse Endocrinology: Decoding Physiology

The orphan receptors would transform our view of endocrine physiology with unexpected links to toxicology, nutrition, cholesterol, and triglyceride metabolism as well as to a myriad of diseases including atherosclerosis, diabetes, and cancer. The three RXR isoforms formed the core with 14 heterodimer partners including the vitamin D receptor (VDR), TR/, and RAR//. The initial adopters of orphan receptors included Giguere, Mangelsdorf, Weinberger, Bruce Blumberg, Steve Kliewer, and Barry Forman. Barry unlocked the first secret to for peroxisome proliferator-activated receptor (PPAR) by identifying prostaglandin J2 (PGJ2) as a high-affinity ligand (40). The second step, in collaboration with Peter Tontonoz in Bruce Spiegleman’s lab, revealed that PGJ2 was adipogenic in cell lines and perhaps more importantly that the synthetic antidiabetic drug Troglitazone was a potent PPAR agonist (41). Similar work was conducted and published by Kliewer, who had now moved to Glaxo (42). By acquiring a ligand, a physiologic response, and a drug, PPAR was suddenly transported to the center of a physiologic cyclone that would spin into its own specialty field. Since 1995, more than 1000 papers (see PubMed) have been published on PPAR and its natural and synthetic ligands. This early work illuminated the molecular strategy of reverse endocrinology and the emerging importance of the orphan receptors in human disease and drug discovery. Cary returned to the lab for a sabbatical and, with Barry, demonstrated that FXR was responsive to farnesoids and other molecules in the mevalonate pathway. The findings by Mangelsdorf that liver X receptors (LXRs) bound oxysterols (43) and by Kliewer, Mangelsdorf, and Forman that FXR is a bile acid receptor (44–46) provided a whole new conceptual approach to cholesterol and triglyceride homeostasis. The steroid and xenobiotic receptors (SXR)/pregnane X receptor (PXR) (47–49) and the constituitive androstane receptor (CAR) (50) respond to xenobiotics to activate genes for P450 Fig. 2. Examples of Receptor Heterodimer Combinations that Fill the Direct Repeat (DR) Response Element Ladder from DR1 to DR5 Evans enzymes, conjugation and transport systems that detoxify drugs, foreign chemicals, and endogenous steroids. RXR and its associated heterodimeric partners quickly established a new branch of physiology, shedding its dependence on endocrine glands and allowing the body to decode signals from environmental toxins, dietary nutrients, and common metabolites of intermediary metabolism.

Continued…

ROCK OF AGES

The human body is, after all a living machine, a complex device that consumes and uses energy to sustain itself, defend against predators, and ultimately reproduce. One might reasonably ask, “If the superfamily acts through a common molecular template, can the family as a whole be viewed as a functional entity?” In other words, is there yet some overarching principle that we have yet to grasp. . . and might this imaginary principle lie at the heart of systems physiology? Simply stated, what led to the evolution of integrated physiology as the functional output of the superfamily? One obvious speculation is survival. To survive, all organisms must be able to acquire, absorb, distribute, store, and use energy. The receptors are exquisitely evolved to manage fuel—everything from dietary and endogenous fats (PPARs), cholesterol (LXR, FXR), sugar mobilization (GR), salt (MR), and calcium (VDR) balance and maintenance of basal metabolic rate (TR). Because only a fraction of the material we voluntarily place in our bodies is nutritional, the xenobiotic receptors (PXR, CAR) are specialized to defend against the innumerable toxins in our environment. Survival also means reproduction, which is controlled by the gonadal steroid receptors (progesterone receptor, ER, AR). However, fertility is dependent on nutritional status, indicating the presumptive communication between these two branches of the family. The third key component managed by the nuclear receptor family is inflammation. During viral, bacterial, or fungal infection, the inflammatory response defends the body while suppressing appetite, conserving fuel, and encouraging sleep (associated with cytokine release). However, if needed, even an ill body is capable of defending itself by releasing adrenal steroids, mobilizing massive amounts of fuel, and transiently suppressing inflammation. In fact, clinically, (with the exception of hormone replacement) glucocorticoids are only used as antiinflammatory agents. Other receptors including the RARs, LXRs, PPAR and , and vitamin D receptor protect against inflammation. Thus, nature evolved within the structure of the receptor the combined ability to manage energy and inflammation, indicating the important duality between these two systems. In aggregate, this commonality between distinct physiologic branches suggests that the superfamily might be approached as an intact functional dynamic entity.

Historically, endocrinologists and geneticists rarely saw eye to eye. As I have indicated in this perspective article, the disciplines have now become united in a new subject—transcriptional physiology. With this in mind, we might expect the existence of larger organizational principles that establish how the various evolutionary branches of the superfamily integrate to form whole body physiology. The existence of molecular rules governing the function and evolution of a megagenetic entity like the nuclear receptor superfamily, if correct, may be useful in understanding complex human disease and provide a conceptual basis to create more effective pharmacology. With so much accomplished in the last 20 yr (see Fig. 3), there are glimpses of clarity—enough to see the enormity and wonder of the problem and enough to know there is still a long and challenging voyage ahead. But who knows, the next breakthrough may only be a stone’s throw away.

http://press.endocrine.org/doi/pdf/10.1210/me.2005-0046

 

Pierre Chambon MD

Recipient of the Canada Gairdner International Award, 2010
“For the elucidation of fundamental mechanisms of transcription in animal cells and to the discovery of the nuclear receptor superfamily.”

Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch-Graffenstaden, France

Dr. Pierre Chambon is Honorary Professor at the College de France (Paris), and Emeritus Professor at the Faculté de Médecine of the Strasbourg University. He was the Founder and former Director of the IGBMC, and also the Founder and former Director of the Institut Clinique de la Souris (ICS/MCI), in Strasbourg.

Dr. Pierre Chambon is a world expert in the fields of gene structure, and transcriptional control of gene expression. During the last 25 years his studies on the structure and function of nuclear receptors has changed our concept of signal transduction and endocrinology. By cloning the estrogen and progesterone receptors, and discovering the retinoic acid receptor family, he markedly contributed to the discovery of the superfamily of nuclear receptors and to the elucidation of their universal mechanism of action that links transcription, physiology and pathology. Through extensive site-directed mutagenesis and genetic studies in the mouse, Pierre Chambon has unveiled the paramount importance of nuclear receptor signaling in embryonic development and homeostasis at the adult stage. The discoveries of Pierre Chambon have revolutionized the fields of development, endocrinology and metabolism, and their disorders, pointing to new tactics for drug discovery, and finding important applications in biotechnology and modern medicine.

These scientific achievements are logically inscribed in an uninterrupted series of discoveries made by Pierre Chambon over the last 45 years in the field of transcriptional control of gene expression in higher eukaryotes: discovery of PolyADPribose (1963), discovery of multiple RNA polymerases differently sensitive to a-amanitin (1969), contribution to elucidation of chromatin structure: the Nucleosome (1974), discovery of animal split genes (1977), discovery of enhancer elements (1981), discovery of multiple promoter elements and their cognate factors (1980-1993).

Pierre Chambon has received numerous international awards, including the 2004 Lasker Basic Medical Research Award for the discovery of the superfamily of nuclear hormone receptors and the elucidation of a unifying mechanism that regulates embryonic development and diverse metabolic pathways. He is a member of the French Académie des Sciences, and also a Foreign Member of the National Academy of Sciences (USA) and of the Royal Swedish Academy of Sciences. Pierre Chambon serves on a number of editorial boards, including Cell, and Molecular Cell. Pierre Chambon is author of more than 900 publications. He has been ranked fourth among most prominent life scientists for the 1983-2002 period.

An Interview with Pierre Chambon
2004 Albert Lasker Basic Medical Research Award
http://www.laskerfoundation.org/media/v_chambon.htm

Pierre Chambon, MD

​Honorary Professor at the Collège-de-France and Professor of Molecular Biology and Genetics, Institute for Advanced Study, University of Strasbourg; Group Leader, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Illkirch-Graffenstaden, Strasburg, France

A pioneer in the fields of gene structure and transcriptional control of gene expression, Dr. Chambon has fundamentally changed our understanding of signal transduction, which has led to revolutionary new tactics for drug discovery. His work elucidated how molecules that promote gene transcription are organized and regulated in eukaryotic organisms and, independently of Dr. Ronald Evans, he discovered in 1987 the retinoid receptor families, which led to the discovery and characterization of the superfamily of nuclear hormone receptors, including steroid and retinoid receptors.

Dr. Chambon’s previous research led to the discovery of PolyADPribose, multiple RNA polymerases differentially sensitive to α-amaniti, and has markedly contributed to the elucidation of the nucleosome and chromatin structure, as well as to the discovery of animal split genes, DNA sequences called enhancer elements, and multiple promoter elements and their cognate factors. These discoveries have greatly enhanced understanding of embryonic development and cell differentiation. To further studies of various nuclear receptors, Dr. Chambon has developed a method that allows in the mouse the generation of somatic mutations of any gene, at any time, and in any specific cell type, a tool valuable in generating mouse models of cancer.

In 1994, Dr. Chambon took on the role of founding a major research institute in France. As the first director of IGBMC, he built the institute to encompass hundreds of top researchers and multiple research programs funded by public agencies and private industry. In 2002, he founded and was the first director of the Institut Clinique de la Souris in Strasbourg. In these positions, he has succeeded in supporting and influencing a generation of scientists.

