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Summary to Metabolomics

Summary to Metabolomics

Author and Curator: Larry H. Bernstein, MD, FCAP 

This concludes a long step-by-step journey into rediscovering biological processes from the genome as a framework to the remodeled and reconstituted cell through a number of posttranscription and posttranslation processes that modify the proteome and determine the metabolome.  The remodeling process continues over a lifetime. The process requires a balance between nutrient intake, energy utilization for work in the lean body mass, energy reserves, endocrine, paracrine and autocrine mechanisms, and autophagy.  It is true when we look at this in its full scope – What a creature is man?

http://masspec.scripps.edu/metabo_science/recommended_readings.php
 Recommended Readings and Historical Perspectives

Metabolomics is the scientific study of chemical processes involving metabolites. Specifically, metabolomics is the “systematic study of the unique chemical fingerprints that specific cellular processes leave behind”, the study of their small-molecule metabolite profiles.[1] The metabolome represents the collection of all metabolites in a biological cell, tissue, organ or organism, which are the end products of cellular processes.[2] mRNA gene expression data and proteomic analyses reveal the set of gene products being produced in the cell, data that represents one aspect of cellular function. Conversely, metabolic profiling can give an instantaneous snapshot of the physiology of that cell. One of the challenges of systems biology and functional genomics is to integrate proteomic, transcriptomic, and metabolomic information to provide a better understanding of cellular biology.

The term “metabolic profile” was introduced by Horning, et al. in 1971 after they demonstrated that gas chromatography-mass spectrometry (GC-MS) could be used to measure compounds present in human urine and tissue extracts. The Horning group, along with that of Linus Pauling and Arthur B. Robinson led the development of GC-MS methods to monitor the metabolites present in urine through the 1970s.

Concurrently, NMR spectroscopy, which was discovered in the 1940s, was also undergoing rapid advances. In 1974, Seeley et al. demonstrated the utility of using NMR to detect metabolites in unmodified biological samples.This first study on muscle highlighted the value of NMR in that it was determined that 90% of cellular ATP is complexed with magnesium. As sensitivity has improved with the evolution of higher magnetic field strengths and magic angle spinning, NMR continues to be a leading analytical tool to investigate metabolism. Efforts to utilize NMR for metabolomics have been influenced by the laboratory of Dr. Jeremy Nicholson at Birkbeck College, University of London and later at Imperial College London. In 1984, Nicholson showed 1H NMR spectroscopy could potentially be used to diagnose diabetes mellitus, and later pioneered the application of pattern recognition methods to NMR spectroscopic data.

In 2005, the first metabolomics web database, METLIN, for characterizing human metabolites was developed in the Siuzdak laboratory at The Scripps Research Institute and contained over 10,000 metabolites and tandem mass spectral data. As of September 2012, METLIN contains over 60,000 metabolites as well as the largest repository of tandem mass spectrometry data in metabolomics.

On 23 January 2007, the Human Metabolome Project, led by Dr. David Wishart of the University of Alberta, Canada, completed the first draft of the human metabolome, consisting of a database of approximately 2500 metabolites, 1200 drugs and 3500 food components. Similar projects have been underway in several plant species, most notably Medicago truncatula and Arabidopsis thaliana for several years.

As late as mid-2010, metabolomics was still considered an “emerging field”. Further, it was noted that further progress in the field depended in large part, through addressing otherwise “irresolvable technical challenges”, by technical evolution of mass spectrometry instrumentation.

Metabolome refers to the complete set of small-molecule metabolites (such as metabolic intermediates, hormones and other signaling molecules, and secondary metabolites) to be found within a biological sample, such as a single organism. The word was coined in analogy with transcriptomics and proteomics; like the transcriptome and the proteome, the metabolome is dynamic, changing from second to second. Although the metabolome can be defined readily enough, it is not currently possible to analyse the entire range of metabolites by a single analytical method. The first metabolite database(called METLIN) for searching m/z values from mass spectrometry data was developed by scientists at The Scripps Research Institute in 2005. In January 2007, scientists at the University of Alberta and the University of Calgary completed the first draft of the human metabolome. They catalogued approximately 2500 metabolites, 1200 drugs and 3500 food components that can be found in the human body, as reported in the literature. This information, available at the Human Metabolome Database (www.hmdb.ca) and based on analysis of information available in the current scientific literature, is far from complete.