Career Highlights

​2010  Canada Gairdner International Award

2004  Albert Lasker Basic Medical Research Award

2003  Alfred P. Sloan, Jr., Prize, General Motors Cancer Foundation

1999  Louisa Gross Horwitz Prize, Columbia University

1998  Robert A. Welch Award in Chemistry

1991  Prix Louis-Jeantet de médecine, Fondation Louis-Jeantet

1990  Sir Hans Krebs Medal, Federation of European Biochemical Societies

1988  King Faisal International Prize for Science, King Faisal Foundation

1987  Harvey Prize, Technicon-Israel Institute of Technology

more…

 

Minireviews In This Series:

Thematic Minireview Series on Nuclear Receptors in Biology and Diseases

Sohaib Khan and Jerry B Lingrel

Steroid Receptor Coactivator (SRC) Family: Masters of Systems Biology

Brian York and Bert W. O’Malley

Estrogen Signaling via Estrogen Receptor β

Chunyan Zhao, Karin Dahlman-Wright, and Jan-Åke Gustafsson

Small Molecule Inhibitors as Probes for Estrogen and Androgen Receptor Action

David J. Shapiro, Chengjian Mao, and Milu T Cherian

Cellular Processing of the Glucocorticoid Receptor Gene and Protein: New Mechanisms for Generating Tissue Specific Actions of Glucocorticoids

Robert H Oakley and John A Cidlowski

Endogenous Ligands for Nuclear Receptors: Digging Deeper

Michael Schupp and Mitchell A. Lazar

 

 

 

Read Full Post »

Roeder – the coactivator OCA-B, the first cell-specific coactivator, discovered by Roeder in 1992, is unique to immune system B cells

Larry H Bernstein, MD, FCAP, Curator

Leaders in Pharmaceutical Intelligence
The B-cell-specific transcription coactivator OCA-B/OBF-1/Bob-1 is essential for normal production of immunoglobulin isotypes

Unkyu Kim*, Xiao-Feng Qin†, Shiaoching Gong†, Sean Stevens*, Yan Luo*, Michel Nussenzweig† & Robert G. Roeder*
Nature 383, 542 – 547 (10 October 1996);  http://dx.doi.org:/10.1038/383542a0
* Laboratory of Biochemistry and Molecular Biology, and Laboratory of Molecular Immunology, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021, USA

OCA-B was initially identified as a B-cell-restricted coactivator that functions with octamer binding transcription factors (Oct-1 and Oct-2) to mediate efficient cell type-specific transcription of immunoglobulin promoters in vitro 1–3. Subsequent cloning studies led to identification of the coactivator as a single poly-peptide, designated either as OCA-B (ref. 3), OBF-1 (ref. 4) or Bob-1 (ref. 5). OCA-B itself does not bind to DNA directly, but interacts with either Oct-1 or Oct-2 to potentiate transcriptional activation1–5. To determine the biological role of OCA-B, we generated OCA-B-deficient mice by gene targeting. Mice lacking OCA-B undergo normal antigen-independent, B-cell differentiation, including appropriate expression of both immunoglobulin genes and other early B-cell-restricted genes. However, antigen-dependent maturation of B cells is greatly affected. The pro- liferative response to surface IgM crosslinking is impaired, and there is a severe deficiency in the production of secondary immunoglobulin isotypes including IgGl, IgG2a, IgG2b, IgG3, IgA and IgE in OCA-B-deficient B cells. This defect is not due to a failure of the isotype switching process, but rather to reduced levels of transcription from normally switched immunoglobulin heavy-chain loci. In accord with the defective isotype production, germinal centre formation is absent in these mutant mice.

References

1. Pierani, A., Heguy, A., Fujii, H. & Roeder, R. G. Mol. Cell. Biol. 10, 6204−6215 (1990). | PubMed | ChemPort |
2. Luo, Y., Fujii, H., Gerster, T. & Roeder, R. G. Cell 71, 231−241 (1992). | Article | PubMed | ISI | ChemPort |
3. Luo, Y. & Roeder, R. G. Mol. Cell. Biol. 15, 4115−4124 (1995). | PubMed | ISI | ChemPort |
4. Strubin, M., Newell, J. W. & Matthias, P. Cell 80, 497−506 (1995). | Article | PubMed | ISI | ChemPort |
5. Gstaiger, M., Knoepfel, L., Georgiev, O., Schaffner, W. & Hovens, C. M. Nature 373, 360−362 (1995). | Article | PubMed | ISI | ChemPort |
6. Yancopoulos, G. D. & Alt, F. W. Cell 40, 271−281 (1985). | Article | PubMed | ISI | ChemPort |
7. Yancopoulos, G. D. & Alt, F. W. Annu. Rev. Immunol. 4, 339−368 (1986). | Article | PubMed | ISI | ChemPort |
8. Rajewsky, K. Curr. Opin. Immunol. 4, 171−176 (1992). | Article | PubMed | ChemPort |
9. Rolink, A. & Melchers, F. Adv. Immunol. 53, 123−156 (1993). | PubMed | ISI | ChemPort |
10. Gold, M. R. & DeFranco, A. L. Adv. Immunol. 55, 221−295 (1994). | PubMed | ISI | ChemPort |
11. Coffman, R. L., Lebman, D. A. & Rothman, P. Adv. Immunol. 54, 229−270 (1993). | PubMed | ISI | ChemPort |
12. Parker, D. C. Annu. Rev. Immunol. 11, 331−360 (1993). | Article | PubMed | ISI | ChemPort |
13. Wang, H. Y., Paul, W. E. & Keegan, A. Immunity 4, 113−122 (1996). | Article | PubMed | ISI | ChemPort |
14. McLennan, I. C. Annu. Rev. Immunol. 12, 117−139 (1994). | Article | PubMed | ISI | ChemPort |
15. Lutzker, S. & Alt, F. W. Mol. Cell. Biol. 8, 1849−1852 (1988). | PubMed | ISI | ChemPort |
16. Stavnezer, J. et al. Proc. Natl Acad. Sci. USA 85, 7704−7708 (1988). | PubMed | ChemPort |
17. Staudt, L. M. & Lenardo, M. J. Annu. Rev. Immunol. 9, 373−398 (1991). | Article | PubMed | ISI | ChemPort |
18. Dariavach, P., Williams, G. T., Campbell, K., Pettersson, S. & Neuberger, M. S. Eur. J. Immunol. 21, 1499−1504 (1991). | PubMed | ISI | ChemPort |
19. Grant, P. A., Thompson, C. B. & Pettersson, S. EMBO J. 14, 4501−4513 (1995). | PubMed | ISI | ChemPort |
20. Bain, G., Gruenwald, S. & Murre, C. Mol. Cell. Biol. 13, 3522−3529 (1993). | PubMed | ISI | ChemPort |
21. Tybulewicz, V. L., Crawford, C. E., Jackson, P. K., Bronson, R. T. & Mulligan, R. C. Cell 65, 1153−1163 (1991). | Article | PubMed | ISI | ChemPort |
22. DeFranco, A. L. J. Exp. Med. 155, 1523−1536 (1982). | Article | PubMed | ISI | ChemPort |
23. Bottaro, A. et al. EMBO J. 13, 665−674 (1994). | PubMed | ISI | ChemPort |
24. Cogne, M. et al. Cell 77, 737−747 (1994). | Article | PubMed | ISI |
25. Gong, S. & Nussenzweig, M. C. Science 272, 411−414 (1996). | PubMed | ISI | ChemPort |
26. Qin, X. F. et al. EMBO J. 13, 5967−5976 (1994). | PubMed | ISI | ChemPort |
27. Li, S. C. et al. Int. Immunol. 6, 491−497 (1994). | PubMed | ChemPort |

 

Cloning, Functional Characterization, and Mechanism of Action of the B-Cell-Specific Transcriptional Coactivator

Oca-B Yan Luo & Robert G. Roeder*
Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10021
Molecular And Cellular Biology, Aug. 1995;  15(8):4115–4124 0270-7306/95/
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC230650/pdf/154115.pdf

Biochemical purification and cognate cDNA cloning studies have revealed that the previously described transcriptional coactivator OCA-B consists of a 34- or 35-kDa polypeptide with sequence relationships to known coactivators that function by protein-protein interactions. Studies with a recombinant protein have proved that a single OCA-B polypeptide is the main determinant for B-cell-specific activation of immunoglobulin (Ig) promoters and provided additional insights into its mechanism of action. Recombinant OCA-B can function equally well with Oct-1 or Oct-2 on an Ig promoter, but while corresponding POU domains are sufficient for OCA-B interaction, and for octamer-mediated transcription of a histone H2B promoter, an additional Oct-1 or Oct-2 activation domain(s) is necessary for functional synergy with OCA-B. Further studies show that Ig promoter activation by Oct-1 and OCA-B requires still other general (USA-derived) cofactors and also provide indirect evidence that distinct Oct-interacting cofactors regulate H2B transcription.