Each type of cell and tissue has a unique metabolic ‘fingerprint’ that can elucidate organ or tissue-specific information, while the study of biofluids can give more generalized though less specialized information. Commonly used biofluids are urine and plasma, as they can be obtained non-invasively or relatively non-invasively, respectively. The ease of collection facilitates high temporal resolution, and because they are always at dynamic equilibrium with the body, they can describe the host as a whole.

Metabolites are the intermediates and products of metabolism. Within the context of metabolomics, a metabolite is usually defined as any molecule less than 1 kDa in size.
A primary metabolite is directly involved in the normal growth, development, and reproduction. A secondary metabolite is not directly involved in those processes.  By contrast, in human-based metabolomics, it is more common to describe metabolites as being either endogenous (produced by the host organism) or exogenous. Metabolites of foreign substances such as drugs are termed xenometabolites. The metabolome forms a large network of metabolic reactions, where outputs from one enzymatic chemical reaction are inputs to other chemical reactions.

Metabonomics is defined as “the quantitative measurement of the dynamic multiparametric metabolic response of living systems to pathophysiological stimuli or genetic modification”. The word origin is from the Greek μεταβολή meaning change and nomos meaning a rule set or set of laws. This approach was pioneered by Jeremy Nicholson at Imperial College London and has been used in toxicology, disease diagnosis and a number of other fields. Historically, the metabonomics approach was one of the first methods to apply the scope of systems biology to studies of metabolism.

There is a growing consensus that ‘metabolomics’ places a greater emphasis on metabolic profiling at a cellular or organ level and is primarily concerned with normal endogenous metabolism. ‘Metabonomics’ extends metabolic profiling to include information about perturbations of metabolism caused by environmental factors (including diet and toxins), disease processes, and the involvement of extragenomic influences, such as gut microflora. This is not a trivial difference; metabolomic studies should, by definition, exclude metabolic contributions from extragenomic sources, because these are external to the system being studied.

Toxicity assessment/toxicology. Metabolic profiling (especially of urine or blood plasma samples) detects the physiological changes caused by toxic insult of a chemical (or mixture of chemicals).

Functional genomics. Metabolomics can be an excellent tool for determining the phenotype caused by a genetic manipulation, such as gene deletion or insertion. Sometimes this can be a sufficient goal in itself—for instance, to detect any phenotypic changes in a genetically-modified plant intended for human or animal consumption. More exciting is the prospect of predicting the function of unknown genes by comparison with the metabolic perturbations caused by deletion/insertion of known genes.

Nutrigenomics is a generalised term which links genomics, transcriptomics, proteomics and metabolomics to human nutrition. In general a metabolome in a given body fluid is influenced by endogenous factors such as age, sex, body composition and genetics as well as underlying pathologies. The large bowel microflora are also a very significant potential confounder of metabolic profiles and could be classified as either an endogenous or exogenous factor. The main exogenous factors are diet and drugs. Diet can then be broken down to nutrients and non- nutrients.

http://en.wikipedia.org/wiki/Metabolomics

Jose Eduardo des Salles Roselino

The problem with genomics was it was set as explanation for everything. In fact, when something is genetic in nature the genomic reasoning works fine. However, this means whenever an inborn error is found and only in this case the genomic knowledge afterwards may indicate what is wrong and not the completely way to put biology upside down by reading everything in the DNA genetic as well as non-genetic problems.

Coordination of the transcriptome and metabolome by the circadian clock PNAS 2012

Coordination of the transcriptome and metabolome by the circadian clock PNAS 2012

analysis of metabolomic data and differential metabolic regulation for fetal lungs, and maternal blood plasma

conformational changes leading to substrate efflux.img

conformational changes leading to substrate efflux.img

The cellular response is defined by a network of chemogenomic response signatures.

The cellular response is defined by a network of chemogenomic response signatures.

Dynamic Construct of the –Omics

Dynamic Construct of the –Omics

 genome cartoon

genome cartoon

central dogma phenotype

central dogma phenotype

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Functional Correlates of Signaling Pathways

Author and Curator: Larry H. Bernstein, MD, FCAP

 

We here move on to a number of specific, key published work on signaling, and look at the possible therapeutic applications to disease states.