A novel B cell-derived coactivator potentiates the activation of immunoglobulin promoters by octamer-binding transcription factors

Yan Luo, Hiroshi Fujii, Thomas Gerster, Robert G. Roeder

Laboratory of Biochemistry and Molecular Biology The Rockefeller University New York, New York 10021 USA
Present address: Department of Biochemistry, Niigata University School of Medicine, Niigata 951, Japan.
Present address: Biozentrum der Universität Basel, Abteilung Zellbiologie, 4056 Basel, Switzerland.
Cell Oct 1992 71(2):231–241    http://dx.doi.org/10.1016/0092-8674(92)90352-D
A novel B cell-restricted activity, required for high levels of octamer/Oct-dependent transcription from an immunoglobulin heavy chain (IgH) promoter, was detected in an in vitro system consisting of HeLa cell-derived extracts complemented with fractionated B cell nuclear proteins. The factor responsible for this activity was designated Oct coactivator from B cells (OCA-B). OCA-B stimulates the transcription from an IgH promoter in conjunction with either Oct-1 or Oct-2 but shows no significant effect on the octamer/Oct-dependent transcription of the ubiquitously expressed histone H2B promoter and the transcription of USF- and Sp1-regulated promoters. Taken together, our results suggest that OCA-B is a tissue-, promoter-, and factor-specific coactivator and that OCA-B may be a major determinant for B cell-specific activation of immunoglobulin promoters. In light of the evidence showing physical and functional interactions between Oct factors and OCA-B, we propose a mechanism of action for OCA-B and discuss the implications of OCA-B for the transcriptional regulation of other tissue-specific promoters.

Identification of transcription coactivator OCA-B dependent genes involved in antigen-dependent B cell differentiation by cDNA array analyses

Unkyu Kim*, Rachael Siegel*, Xiaodi Ren*, Cary S. Gunther*, Terry Gaasterland†, and Robert G. Roeder*‡
*Laboratory of Biochemistry and Molecular Biology and †Laboratory of Computational Genomics, The Rockefeller University, 1230 York Avenue, New York, NY 10021

PNAS  http://www.pnas.org/content/100/15/8868.full.pdf

The tissue-specific transcriptional coactivator OCA-B is required for antigen-dependent B cell differentiation events, including germinal center formation. However, the identity of OCA-B target genes involved in this process is unknown. This study has used large-scale cDNA arrays to monitor changes in gene expression patterns that accompany mature B cell differentiation. B cell receptor ligation alone induces many genes involved in B cell expansion, whereas B cell receptor and helper T cell costimulation induce genes associated with B cell effector function. OCA-B expression is induced by both B cell receptor ligation alone and helper T cell costimulation, suggesting that OCA-B is involved in B cell expansion as well as B cell function. Accordingly, several genes involved in cell proliferation and signaling, such as Lck, Kcnn4, Cdc37, cyclin D3, B4galt1, and Ms4a11, have been identified as OCA-B-dependent genes. Further studies on the roles played by these genes in B cells will contribute to an understanding of B cell differentiation.

 

Identification and Characterization of a Novel OCA-B Isoform: Implications for a Role in B Cell Signaling Pathways

Xin Yu, Lu Wang†, Yan Luo, Robert G. Roeder
Immunity Feb 2001; 14(2): 157–167   http://dx.doi.org:/10.1016/S1074-7613(01)00099-1

OCA-B is a B lymphocyte–specific transcription coactivator that mediates tissue- and stage-restricted transcription of immunoglobulin genes. Earlier genetic studies revealed that OCA-B is essential for germinal center formation and production of secondary immunoglobulin isotypes. Biochemically purified OCA-B contains p35 and p34 isoforms, and a further analysis has now revealed that p35 is derived from a newly found isoform, p40. More importantly, it has been found that p35 is myristoylated in vivo and that this leads to dramatic changes (including localization to membrane compartments) in its properties. These results suggest that the p35 isoform of OCA-B has functions distinct from those of the nuclear p34 and that it might be a component of a signaling pathway that is required for late-stage B cell development.

 

The B cell–restricted function of immunoglobulin (Ig) promoters is mediated mainly by an octamer element (5′-ATGCAAAT-3′) that is conserved in virtually all Ig heavy (H) and light (L) chain gene promoters, as well as in some Ig enhancers (reviewed by Staudt and Lenardo, 1990). However, this same element is also a key central element for transcription of differentially regulated genes that include ubiquitously expressed small nuclear RNA genes (snRNA) and cell cycle-regulated histone H2B genes (reviewed inLuo et al., 1992). The regulatory functions of octamer elements, therefore, are likely dependent on transcription factors that bind this DNA sequence. The well-characterized octamer binding transcription factors include the ubiquitous Oct-1 and the B cell–enriched Oct-2, both of which belong to the POU family and share a conserved DNA binding structure called the POU domain (reviewed by Herr et al. 1988 and Wegner et al. 1993). It was originally thought that Oct-2 would account for the tissue-specific activity of Ig promoters, whereas Oct-1 would facilitate transcription of the ubiquitously expressed genes regulated through octamer elements (e.g., snRNA and histone H2B genes) Staudt et al. 1986, Cockerill and Klinken 1990 and Murphy et al. 1992. However, subsequent biochemical Pierani et al. 1990 and Luo et al. 1992 and genetic (Corcoran et al., 1993)analyses clearly demonstrated that this was not the case. Instead, the promoter specificity was shown to be due to an Oct-1 interacting factor called OCA-B (Luo et al., 1992), and the purification of related p35 and p34 isoforms with apparently equivalent activity in vitro (Luo and Roeder, 1995) set the stage for further studies of the structure and function of OCA-B.

Subsequent to the biochemical identification of OCA-B and its mechanism of action, cognate cDNAs were cloned using both biochemical (Luo and Roeder, 1995) and genetic screening Gstaiger et al. 1995 and Strubin et al. 1995 methods. Analyses of recombinant OCA-B (p34) function in cell-free systems and in transfection assays confirmed both physical and functional interactions with Oct-1 and Oct-2 (via their POU domains) on Ig promoters Gstaiger et al. 1995, Luo and Roeder 1995 and Strubin et al. 1995 and led to the definition of an N-terminal OCA-B domain that interacts with the Oct POU domainCepek et al. 1996, Gstaiger et al. 1996, Babb et al. 1997 and Chaseman et al. 1999 and a C-terminal activation domain that acts synergistically with Oct activation domains to recruit additional coactivators (Luo et al., 1998).

The physiological roles of OCA-B were further investigated by genetic disruption of OCA-B expression in mice Kim et al. 1996, Nielson et al. 1996 and Schubart et al. 1996. These studies showed that, although not required for early B cell development, OCA-B functions are essential both for germinal center formation and for efficient secondary Ig isotype production (including IgGs, IgA, and IgE). In accordance with the biochemical function of OCA-B in activating Ig promoter transcription, it has been found that the decrease of secondary antibody production in OCA-B-deficient mice is largely due to reduced levels of transcription from normally switched IgH chain loci, rather than a reduced capacity for class switching events per se Kim et al. 1996 and Schubart et al. 1996. Recent results further demonstrated that OCA-B plays an essential role in efficient transcription from switched IgH loci by directly regulating 3′ IgH enhancer function in conjunction with Oct-1 or Oct-2 Tang and Sharp 1999 and Stevens et al. 2000b. On the other hand, the lack of germinal center formation in OCA-B-deficient mice cannot be explained by reduced Ig isotype production, since these are two independent events in B cell development (Vajdy et al., 1995). Therefore, OCA-B may regulate germinal center formation by activating the expression of other target genes or by mediating signal pathways that in turn trigger a specific genetic program. At least two lines of evidence support this idea: (1) B cells lacking OCA-B are defective in the proliferative response to surface IgM cross-linking (Kim et al., 1996); (2) OCA-B expression, which is very low in early B cells but high in activated B cells in vivo, can be dramatically and synergistically induced in naive B cells by B cell stimuli (CD40L, Ig cross-linking, and IL4) that are required for germinal center formation (Qin et al., 1998).

Our findings in this report raise the possibility that OCA-B may be directly involved in B cell signaling pathways through novel mechanisms. We report the presence of a novel isoform of OCA-B (p40) that results from utilization of an upstream alternative translation initiation codon and that serves as a precursor to the p35 isoform of OCA-B. Relative to the conventional p34 OCA-B isoform, p35 shows distinct protein modification, subcellular localization, and transcriptional coactivator properties. The unique features of p35 suggest a novel function for this molecule in signal transduction.

 

Synergism with the Coactivator OBF-1 (OCA-B, BOB-1) Is Mediated by a Specific POU Dimer Configuration

Alexey Tomilin1, 2, #, Attila Reményi2, 4, #, Katharina Lins1, Hanne Bak2, Sebastian Leidel1, Gerrit Vriend3, Matthias Wilmanns4, Hans R Schöler1, 2
Cell   Dec 2000; 103(6):853–864  doi:10.1016/S0092-8674(00)00189-6

POU domain proteins contain a bipartite DNA binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer formed on the PORE (ATTTGAAATGCAAAT) can recruit the transcriptional coactivator OBF-1, whereas POU dimers formed on the consensus MORE (ATGCATATGCAT) or on MOREs from immunoglobulin heavy chain promoters (AT[G/A][C/A]ATATGCAA) fail to interact. An interaction with OBF-1 is precluded since the same Oct-1 residues that form the MORE dimerization interface are also used for OBF-1/Oct-1 interactions on the PORE. Our findings provide a paradigm of how specific POU dimer assemblies can differentially recruit a coregulatory activity with distinct transcriptional readouts.

Development of multicellular organisms is characterized by an intricate series of genetic and epigenetic events that generate the complex adult body from the unicellular zygote. A refined and sophisticated regulatory network that is established during embryogenesis reflects the complexity of organisms. Although embryonic development is a multistep process characterized by the sequential activation and repression of many genes, only a relatively small number of transcription factors are responsible for regulating the expression of developmental genes. This diversity in transcriptional control by a limited array of transcription factors is achieved through a complex network of interactions between these proteins and specific DNA sequences found in promoters and enhancers of developmental genes. The primary structure of these DNA elements defines the composition and architecture of the transcriptional activation complexes that ultimately control gene expression in the appropriate temporo-spatial context of the developing organism. For example, nonsteroid members of the nuclear receptor superfamily that possess a zinc-finger DNA binding domain operate by binding to the hormone response elements (HREs). HREs consist of two minimal core hexad sequences, AGGTCA, which can be configured into various functional motifs. The orientation and spacing between these two hexamers as well as subtle differences in their sequence dictate the identity and the mode (monomer, hetero-, or homodimer) of nuclear receptor binding that results in diverse effects on transcription (Mangelsdorf and Evans 1995).

The operation of members of the POU domain family of transcription factors is also highly dependent on the nature of cognate DNA elements. The 160 amino-acid-long DNA binding domain of these proteins is composed of two structurally independent subdomains: the POU-type homeodomain (POU-homeo or POUH), and the POU-specific domain (POUS) that are connected by a flexible linker region (27 and 36). POU domain proteins demonstrate impressive versatility in how they regulate transcription. This is due to several, often interdependent, factors: (1) flexible amino acid–base interaction, (2) variable orientation, spacing, and positioning of DNA-tethered POU subdomains relative to each other, (3) posttranslational modification, and (4) interaction with heterologous proteins (Herr and Cleary 1995).

POU domain proteins are able to bind to DNA cooperatively, thus conferring additional functional variability. The homo- and heterodimerization of Oct-1 and Oct-2 on immunoglobulin (Ig) heavy chain promoters (VH) provided evidence of cooperativity, with a yet unknown dimer arrangement (13, 16 and 23). The cis-elements are considered to consist of low-affinity heptamer and high-affinity octamer sites separated by two nucleotides (Full-size image (<1 K)ATFull-size image (<1 K)).

The pituitary-specific POU domain protein Pit-1 binds to DNA either as a homodimer or as a heterodimer with Oct-1 (Voss et al. 1991). Crystallographic studies determined the structure of a Pit-1 homodimer assembled on the synthetic motif ATGTATATACAT (referred to here as PitD) that had been derived from the natural Pit-1 cognate element within the prolactin gene promoter (ATATATATTCAT) (Jacobson et al. 1997). The structure of the Pit-1 POUS and POUH domains, and their docking onto DNA, are very similar to that observed in the cocrystal of the Oct-1 POU domain monomer with the octamer site (ATGCAAAT, Klemm et al. 1994). The Oct-1 POUS domain recognizes the ATGC subsite whereas the Pit-1 POUS domain binds to the sequence ATAC. However, the latter subsite lies on the opposite strand and, as a consequence, the orientation of POUS relative to the POUH domain is inverted (Jacobson et al. 1997).

Another mechanism outlining cooperative DNA binding by POU proteins was recently determined during the course of an Oct-4 target gene characterization (Botquin et al. 1998). The P alindromic O ct factor R ecognition E lement (PORE), ATTTGAAATGCAAAT (15 bp), of the Osteopontin (OPN) enhancer interacts with an Oct-4 dimer, thereby mediating strong transcriptional activation in preimplantation mouse embryos. Homo- and heterodimerization of other Oct factors like Oct-1 and Oct-6 on the PORE has also been demonstrated.

The aforementioned examples provide evidence of the various ways in which POU domain proteins are able to cooperatively bind to substrate DNA. The particular mode of binding employed is primarily defined by the DNA sequence. To address the question of whether diversity in cooperative binding is reflected in transcriptional regulation, we have assessed and compared the ability of two different types of POU dimers to interact with the coactivator OBF-1 (OCA-B, Bob-1). This coactivator synergistically interacts with Oct-1 and Oct-2 monomers bound to the octamer motif (18, 9, 17 and 33). We have investigated one type of POU dimer that is formed on the PORE and another that is formed on another palindromic DNA motif called MORE (M ore P ORE), ATGCATATGCAT. The data presented in this study provide an example of how POU domain molecules that bind to DNA in the same stoichiometry but in different configurations can differentially recruit a transcriptional coactivator to the promoter resulting in differential transcriptional activation.

B-cell-specific Coactivator OCA-B: Biochemical Aspects, Role in B-Cell Development and Beyond

Cold Spring Harb Symp Quant Biol 1999 64: 119-132;
http://dx.doi.org:/10.1101/sqb.1999.64.119

Read Full Post »

The structure of our visual and auditory system

Larry H. Bernstein, MD, FCAP, Curator

Leaders in Pharmaceutical Intelligence

Series E. 2; 5.8

Revised 9/30/2015

Torsten N. Wiesel (1921— )
President Emeritus
Vincent and Brooke Astor Professor Emeritus – Rockefeller Univerity
1981 Nobel Prize in Physiology or Medicine

Torsten N. Wiesel

The structure of our visual system, beginning at the eyes and ending at the primary visual cortex at the back of the brain, is a little like a maze, intricately constructed to send visual signals through myriad portals and passageways to reach just the right neurons at the end of the path. In the 1950s, H. Keffer Hartline, a member of The Rockefeller Institute for Medical Research, charted the first avenues of that maze when he revealed how the visual stimulus received by the retina is divided, altered and sharpened by the optic nerve network in order to send a more useful picture to the brain. Former Rockefeller president Torsten N. Wiesel, along with his colleague David H. Hubel, continued Dr. Hartline’s exploration at their Harvard Medical School laboratory by delving further back, into the brain, and described for the first time how the system develops innately, how experience shapes it further and how it analyzes visual signals. For this work, Drs. Wiesel and Hubel shared the 1981 Nobel Prize in Physiology or Medicine.

The complex array of stimuli in our visual field passes first through several distinct layers of cells known collectively as the retina. Next they are analyzed by the optic nerve and make their way to the lateral geniculate nucleus (LGN), the first visual processing center in the brain, located in the thalamus of each brain hemisphere. From the LGN, the signals are sent to the primary visual cortex, also known as the striate cortex. Working with cats and rhesus macaque monkeys, Drs. Wiesel and Hubel recorded the electrical impulses of cortical cells in response to various patterns flashed before the eyes. They coined the terms “simple” and “complex” for cells that respond to only one type of stimulus and those that respond to multiple and opposite stimuli.

To understand the differentiation, the scientists conducted a series of experiments to observe the brain’s response when one eye is kept closed for different periods of time. They discovered that animals with one eye closed for the first three months of life become blind in that eye. Examinations revealed no change in the eye itself or in the retina; the LGN cells devoted to that eye had shrunken but still responded to stimulation of the deprived eye as efficiently as those for the normal eye. The difference, they concluded, must therefore be in the striate cortex.

Awards: Nobel Prize in Physiology or Medicine, Louisa Gross Horwitz Prize, National Medal of Science for Biological Sciences

Swedish-born American neurobiologist Torsten N. Wiesel was raised at Beckomberga Hospital, the mental institute where his father was chief psychiatrist. He described himself as a lazy student until his late teens, before embarking on a career of research into the physiology of vision. Wiesel was awarded the Nobel Prize for Medicine in 1981, along with his long-time collaborator David H. Hubel, for mapping the visual or striate cortex, the posterior section of the cerebral cortex. Roger W. Sperry shared that year’s Nobel honors, for work conducted at CalTech. Wiesel also demonstrated the importance of early diagnosis of childhood visual problems.

When a reporter informed him he had won the Nobel Prize, Wiesel’s first response was, “Oh, no, I was afraid of that”, explaining that he feared the hubbub might prove a distraction from his work. In the 1990s he was President of Rockefeller University, and since 2000, he has been Secretary-General of the Human Frontier Science Program, a group which supports collaboration across different scientific fields. He also served more than a decade as Chair of the Human Rights Committee for the National Academy of Sciences.

In 2001, he was named to a high-level post at the National Institutes of Health, but his nomination was scuttled by then-Secretary of Health and Human Services Tommy Thompson, with the official explanation that he had “signed too many full-page letters in the New York Times critical of President Bush.” Wiesel responded, “I have not signed a statement against Bush, but nonetheless for some reason I am on the administration’s blacklist. Perhaps [it is because of] my human rights activities and being contrary in general.”

Structure and evolution of hearing

9.2015 The Scientist

Inner Ear Cartography

Scientists map the position of cells within the organ of Corti.  by Ruth Williams

Age-related hearing loss caused by damage to the sensory hair cells within the cochlea is extremely common, but studying the inner ear is tough. “It’s in the densest bone in the body, so you don’t have access,” says John Brigande of Oregon Health and Science University in Portland. Even if you can extract cells, he says, “there are so darn few of them.” Despite these technical difficulties, researchers have gleaned gene-expression information about different cell types within the organ of Corti—home to the sensory cells within the cochlea. But “it’s not only important to know what a cell expresses,” says Robert Durruthy-Durruthy, a postdoc in the Stanford University lab of Stefan Heller. “It’s also important to know where it can be found within a tissue.” To this end, Durruthy-Durruthy, Heller, and postdoc Jörg Waldhaus have derived a 2-D map of organ of Corti cells from neonatal mice. First, the team sorted all cell types across the medial-to-lateral axis (or width) of the organ based on marker gene expression. The approximately 900 sorted cells, representing nine cell types, were then each quantitatively analyzed for the expression of 192 selected genes. Computational analysis of these expression data then enabled reconstruction of the cells’ positions along the organ’s apical-to-basal (length) and medial-to-lateral axes. In principle, the technique, which harnesses gene-expression information to determine cells’ spatial organization, could be applied to generate 2-D maps of any complex tissue, says Durruthy-Durruthy. Within the mammalian cochlea, apical cells retain regenerative capacity for a few weeks after birth, but basal cells do not. “Spatial mapping allows us to get at the differences [between these cells],” says Brigande, and that could ultimately highlight possible ways to reinstate regeneration in the adult ear. (Cell Reports, 11:1385-99, 2015) To build a map of cells within the organ of Corti—where sound is translated to neural activity— scientists divide the cochlea in two. Each half of the organ of Corti is then broken up into its constituent cells, which comprise nine cell types (represented by the nine colors) spanning the organ’s medial-to-lateral axis.