Scripps Research Professor Wolfram Ruf and colleagues have identified a key connection between

  • the signaling pathways and the immune system spiraling out of control involving
  • the coagulation system and vascular endothelium that,
  • if disrupted may be a target for sepsis. (Science Daily, Feb 29, 2008).

It may be caused by a bacterial infection that enters the bloodstream, but

  • we now recognize the same cascade not triggered by bacterial invasion.

The acute respiratory distress syndrome (ARDS) has been defined as

  • a severe form of acute lung injury featuring
  • pulmonary inflammation and increased capillary leak.

ARDS is associated with a high mortality rate and accounts for 100,000 deaths annually in the United States. ARDS may arise in a number of clinical situations, especially in patients with sepsis. A well-described pathophysiological model of ARDS is one form of

  • the acute lung inflammation mediated by
  1. neutrophils,
  2. cytokines, and
  3. oxidant stress.

Neutrophils are major effect cells at the frontier of

  • innate immune responses, and they play
  • a critical role in host defense against invading microorganisms.

The tissue injury appears to be related to

  • proteases and toxic reactive oxygen radicals
  • released from activated neutrophils.

In addition, neutrophils can produce cytokines and chemokines that

enhance the acute inflammatory response.

Neutrophil accumulation in the lung plays a pivotal role in the pathogenesis of acute lung injury during sepsis. Directed movement of neutrophils is

  • mediated by a group of chemoattractants,
  • especially CXC chemokines.

Local lung production of CXC chemokines is intensified during experimental sepsis induced by cecal ligation and puncture (CLP).

Sepsis, Multi-organ Dysfunction Syndrome, and Septic Shock: A Conundrum of Signaling Pathways Cascading Out of Control

http://pharmaceuticalintelligence.com/2012/10/13/sepsis-multi-organ-dysfunction-syndrome-and-septic-shock-a-conundrum-of-signaling-pathways-cascading-out-of-control/

Integrins and extracellular matrix in mechanotransduction

ligand binding of integrins

ligand binding of integrins

Integrins are a family of cell surface receptors which

mediate cell–matrix and cell–cell adhesions.

Among other functions they provide an important

mechanical link between the cells external and intracellular environments while

the adhesions that they form also have critical roles in cellular signal-transduction.

Cell–matrix contacts occur at zones in the cell surface where

adhesion receptors cluster and when activated

the receptors bind to ligands in the extracellular matrix.

The extracellular matrix surrounds the cells of tissues and forms the

structural support of tissue which is particularly important in connective tissues.

Cells attach to the extracellular matrix through

specific cell-surface receptors and molecules

including integrins and transmembrane proteoglycans.

The integrin family of αβ heterodimeric receptors act as

cell adhesion molecules

connecting the ECM to the actin cytoskeleton.

The actin cytoskeleton is involved in the regulation of

1.cell motility,

2.cell polarity,

3.cell growth, and

4.cell survival.

The combination of αβ subunits determines

binding specificity and

signaling properties.

Both α and β integrin subunits contain two separate tails, which

penetrate the plasma membrane and possess small cytoplasmic domains which facilitate

the signaling functions of the receptor.

There is some evidence that the β subunit is the principal site for

binding of cytoskeletal and signaling molecules,

whereas the α subunit has a regulatory role. The integrin tails

link the ECM to the actin cytoskeleton within the cell and with cytoplasmic proteins,

such as talin, tensin, and filamin. The extracellular domains of integrin receptors bind the ECM ligands.

binding of integrins depends on ECM divalent cations ch19

binding of integrins depends on ECM divalent cations ch19

integrin coupled to F-actin via linker

integrin coupled to F-actin via linker

http://www.nature.com/nrm/journal/vaop/ncurrent/images/nrm3896-f4.jpg

Schematic of the ‘focal adhesion clutch’ on stiff (a) versus soft (b) extracellular matrix (ECM). In all cases, integrins are coupled to F-actin via linker proteins (for example, talin and vinculin). The linker proteins move backwards (as indicated by the small arrows) as F-actin also moves backwards, under pushing forces from actin polymerization and/or pulling forces from myosin II activity. This mechanism transfers force from actin to integrins, which pull on the ECM. A stiff ECM (a) resists this force so that the bound integrins remain immobile. A compliant matrix (b) deforms under this force (as indicated by the compressed ECM labelled as deformed matrix) so that the bound integrins can also move backwards. Their movement reduces the net loading rate on all the force-bearing elements, which results in altered cellular responses