FROM CELLS TO GENE-EXPRESSION: Each cell is analyzed for the expression of 192 selected genes. Based on the pattern of expression, a cell is given a position within the organ of Corti along both the basal-apical and the medial-lateral axes. Each column represents one of the nine cell types.

Human Hearing: A Primer

Semicircular canals of the vestibular system OSSICLES Ear canal Tympanic membrane (eardrum) When sound enters the ear canal, it vibrates the tympanic membrane, or eardrum. These vibrations are passed through the inner ear via three small bones called ossicles: the malleus, the incus, and the stapes. Finally, vibrations of the stapes stimulate the movement of a fluid called perilymph within the bony labyrinth of the inner ear.

Cochlea – How the human ear translates sound waves into nervous impulses.

Perilymph fills the both the vestibular and tympanic ducts of the cochlea. Between these two channels lies the cochlear duct, which is home to the organ of Corti. There, the soundinduced movement of perilymph in the cochlea is translated to an electrical signal that is sent to the brain for processing.

The organ of Corti sits on the basilar membrane, which separates the cochlear duct from the tympanic duct. As the basilar membrane vibrates in response to fluid movement, it pushes the organ along the tectorial membrane, which shifts laterally over the hair cells. This shift bends projections at the tips of the cells, called stereocilia, resulting in the generation of electrical signals.

The bending of the stereocilia results in the depolarization of the inner hair cell and initiates a nerve impulse through the spinal ganglion neuron at the base of the cell. A series of outer hair cells serves to mechanically amplify the vibrations that trigger the inner hair cells to fire. High-frequency sounds stimulate hair cells at the base of the cochlea, while low-frequency sounds stimulate hair cells at the apex.

Aural History -The form and function of the ears of modern land vertebrates cannot be understood without knowing how they evolved.

by Geoffrey A. Manley

Unlike eyes, which are generally instantly recognizable, ears differ greatly in their appearance throughout the animal kingdom. Some hearing structures may not be visible at all. For example, camouflaged in the barn owl’s facial ruff—a rim of short, brown feathers surrounding the bird’s white face—are clusters of stiff feathers that act as external ears on either side of its head. These feather structures funnel sound collected by two concave facial disks to the ear canal openings, increasing the bird’s hearing sensitivity by 20 decibels—approximately the difference between normal conversation and shouting.

Similar increases in sensitivity result from the large and often mobile external structures, or pinnae, of many mammals, such as cats and bats. Internally, the differences among hearing organs are even more dramatic.

Although fish can hear, only amphibians and true land vertebrates—including the aquatic species that descended from them, such as whales and pinnipeds—have dedicated hearing organs. In land vertebrates belonging to the group Amniota, including lizards, birds, and mammals, sound usually enters through an external canal and impinges on an eardrum that is connected through middle-ear bones to the inner ear. There, hundreds or thousands of sensory hair cells are spread along an elongated membrane that acts as a spectral analyzer, with the result that each local group of hair cells responds best to a certain range of pitches, or sound frequencies. The hair cells then feed this information into afferent nerve fibers that carry the information to the brain. (See “Hearing Primer” on page 34.)

Together, these hair cells and nerve fibers encode a wide range of sounds that enter the ear on that side of the head. Two ears complete the picture, allowing animals’ brains to localize the source of the sounds they hear by comparing the two inputs. Although it seems obvious that the ability to process nearby sounds would be enormously useful, modern amniote ears in fact arose quite late in evolutionary history, and to a large extent independently in different lineages. As a result, external, middle, and inner ears of various amniotes are characteristically different.1

Moreover, the early evolution of these dedicated auditoryorgans in land vertebrates led to the loss of the heavy otolithic membrane that overlies the hair-cell bundles of vestibular organs and is responsible for their slow responses. What remains is the watery macromolecular gel known as the tectorial membrane, which assures that local groups of hair cells move synchronously, resulting in greater sensitivity.

Good high-frequency hearing did not exist from the start, however. For a period of at least 50 million years after amniotes arose, the three main lineages were most likely quite hard of hearing. They had not yet evolved any mechanism for absorbing sound energy from air; they lacked the middle ear and eardrum that are vital for the function of modern hearing organs. As such, ancestral amniotes most likely perceived only sounds of relatively low frequency and high amplitude that reached the inner ear via the limbs or, if the skull were rested on the ground, through the tissues of the head. It is unclear what kind of stimuli could have existed that would have led to the retention of such hearing organs for such a long time.

The magnificent middle ear

During the Triassic period, some 250 to 200 million years ago, a truly remarkable thing happened. Independently, but within just 20 million to 30 million years of one another, all three amniote lineages evolved a tympanic middle ear from parts of the skull and the jaws.2 The tympanic middle ear is the assemblage of tiny bones that connects at one end to an eardrum and at the other end to the oval window, an aperture in the bone of the inner ear. Despite the temporal coincidence in the evolution of these structures in the three amniote lineages and the functional similarities of the adaptations, the groups were by this time so far separated that the middle ears evolved from different structures into two different configurations. The single middle-ear bone, the columella, of archosaurs and lepidosaurs derived from the hyomandibular, a bone that earlier had formed a large strut connecting the braincase to the outer skull.

Research on hearing organs have revealed the remarkable history of this unexpected diversity of ears. Divergence from a common origin Amniote vertebrates comprise three lineages of extant groups that diverged roughly 300 million years ago: the lepidosaurs, which include lizards and snakes; the archosaurs, which include crocodilians and birds; and mammals, which include egg-laying, pouched, and placental mammals. By comparing the skulls of the extinct common ancestors of these three lineages, as well as the ears of the most basal modern amniotes, researchers have concluded that ancestral amniotes had a small (perhaps less than 1 millimeter in length) but dedicated hearing organ: a sensory epithelium called a basilar papilla, with perhaps a few hundred sensory hair cells supported by a thin basilar membrane that is freely suspended in fluid. These rudimentary structures evolved from the hair cells of vestibular organs, which help organisms maintain their balance by responding to physical input, such as head rotation or gravity. Initially, the hearing organ only responded to low-frequency sounds. On their apical surface, all hair cells have tight tufts or bundles of large, hairlike villi known as stereovilli (or, more commonly stereocilia, even though they are not true cilia), which give hair cells their name. Between these stereovilli are proteinaceous links, most of which are closely coupled to sensory transduction channels that respond to a tilting of the stereovilli bundles caused by sound waves.

The amniote hearing organ evolved as a separate group of hair cells that lay between two existing vestibular epithelia. Low-frequency vestibular hair cells became specialized to transduce higher frequencies, requiring much faster response rates. This change is attributable in part to modifications in the ion channels of the cell membrane, such that each cell is “electrically tuned” to a particular frequency, a phenomenon still observed in some modern amniote ears.

MODERN INNER EARS

Arose starting about 200 million years ago In all three lineages, hair cells are arranged along the auditory papilla from low- to high-frequency sensitivity, called a tonotopic organization. In both archosaurs and mammals, one type of hair cell serves to amplify the sound signal received by the other type. In lepidosaurs, the auditory papilla ranges from a few hundred micrometers to 2 millimeters in length and contains two types of hair cells: one with taller bundles and fewer stereovilli that responds to sounds below 1 kHz and another with shorter, thicker bundles that responds to higher-frequency pitches.

The archosaur papilla, which reaches lengths of up to 10 millimeters in some owls, contains many thousands of hair cells of types: tall hair cells, which serve to detect sound, and short hair cells, which amplify the signal. In most mammals, the auditory papilla, called the organ of Corti, evolved to be so long that it began to coil on top of itself. The papilla ranges from 1.5 to 4 coils and 7 millimeters (mouse) to 75 millimeters (blue whale) in length. Mammals have two types of hair cells: covering the oval window, which detect sound, and outer hair cells, which inner hair cells amplify it.

Tectorial membrane

Tall hair cell

Short hair cell

Basilar membrane

Inner

hair cell

Outer

hair cell

In modern representatives, the columella is long and thin, with several, usually cartilaginous extensions known as the extracolumella. One of these, the “inferior process,” connects the inner surface of the eardrum and the columella, which then connects to the footplate that covers the oval window of the inner ear. This two-part system forms a lever that, together with the pressure increase incurred by transmitting from the much larger eardrum to the footplate, greatly magnifies sound entering the inner ear.

In the mammals of the Triassic, the equivalent events were more complex, but the functional result was remarkably similar. Mammal ancestors reduced the number of bones in the lower jaw from seven to one and, in the process, formed a new jaw joint. Initially, the old and new jaw structures existed in parallel, but over time the old joint moved towards the rear of the head. This event, which at any other time would likely have led to the complete loss of the old joint bones, occurred simultaneously with the origin of the mammalian tympanic middle ear. Older paleontological and newer developmental evidence from Shigeru Kuratani’s lab at RIKEN in Japan indicate that the mammalian eardrum evolved at a lower position on the skull relative to that of the other amniotes, a position outside the old jaw joint.3 In time, the bones of this old joint, together with the hyomandibula, became the three bony ossicles (malleus, incus, and stapes) of the new middle ear. Like the middle ear of archosaurs and lepidosaurs, these ossicles form a lever system that, along with the large area difference between eardrum and footplate, greatly magnifies sound input. Thus, remarkably, these complex events led independently to all modern amniotes possessing a middle ear that, at frequencies below 10 kHz, works equally effectively despite the diverse structures and origins. There is also evidence that the three-ossicle mammalian middle ear itself evolved at least twice—in egg-laying mammals such as the platypus, and in therians, which include marsupials and placentals—with similar outcomes.

More…

Aural History

The form and function of the ears of modern land vertebrates cannot be understood without knowing how they evolved.

http://www.the-scientist.com//?articles.view/articleNo/43806/title/Aural-History/

By Geoffrey A. Manley | September 1, 2015

PHOTO CREDITS SEE END OF ARTICLE
http://www.the-scientist.com/Sept2015/feature1.jpg

Unlike eyes, which are generally instantly recognizable, ears differ greatly in their appearance throughout the animal kingdom. Some hearing structures may not be visible at all. For example, camouflaged in the barn owl’s facial ruff—a rim of short, brown feathers surrounding the bird’s white face—are clusters of stiff feathers that act as external ears on either side of its head. These feather structures funnel sound collected by two concave facial disks to the ear canal openings, increasing the bird’s hearing sensitivity by 20 decibels—approximately the difference between normal conversation and shouting. Similar increases in sensitivity result from the large and often mobile external structures, or pinnae, of many mammals, such as cats and bats. Internally, the differences among hearing organs are even more dramatic.

Although fish can hear, only amphibians and true land vertebrates—including the aquatic species that descended from them, such as whales and pinnipeds—have dedicated hearing organs. In land vertebrates belonging to the group Amniota, including lizards, birds, and mammals, sound usually enters through an external canal and impinges on an eardrum that is connected through middle-ear bones to the inner ear. There, hundreds or thousands of sensory hair cells are spread along an elongated membrane that acts as a spectral analyzer, with the result that each local group of hair cells responds best to a certain range of pitches, or sound frequencies. The hair cells then feed this information into afferent nerve fibers that carry the information to the brain. (See “Human Hearing: A Primer.”)

For a period of at least 50 million years after amniotes arose, the three main lineages were most likely quite hard of hearing.

Together, these hair cells and nerve fibers encode a wide range of sounds that enter the ear on that side of the head. Two ears complete the picture, allowing animals’ brains to localize the source of the sounds they hear by comparing the two inputs. Although it seems obvious that the ability to process nearby sounds would be enormously useful, modern amniote ears in fact arose quite late in evolutionary history, and to a large extent independently in different lineages. As a result, external, middle, and inner ears of various amniotes are characteristically different.1 New paleontological studies and comparative research on hearing organs have revealed the remarkable history of this unexpected diversity of ears.

Divergence from a common origin

Amniote vertebrates comprise three lineages of extant groups that diverged roughly 300 million years ago: the lepidosaurs, which include lizards and snakes; the archosaurs, which include crocodilians and birds; and mammals, which include egg-laying, pouched, and placental mammals. By comparing the skulls of the extinct common ancestors of these three lineages, as well as the ears of the most basal modern amniotes, researchers have concluded that ancestral amniotes had a small (perhaps less than 1 millimeter in length) but dedicated hearing organ: a sensory epithelium called a basilar papilla, with perhaps a few hundred sensory hair cells supported by a thin basilar membrane that is freely suspended in fluid. These rudimentary structures evolved from the hair cells of vestibular organs, which help organisms maintain their balance by responding to physical input, such as head rotation or gravity. Initially, the hearing organ only responded to low-frequency sounds. On their apical surface, all hair cells have tight tufts or bundles of large, hairlike villi known as stereovilli (or, more commonly stereocilia, even though they are not true cilia), which give hair cells their name. Between these stereovilli are proteinaceous links, most of which are closely coupled to sensory transduction channels that respond to a tilting of the stereovilli bundles caused by sound waves.

The amniote hearing organ evolved as a separate group of hair cells that lay between two existing vestibular epithelia. Low-frequency vestibular hair cells became specialized to transduce higher frequencies, requiring much faster response rates. This change is attributable in part to modifications in the ion channels of the cell membrane, such that each cell is “electrically tuned” to a particular frequency, a phenomenon still observed in some modern amniote ears. Moreover, the early evolution of these dedicated auditory organs in land vertebrates led to the loss of the heavy otolithic membrane that overlies the hair-cell bundles of vestibular organs and is responsible for their slow responses. What remains is the watery macromolecular gel known as the tectorial membrane, which assures that local groups of hair cells move synchronously, resulting in greater sensitivity.

Good high-frequency hearing did not exist from the start, however. For a period of at least 50 million years after amniotes arose, the three main lineages were most likely quite hard of hearing. They had not yet evolved any mechanism for absorbing sound energy from air; they lacked the middle ear and eardrum that are vital for the function of modern hearing organs. As such, ancestral amniotes most likely perceived only sounds of relatively low frequency and high amplitude that reached the inner ear via the limbs or, if the skull were rested on the ground, through the tissues of the head. It is unclear what kind of stimuli could have existed that would have led to the retention of such hearing organs for such a long time.

The magnificent middle ear

http://www.the-scientist.com/Sept2015/Manleyonline.jpg

CONVERGING ON THE EAR: Starting around 250 million years ago, the three amniote lineages—lepidosaurs (lizards and snakes), archosaurs (crocodilians and birds), and mammals—separately evolved a tympanic middle ear, followed by evolution of the inner ear, both of which served to increase hearing sensitivity. Despite the independent origin of hearing structures in the three lineages, the outcomes were functionally quite similar, serving as a remarkable example of convergent evolution.
See full infographic: JPG

ILLUSTRATIONS: PHEBE LI FOR THE SCIENTIST. ICONS: ISTOCK.COMDuring the Triassic period, some 250 to 200 million years ago, a truly remarkable thing happened. Independently, but within just 20 million to 30 million years of one another, all three amniote lineages evolved a tympanic middle ear from parts of the skull and the jaws.2

The tympanic middle ear is the assemblage of tiny bones that connects at one end to an eardrum and at the other end to the oval window, an aperture in the bone of the inner ear. Despite the temporal coincidence in the evolution of these structures in the three amniote lineages and the functional similarities of the adaptations, the groups were by this time so far separated that the middle ears evolved from different structures into two different configurations. The single middle-ear bone, the columella, of archosaurs and lepidosaurs derived from the hyomandibular, a bone that earlier had formed a large strut connecting the braincase to the outer skull. In modern representatives, the columella is long and thin, with several, usually cartilaginous extensions known as the extracolumella. One of these, the “inferior process,” connects the inner surface of the eardrum and the columella, which then connects to the footplate that covers the oval window of the inner ear. This two-part system forms a lever that, together with the pressure increase incurred by transmitting from the much larger eardrum to the footplate, greatly magnifies sound entering the inner ear.

In the mammals of the Triassic, the equivalent events were more complex, but the functional result was remarkably similar. Mammal ancestors reduced the number of bones in the lower jaw from seven to one and, in the process, formed a new jaw joint. Initially, the old and new jaw structures existed in parallel, but over time the old joint moved towards the rear of the head. This event, which at any other time would likely have led to the complete loss of the old joint bones, occurred simultaneously with the origin of the mammalian tympanic middle ear. Older paleontological and newer developmental evidence from Shigeru Kuratani’s lab at RIKEN in Japan indicate that the mammalian eardrum evolved at a lower position on the skull relative to that of the other amniotes, a position outside the old jaw joint.3 In time, the bones of this old joint, together with the hyomandibula, became the three bony ossicles (malleus, incus, and stapes) of the new middle ear. Like the middle ear of archosaurs and lepidosaurs, these ossicles form a lever system that, along with the large area difference between eardrum and footplate, greatly magnifies sound input.

Thus, remarkably, these complex events led independently to all modern amniotes possessing a middle ear that, at frequencies below 10 kHz, works equally effectively despite the diverse structures and origins. There is also evidence that the three-ossicle mammalian middle ear itself evolved at least twice—in egg-laying mammals such as the platypus, and in therians, which include marsupials and placentals—with similar outcomes.

Inner-ear evolution

http://www.the-scientist.com/Sept2015/piano_med.jpg

PITCH PERFECT: The hearing organs of amniotes are organized tonotopically, with hair cells sensitive to high frequencies at the basal end of the papilla, grading into low-frequency hair cells at the apical end.BASED ON MED-EL WWW.MEDEL.COMThe evolution of tympanic middle ears kick-started the evolution of modern inner ears, where sound waves are converted into the electrical signals that are sent to the brain. The inner ear is least developed in the lepidosaurs, most of which retained a relatively small auditory papilla, in some just a few hundred micrometers long. Many lepidosaurs, predominantly diurnal species, also lost their eardrum. Snakes reduced their middle ear, limiting their hearing to frequencies less than 1 kHz, about two octaves above middle C. (For comparison, humans can hear sounds up to about 15 or 16 kHz.) Clearly, hearing was not under strong selective pressure in this group. There are a few exceptions, however. In geckos, for example, which are largely nocturnal, the papillar structure shows unique specializations, accompanied by high sensitivity and strong frequency selectivity. Indeed, the frequency selectivity of gecko auditory nerve fibers exceeds that of many mammals.