The ECM is a complex mixture of matrix molecules, including –

  • glycoproteins, collagens, laminins, glycosaminoglycans, proteoglycans,
  • and nonmatrix proteins, – including growth factors

The integrin receptor formed from the binding of α and β subunits is

  • shaped like a globular head supported by two rod-like legs (Figure 1).

Most of the contact between the two subunits occurs in the head region, with

  • the intracellular tails of the subunits forming the legs of the receptor.

Integrin recognition of ligands is not constitutive but

  • is regulated by alteration of integrin affinity for ligand binding.

For integrin binding to ligands to occur

  • the integrin must be primed and activated, both of which involve
  • conformational changes to the receptor.

Linking integrin conformation to function

Figure  Integrin binding to extracellular matrix (ECM). Conformational changes to integrin structure and clustering of subunits which allow enhanced function of the receptor.

Integrins work alongside other proteins such as

cadherins,

immunoglobulin superfamily

cell adhesion molecules,

selectins, and

syndecans

to mediate

cell–cell and

cell–matrix interactions and communication.

Activation of adhesion receptors triggers the formation of matrix contacts in which

bound matrix components,

adhesion receptors,

and associated intracellular cytoskeletal and signaling molecules

form large functional, localized multiprotein complexes.

Cell–matrix contacts are important in a variety of different cell and

tissue properties including

1.embryonic development,

2.inflammatory responses,

3.wound healing,

4.and adult tissue homeostasis.

Integrin extracellular binding activity is regulated from inside the cell and binding to the ECM induces signals that are transmitted into the cell. This bidirectional signaling requires

dynamic,

spatially, and

temporally regulated formation and

disassembly of multiprotein complexes that

form around the short cytoplasmic tails of integrins.

Ligand binding to integrin family members leads to clustering of integrin molecules in the plasma membrane and recruitment of actin filaments and intracellular signaling molecules to the cytoplasmic domain of the integrins. This forms focal adhesion complexes which are able to maintain

not only adhesion to the ECM

but are involved in complex signaling pathways

which include establishing

1.cell polarity,

2.directed cell migration, and

3.maintaining cell growth and survival.

Initial activation through integrin adhesion to matrix recruits up to around 50 diverse signaling molecules

to assemble the focal adhesion complex

which is capable of responding to environmental stimuli efficiently.

Mapping of the integrin

adhesome binding and signaling interactions

a network of 156 components linked together which can be modified by 690 interactions.

Genetic programming occurs with the binding of integrins to the ECM

Signal transduction pathway activation arising from integrin-ECM binding results in

  • changes in gene expression of cells and
  • leads to alterations in cell and tissue function.

Various different effects can arise depending on the

1.cell type,

2.matrix composition, and

3.integrins activated

It has been suggested that integrin-type I collagen interaction is necessary for

  • the phosphorylation and activation of osteoblast-specific transcription factors
  • present in committed osteoprogenitor cells.

During mechanical loading/stimulation of chondrocytes there is an

  1. influx of ions across the cell membrane resulting from
  2. activation of mechanosensitive ion channels
  3. which can be inhibited by subunit-specific anti-integrin blocking antibodies or RGD peptides.

Using these strategies it was identified that

  • α5β1 integrin is a major mechanoreceptor in articular chondrocyte
  • responses to mechanical loading/stimulation.

Osteoarthritic chondrocytes show a depolarization response to 0.33 Hz stimulation

  • in contrast to the hyperpolarization response of normal chondrocytes.

The mechanotransduction pathway in chondrocytes derived from normal and osteoarthritic cartilage

  • both involve recognition of the mechanical stimulus
  • by integrin receptors resulting in
  • the activation of integrin signaling pathways
  • leading to the generation of a cytokine loop.