One part of the inner ear that did improve in lizards (but not in snakes) is the hair cells, with the papillae developing different areas occupied by two structural types of these sound-responsive cells. One of these hair cell groups responds to sounds below 1 kHz and perhaps corresponds to the ancestral version. The higher-frequency hair cells have a more specialized structure, particularly with regard to the size and height of the stereovilli, with bundle heights and stereovillus numbers varying consistently along the papilla’s length. Taller bundles with fewer stereovilli, which are much less stiff and therefore respond best to low frequencies, are found at one end of the membrane, while shorter, thicker bundles with more stereovilli that respond best to higher frequencies are found at the other end—a frequency distribution known as a tonotopic organization. Still, with the exception of one group of geckos, lizard hearing is limited to below 5 to 8 kHz.

In contrast to the relatively rudimentary lepidosaur inner ear, the auditory papilla of archosaurs (birds, crocodiles, and their relatives) evolved much greater length. Owls, highly proficient nocturnal hunters, boast the longest archosaur papilla, measuring more than 10 millimeters and containing many thousands of hair cells. As in lizards, archosaur hair cells show strong tonotopic organization, with a gradual change in the diameter and height of the stereovillar bundles contributing to the gradually changing frequency sensitivity along the papilla. In addition, the hair cells are divided along and across the basilar membrane, with tall hair cells (THCs) resting on the inner side and the apical end, most distant from the middle ear, grading into short hair cells (SHCs) on the outer side and at the basal end. Interestingly, many SHCs completely lack afferent innervation, which is the only known case of sensory cells lacking a connection to the brain. Instead of transmitting sensory information to the brain, these hair cells likely amplify the signal received by the inner ear. Despite the more complex anatomy, however, bird hearing is also generally limited to between 5 and 8 kHz, with the exception of some owls, which can hear up to 12 kHz.

The mammalian papilla, called the organ of Corti, also evolved to be larger—generally, but not always, longer than those of birds—but the extension in length varies in different lineages.4 Mammalian papillae also have a unique cellular arrangement. The papillae of modern egg-laying monotremes, which likely resemble those of the earliest mammals, include two groups of hair cells separated by numerous supporting pillar cells that form the tunnel of Corti. In any given cross section, there are approximately five inner hair cells (IHCs) on the inner side of the pillar cells, closer to the auditory nerve, and eight outer hair cells (OHCs) on the outer side. In therian mammals (marsupials and placentals), the numbers of each cell group have been much reduced, with only two pillar cells forming the tunnel in any given cross-section, and generally just a single IHC and three or four OHCs, though the functional consequences of this reduction remain unclear. About 90 percent of afferent fibers innervate IHCs, while only 10 percent or fewer innervate OHCs, despite the fact that OHCs account for some 80 percent of all hair cells. As with bird SHCs that lack afferent innervation, there are indications that the main function of OHCs is to amplify the physical sound signal at very low sound-pressure levels.

Therian mammals also evolved another key hearing adaptation: the cochlea. Shortly before marsupial and placental lineages diverged, the elongating hearing organ, which had always been curved, reached full circle. The only way to further increase its length was to form more than one full coil, a state that was reached roughly 120 million years ago. The result is hearing organs with 1.5 to 4 coils and lengths from 7 millimeters (mouse) to 75 millimeters (blue whale). Hearing ranges also diverged, partly depending on the size of the animal (larger mammals tend to have lower upper-frequency limits), but with a number of remarkable specializations, as expected in a lineage that radiated greatly during several evolutionary episodes.

As a result of these adaptations, most mammals have an upper frequency-response limit that well exceeds those of lepidosaurs and archosaurs. Human hearing extends to frequencies of about 15 kHz; a guinea pig can hear sounds up to about 45 kHz; and in the extreme cases of many bats and toothed whales, hearing extends into ultrasonic frequencies, sometimes as high as 180 kHz, allowing these animals to echolocate in air and water. This impressive increase in frequency limits is due to an extremely stiff middle ear, as well as a stiff cochlea. During early therian evolution, the bone of the canal surrounding the soft tissues invaded the supporting ridges of the basilar membrane, creating stiff laminae. Such bony ridges were retained in species perceiving ultrasonic frequencies, but tended to be reduced and replaced by softer connective-tissue supports in those with lower-frequency limits, such as humans.

Amplification within the ear

http://www.the-scientist.com/Sept2015/ear_hair.jpg

HAIRS OF THE EAR: Rows of inner-ear hair cells have villous bundles (blue) on their apical surface that convert sound waves to nervous signals sent to the brain.© STEVE GSCHMEISSNER/SCIENCE SOURCEIn addition to the specialized structures of the middle and inner ears of amniotes that served to greatly increase hearing sensitivity, the hair cells themselves can produce active movements that further amplify sound stimuli. The evolutionarily oldest such active mechanism was discovered in the late 1980s by Jim Hudspeth’s group, then at the University of California, San Francisco, School of Medicine, working with frogs,5 and Andrew Crawford and Robert Fettiplace, then at the University of Cambridge, working with turtles.6 The amplification mechanism, called the active bundle mechanism, probably evolved in the ancestors of vertebrates and helped overcome the viscous forces of the surrounding fluids, which resist movement. When sound stimuli move the hair-cell bundle and thus open transduction channels to admit potassium ions, some calcium ions also enter the cell. These calcium ions bind to and influence the open transduction channels, increasing the speed with which these channels close. Such closing forces are exerted in phase with the incoming sound waves, increasing the distance that the hair cells move in response, and thereby increasing their sensitivity. It is likely that this mechanism operates in all vertebrate hair cells.5 In lizards, my group provided evidence that this bundle mechanism really does operate in the living animal.7

In 1986, a second mechanism of hair cell–driven sound amplification was discovered in mammalian OHCs by Bill Brownell’s group, then at the University of Florida School of Medicine. Brownell and his colleagues showed that mammalian OHCs, but not IHCs, changed their length very rapidly in phase with the signal if exposed to an alternating electrical field.8 Such fields occur when hair cells respond to sound. Subsequent experiments showed that the change in cell length is due to changes in the molecular configuration of a protein, later named prestin, which occurs in high density along the lateral cell membrane of OHCs. In mammals, the force produced by the OHCs is so strong that the entire organ of Corti, which includes all cell types that surround the hair cells and the basilar membrane itself, is driven in an up-and-down motion. This movement can amplify sounds by at least 40dB, allowing very quiet noises to be detected. There is evidence for the independent evolution of specific molecular configurations of prestins that allow for the amplification of very high ultrasonic frequencies in bats and whales.9

Bird ears also appear to produce active forces that amplify sound. The SHCs have bundles comprising up to 300 stereovilli (about three times as many as the bundles of mammalian OHCs),10 and the movement of these bundles probably drives the movement of THCs indirectly via the tectorial membrane. Also, very recent data from the lab of Fettiplace, now at the University of Wisconsin–Madison, suggests that in birds, prestin (albeit in a different molecular form) may work in the plane across the hearing organ (i.e., not up and down as in mammals), perhaps reinforcing the influence of the bundle active mechanism on the THCs via the tectorial membrane.11

Three hundred million years of evolution have resulted in a fascinating variety of ear configurations that, despite their struc­tural diversity, show remarkably similar physiological responses.

In addition to amplifying hair-cell activity, these active mechanisms manifest as spontaneous movements of the hearing organ, oscillating even in the absence of sound stimuli. Such spontaneous movements actually produce sound that is emitted through the middle ear to the outside world and can be measured in the ear canal. These spontaneous otoacoustic emissions (SOAEs) enable remote sensing of what is going on within the inner ear and have permitted increasingly important research on inner-ear mechanisms and new clinical diagnostic methods to monitor the health of the ear’s sensory epithelium. We recently showed that spectral patterns of SOAEs in lizards, birds, and mammals are remarkably similar, despite up to 70-fold differences in the size of the hearing organs, suggesting that there are profound commonalities among the inner ears of amniotes that we still do not really understand.12

Remarkable convergence

Three hundred million years of evolution have resulted in a fascinating variety of ear configurations that, despite their structural diversity, show remarkably similar physiological responses. There are hardly any differences in sensitivity between the hearing of endothermal birds and mammals, and the frequency selectivity of responses is essentially the same in most lizards, birds, and mammals. The combined research efforts of paleontologists, anatomists, physiologists, and developmental biologists over several decades have clarified the major evolutionary steps in all lineages that modified the malleable middle and inner ears into their present-day kaleidoscopic variety of form, yet a surprising consensus in their function.

Geoffrey A. Manley is a retired professor from the Institute of Zoology at the Technical University in Munich, Germany. He is currently a guest scientist in the laboratory of his wife, Christine Köppl, at Oldenburg University in Germany.