Normal and osteoarthritic chondrocytes show differences

  • at multiple stages of the mechanotransduction cascade.
Signaling pathways activated in chondrocytes

Signaling pathways activated in chondrocytes

http://dx.doi.org/10.1016/j.matbio.2014.08.007

Chondrocyte integrins are important mediators of cell–matrix interactions in cartilage

  • by regulating the response of the cells to signals from the ECM that
  1. control cell proliferation,
  2. survival,
  3. differentiation,
  4. matrix remodeling.

Integrins participate in development and maintenance of the tissue but also

  • in pathological processes related to matrix destruction, where
  • they likely play a role in the progression of OA.

Cellular adaptation to mechanical stress: role of integrins, Rho, cytoskeletal tension and mechanosensitive ion channels

Cells exhibited four types of mechanical responses:

(1) an immediate viscoelastic response;

(2) early adaptive behavior characterized by pulse-to-pulse attenuation in response to oscillatory forces;

(3) later adaptive cell stiffening with sustained (>15 second) static stresses; and

(4) a large-scale repositioning response with prolonged (>1 minute) stress.

Importantly, these adaptation responses differed biochemically.

The immediate and early responses were affected by

chemically dissipating cytoskeletal prestress (isometric tension), whereas

the later adaptive response was not.

The repositioning response was prevented by

inhibiting tension through interference with Rho signaling,

similar to the case of the immediate and early responses, but it was also prevented by

blocking mechanosensitive ion channels or

by inhibiting Src tyrosine kinases.

All adaptive responses were suppressed by cooling cells to 4°C to slow biochemical remodeling. Thus, cells use multiple mechanisms to sense and respond to static and dynamic changes in the level of mechanical stress applied to integrins.

Microtubule-Stimulated ADP Release, ATP Binding, and Force Generation In Transport Kinesins

All three classes of molecular motor proteins are now known to be

  • large protein families with diverse cellular functions.

Both the kinesin family and the myosin family have been defined and their proteins grouped into subfamilies. Finally, the elusive cytoplasmic version of dynein was identified and a multigene family of flagellar and cytoplasmic dyneins defined. Members of a given motor protein family share

  • significant homology in their motor domains with the defining member,
  • kinesin, dynein or myosin; but they also contain
  • unique protein domains that are specialized for interaction with different cargoes.

This large number of motor proteins may reflect

  • the number of cellular functions that require force generation or movement,
  • ranging from mitosis to morphogenesis to transport of vesicles.

Kinesins are a large family of microtubule (MT)-based motors that play important roles in many cellular activities including

mitosis,

motility, and

intracellular transport

Their involvement in a range of pathological processes

  • also highlights their significance as therapeutic targets and
  • the importance of understanding the molecular basis of their function

They are defined by their motor domains that contain both

  • the microtubule (MT) and
  • ATP binding sites.

Three ATP binding motifs—

  1. the P-loop,
  2. switch I,
  3. switch II–

are highly conserved among

  1. kinesins,
  2. myosin motors, and
  • small GTPases.

They share a conserved mode of MT binding such that

  • MT binding,
  • ATP binding, and
  • hydrolysis

are functionally coupled for efficient MT-based work.

The interior of a cell is a hive of activity, filled with

  • proteins and other items moving from one location to another.

A network of filaments called microtubules forms tracks

  • along which so-called motor proteins carry these items.

Kinesins are one group of motor proteins, and a typical kinesin protein has

  • one end (called the ‘motor domain’) that can attach itself to the microtubules.

The other end links to the cargo being carried, and a ‘neck’ connects the two. When two of these proteins work together,

  • flexible regions of the neck allow the two motor domains to move past one another,
  • which enable the kinesin to essentially walk along a microtubule in a stepwise manner.

Although the two kinesins have been thought to move along the microtubule tracks in different ways, Atherton et al. find that the core mechanism used by their motor domains is the same.

When a motor domain binds to the microtubule, its shape changes,

  • first stimulating release of the breakdown products of ATP from the previous cycle.

This release makes room for a new ATP molecule to bind. The structural changes caused by ATP binding

  • produce larger changes in the flexible neck region that
  • enable individual motor domains within a kinesin pair to
  • co-ordinate their movement and move in a consistent direction.