References

  1. G.A. Manley, C. Köppl, “Phylogenetic development of the cochlea and its innervation,” Curr Opin Neurobiol, 8:468-74, 1998.
  2. J.A. Clack, “Patterns and processes in the early evolution of the tetrapod ear,” J Neurobiol, 53:251-64, 2002.
  3. T. Kitazawa et al., “Developmental genetic bases behind the independent origin of the tympanic membrane in mammals and diapsids,” Nat Commun, 6:6853, 2015.
  4. G.A. Manley, “Evolutionary paths to mammalian cochleae,” JARO, 13:733-43, 2012.
  5. A.J. Hudspeth, “How the ear’s works work: Mechanoelectrical transduction and amplification by hair cells,” C R Biol, 328:155-62, 2005.
  6. A.C. Crawford, R. Fettiplace, “The mechanical properties of ciliary bundles of turtle cochlear hair cells,” J Physiol, 364:359-79, 1985.
  7. G.A. Manley et al., “In vivo evidence for a cochlear amplifier in the hair-cell bundle of lizards,” PNAS, 98:2826-31, 2001.
  8. B. Kachar et al., “Electrokinetic shape changes of cochlear outer hair cells,” Nature, 322:365-68, 1986.
  9. Y. Liu et al., “Convergent sequence evolution between echolocating bats and dolphins,” Curr Biol, 20:R53-R54, 2010.
  10. C. Köppl et al., “Big and powerful: A model of the contribution of bundle motility to mechanical amplification in hair cells of the bird basilar papilla,” in Concepts and Challenges in the Biophysics of Hearing, ed. N.P. Cooper, D.T. Kemp (Singapore: World Scientific, 2009), 444-50.
  11. M. Beurg et al., “A prestin motor in chicken auditory hair cells: Active force generation in a nonmammalian species,” Neuron, 79:69-81, 2013.
  12. C. Bergevin et al., “Salient features of otoacoustic emissions are common across tetrapod groups and suggest shared properties of generation mechanisms,” PNAS, 112:3362-67, 2015.

Sea Lion: © iStock/LFStewart; Squirrel: © Erik Mandre/Shutterstock; Frog: ©Frank B. Yuwono/Shutterstock; Owl: ©XNature.Photography/Shutterstock; Lizard: ©Andrew Wijesuriya/Shutterstock; Bat: © iStock/GlobalP; Ostrich: © Jamen Percy/Shutterstock; Dog: ©Annette Shaff/Shutterstock; Lynx: © Dmitri Gomon/Shutterstock

Correction (September 15, 2015): Citation #8 of this story has been updated to accurately reflect the research referenced in the text. The Scientist regrets the error.

Tags

vertebratessensory biologyhearingevolutionary biologyevolution and amniotes

Early Hominin Hearing

http://www.the-scientist.com//?articles.view/articleNo/44119/title/Early-Hominin-Hearing/

Based on the structure of fossilized skulls and ear bones, researchers learn that early hominins heard sounds best between the frequencies that humans and chimpanzees do.

By Karen Zusi | September 29, 2015

africanus skullWIKIMEDIA, JOSÉ BRAGA

http://www.the-scientist.com/images/Nutshell/Sept2015/hominin310.jpg

Early hominin species Australopithecus africanus andParanthropus robustus, which lived around 2 million years ago, possessed hearing capabilities largely similar to modern-day chimpanzees but with a few differences that made their sense more akin to that of humans, according to a recent study. The results were reported last week (September 25) in Science Advances.

“We know that the hearing patterns, or audiograms, in chimpanzees and humans are distinct because their hearing abilities have been measured in the laboratory in living subjects,” study coauthor Rolf Quam of Binghamton University in New York said in a press release. “So we were interested in finding out when this human-like hearing pattern first emerged during our evolutionary history.”

Quam and an international team of researchers studied the anatomy of the ear in three complete fossilized specimens, as well as several partial specimens, from South Africa. The team reconstructed the size and relative proportions of up to six different structures—such as the stapes, a middle ear bone—using 3-D CT scans. The researchers then used a published model to predict how the early hominins may have heard, based on these measurements.

Both species of early hominin evolved an anatomy that allowed them to hear sounds at slightly higher frequencies than chimpanzees, best in the 1.0 kHz to 3.5 kHz range. In comparison, chimpanzees can hear sounds best between 1.0 kHz and 3.0 kHz. Humans can typically hear sounds best between 1.0 kHz and 4.5 kHz; this range encompasses most sounds formed in spoken language.

“[The early hominins] didn’t hear as well as humans, and they are more like chimps,” Quam told The New York Times. But the researchers speculated that the changes in hearing anatomy over time were driven by a lifestyle spent on the open savanna, where short-range communication would have been favored.

“Hearing abilities are closely tied with verbal communication,” Quam wrote at The Conversation. “By figuring out when certain hearing capacities emerged during our evolutionary history, we might be able to shed some light on when spoken language started to evolve.”

Tags

paleontologyhuman evolutionhomininhearingfossilsCT scan and chimpanzee

Hearing Explained

Observe the ins and outs of how our ears perceive sound.

By The Scientist Staff | September 1, 2015

http://www.the-scientist.com//?articles.view/articleNo/43884/title/Hearing-Explained/

Human Hearing: A Primer

How the human ear translates sound waves into nervous impulses

By The Scientist Staff | September 1, 2015

https://youtu.be/46aNGGNPm7s

When sound enters the ear canal, it vibrates the tympanic membrane, or eardrum. These vibrations are passed through the inner ear via three small bones called ossicles: the malleus, the incus, and the stapes. Finally, vibrations of the stapes stimulate the movement of a fluid called perilymph within the bony labyrinth of the inner ear.

See labeled infographic: JPG© CATHERINE DELPHIA

hearing

http://www.the-scientist.com/images/August2015/Primer_2.jpg

Perilymph fills the both the vestibular and tympanic ducts of the cochlea. Between these two channels lies the cochlear duct, which is home to the organ of Corti. There, the sound induced movement of perilymph in the cochlea is translated to an electrical signal that is sent to the brain for processing.

An electrical signal is generated by inner hair cells that sit above the basilar membrane, which separates the cochlear duct from the tympanic duct. As the basilar membrane vibrates in response to fluid movement, it pushes the hair cells along another membrane, known as the tectorial membrane, which shifts laterally to bend projections at the tips of the cells, called stereocilia.

The bending of the stereocilia results in the depolarization of the inner hair cell and initiates a nerve impulse through the spiral ganglion neuron at the base of the cell. A series of outer hair cells serves to mechanically amplify the vibrations that trigger the inner hair cells to fire. High-frequency sounds stimulate hair cells at the base of the cochlea, while low-frequency sounds stimulate hair cells at the apex.

See labeled infographic: JPG© CATHERINE DELPHIA

HAIRS OF THE EAR ear_hair

http://www.the-scientist.com/images/August2015/Primer_1.jpg

Tags

spiral ganglion neuronssensory biologyneuroscienceneuronsmechanotransductionmechanoreception and hearing

Author of books:
Brain Mechanisms of Vision (1991, with David H. Hubel)
Colloquium on Vision: From Photon to Perception (200, with John Dowling and Lubert Stryer)
Brain and Visual Perception: The Story of a 25-Year Collaboration (2005, with David H. Hubel)

Professor: Physiology, Harvard University (1964-74)
Professor: Neurobiology, Harvard University (1974-84)
Professor: Neurobiology, Rockefeller University (1984-98)
Administrator: President, Rockefeller University (1991-98)

The interplay of light and life

Lubert Stryer (born March 2, 1938, in Tianjin, China) is the Mrs. George A. Winzer Professor of Cell Biology, Emeritus, at the Stanford University School of Medicine.[1][2] His research over more than four decades has been centered on the interplay of light and life. In 2007 he received the National Medal of Science for elucidating the biochemical basis of signal amplification in vision, pioneering the development of high density micro-arrays for genetic analysis, and authoring the biochemistry textbook.[3]

Stryer received his B.S. degree from the University of Chicago in 1957 and his M.D. degree from Harvard Medical School. He was a Helen Hay Whitney Research Fellow[4] in the Department of Physics at Harvard and then at the MRC Laboratory of Molecular Biology[5] in Cambridge, England, before joining the faculty of the Department of Biochemistry at Stanford in 1963. In 1969 he moved to Yale to become Professor of Molecular Biophysics and Biochemistry, and in 1976, he returned to Stanford to head a new Department of Structural Biology.[6]

Stryer and coworkers pioneered the use of fluorescence spectroscopy, particularly Förster resonance energy transfer (FRET), to monitor the structure and dynamics of biological macromolecules.[7][8] In 1967, Stryer and Haugland showed that the efficiency of energy transfer depends on the inverse sixth power of the distance between the donor and acceptor,[9][10] as predicted by Förster’s theory. They proposed that energy transfer can serve as a spectroscopic ruler to reveal proximity relationships in biological macromolecules.

A second contribution was Stryer’s discovery of the primary stage of amplification in visual excitation.[11][12] Stryer, together with Fung and Hurley, showed that a single photoexcited rhodopsin molecule activates many molecules of transducin, which in turn activate many molecules of a cyclic GMP phosphodiesterase. Stryer’s laboratory has also contributed to our understanding of the role of calcium in visual recovery and adaptation.[13][14][15]

Stryer participated in developing light-directed, spatially addressable parallel chemical synthesis for the synthesis of peptides and polynucleotides.[16][17][18] Light-directed combinatorial synthesis has been used by Stephen Fodor and coworkers at Affymetrix to make DNA arrays containing millions of different sequences for genetic analyses.

Download Biochemistry Jeremy M Berg John L Tymoczko …

Dec 13, 2014 – Uploaded by Marquita Iraely

Download Biochemistry Jeremy M Berg John L Tymoczko Lubert Stryer PDF. Marquita Iraely …

Macmillan Higher Education: Biochemistry Seventh Edition …

http://www.macmillanhighered.com/Catalog/…/biochemistry-seventhedition-be…

Jeremy M. Berg , John L. Tymoczko (Carleton College) , Lubert Stryer (Stanford … this extraordinary textbook has helped shape the way biochemistry is taught, …

Loose-leaf Version for Biochemistry Seventh Edition Edition

Read Full Post »

« Newer Posts - Older Posts »