The major and largely invariant point of contact between kinesin motor domains and the MT is helix-α4,

  • which lies at the tubulin intradimer interface.

The conformational changes in functionally important regions of each motor domain are described,

  • starting with the nucleotide-binding site,
  • from which all other conformational changes emanate.

The nucleotide-binding site (Figure 2) has three major elements:

(1) the P-loop (brown) is visible in all our reconstructions;

(2) loop9 (yellow, contains switch I) undergoes major conformational changes through the ATPase cycle; and

(3) loop11 (red, contains switch II) that connects strand-β7 to helix-α4, the conformation and flexibility of which is

  • determined by MT binding and motor nucleotide state.

Movement and extension of helix-α6 controls neck linker docking

the N-terminus of helix-α6 is closely associated with elements of the nucleotide binding site suggesting that

  • its conformation alters in response to different nucleotide states.

Further,

  • because the orientation of helix-α6 with respect to helix-α4 controls neck linker docking and
  • because helix-α4 is held against the MT during the ATPase cycle,
    • conformational changes in helix-α6 control movement of the neck linker.

Mechanical amplification and force generation involves conformational changes across the motor domain

A key conformational change in the motor domain following Mg-ATP binding is

  • peeling of the central β-sheet from the C-terminus of helix-α4 increasing their separation;
  • this is required to accommodate rotation of helix-α6 and consequent neck linker docking

ATP binding draws loop11 and loop9 closer together; causing

(1) tilting of most of the motor domain not contacting the MT towards the nucleotide-binding site,

(2) rotation, translation, and extension of helix-α6 which we propose contributes to force generation, and

(3) allows neck linker docking and biases movement of the 2nd head towards the MT plus end.

In both motors, microtubule binding promotes

ordered conformations of conserved loops that

stimulate ADP release,

enhance microtubule affinity and

prime the catalytic site for ATP binding.

ATP binding causes only small shifts of these nucleotide-coordinating loops but induces

large conformational changes elsewhere that

allow force generation and

neck linker docking towards the microtubule plus end.

The study presents evidence provide evidence for a conserved ATP-driven

mechanism for kinesins and

reveals the critical mechanistic contribution of the microtubule interface.

Phosphorylation at endothelial cell–cell junctions: Implications for VE-cadherin function

This review summarizes the role of VE-cadherin phosphorylation in the regulation of endothelial cell–cell junctions and highlights how this affects vascular permeability and leukocyte extravasation.

The vascular endothelium is the inner lining of blood vessels and

forms a physical barrier between the vessel lumen and surrounding tissue;

controlling the extravasation of fluids,

plasma proteins and leukocytes.

Changes in the permeability of the endothelium are tightly regulated. Under basal physiological conditions, there is a continuous transfer of substances across the capillary beds. In addition the endothelium can mediate inducible,

transient hyperpermeability

in response to stimulation with inflammatory mediators,

which takes place primarily in post-capillary venules

However, when severe, inflammation may result in dysfunction of the endothelial barrier

  • in various parts of the vascular tree, including large veins, arterioles and capillaries.

Dysregulated permeability is observed in various pathological conditions, such as

  • tumor-induced angiogenesis,
  • cerebrovascular accident and
  • atherosclerosis.

Two fundamentally different pathways regulate endothelial permeability,

  1. the transcellular and
  2. paracellular pathways.

Solutes and cells can pass through the body of endothelial cells via the transcellular pathway, which includes

  • vesicular transport systems,
  • fenestrae, and
  • biochemical transporters.

The paracellular route is controlled by

  • the coordinated opening and closing of endothelial junctions and
  • thereby regulates traffic across the intercellular spaces between endothelial cells.

Endothelial cells are connected by

tight, gap and

adherens junctions,

of which the latter, and particularly the adherens junction component,

vascular endothelial (VE)-cadherin,

are of central importance for the initiation and stabilization of cell–cell contacts.

Although multiple adhesion molecules are localized at endothelial junctions,

  • blocking the adhesive function of VE-cadherin using antibodies
  • is sufficient to disrupt endothelial junctions and
  • to increase endothelial monolayer permeability both in vitro and in vivo.

Like other cadherins, VE-cadherin mediates adhesion via

  • homophilic, calcium-dependent interactions.

This cell–cell adhesion

is strengthened by binding of cytoplasmic proteins, the catenins,

to the C-terminus of VE-cadherin.

VE-cadherin can directly bind

  • β-catenin and plakoglobin, which
  • both associate with the actin binding protein α-catenin.

Initially, α-catenin was thought to directly anchor cadherins to the actin cytoskeleton, but recently it became clear that

  • α-catenin cannot bind to both β-catenin and actin simultaneously.

Numerous lines of evidence indicate that p120-catenin

  • promotes VE-cadherin surface expression and stability at the plasma membrane.

Different models are proposed that describe how

  • p120-catenin regulates cadherin membrane dynamics, including the hypothesis
  • that p120-catenin functions as a ‘cap’ that prevents the interaction of VE-cadherin
  • with the endocytic membrane trafficking machinery.

In addition, p120-catenin might regulate VE-cadherin internalization

  • through interactions with small GTPases.

Cytoplasmic p120-catenin, which is not bound to VE-cadherin, has been shown to

decrease RhoA activity,

elevate active Rac1 and Cdc42, and thereby is thought

to regulate actin cytoskeleton organization and membrane trafficking.

The intact cadherin-catenin complex is required for proper functioning of the adherens junction.

Several mechanisms may be involved in the

  • regulation of the organization and function of the cadherin–catenin complex, including
  1. endocytosis of the complex,
  2. VE-cadherin cleavage and
  3. actin cytoskeleton reorganization.

The remainder of this review primarily focuses on the

role of tyrosine phosphorylation in the control of VE-cadherin-mediated cell–cell adhesion.

Regulation of the adhesive function of VE-cadherin by tyrosine phosphorylation

It is a widely accepted concept that tyrosine phosphorylation of

  • components of the VE–cadherin-catenin complex
  • Correlates with the weakening of cell–cell adhesion.

A general idea has emerged that

tyrosine phosphorylation of the VE-cadherin complex

leads to the uncoupling of VE-cadherin from the actin cytoskeleton

through dissociation of catenins from the cadherin.

However, tyrosine phosphorylation of VE-cadherin

  • is required for efficient transmigration of leukocytes.

This suggests that VE-cadherin-mediated cell–cell contacts

1.are not just pushed open by the migrating leukocytes, but play

2.a more active role in the transmigration process.

A schematic overview of leukocyte adhesion-induced signals leading to VE-cadherin phosphorylation

Regulation of the integrity of endothelial cell–cell contacts by phosphorylation of VE-cadherin.

Regulation of the integrity of endothelial cell–cell contacts by phosphorylation of VE-cadherin

Regulation of the integrity of endothelial cell–cell contacts by phosphorylation of VE-cadherin

N-glycosylation status of E-cadherin controls cytoskeletal dynamics through the organization of distinct β-catenin- and γ-catenin-containing AJs

N-glycosylation of E-cadherin has been shown to inhibit cell–cell adhesion.

Specifically, our recent studies have provided evidence that

  • the reduction of E-cadherin N-glycosylation
  • promoted the recruitment of stabilizing components,
  • vinculin and serine/ threonine protein phosphatase 2A (PP2A), to adherens junctions (AJs)
  • and enhanced the association of AJs with the actin cytoskeleton.

Here, we examined the details of how

N-glycosylation of E-cadherin affected the molecular organization of AJs and their cytoskeletal interactions.

Using the hypoglycosylated E-cadherin variant, V13, we show that

V13/β-catenin complexes preferentially interacted with PP2A and with the microtubule motor protein dynein.

This correlated with dephosphorylation of the microtubule-associated protein tau, suggesting that

increased association of PP2A with V13-containing AJs promoted their tethering to microtubules.

These studies provide the first mechanistic insights into how N-glycosylation of E-cadherin drives changes in AJ composition through

  • the assembly of distinct β-catenin- and γ-catenin-containing scaffolds that impact the interaction with different cytoskeletal components

Cytoskeletal Basis of Ion Channel Function in Cardiac Muscle

MacKinnon. Fig 1  Ion channels exhibit three basic properties

MacKinnon. Fig 1 Ion channels exhibit three basic properties

In order to contract and accommodate the repetitive morphological changes induced by the cardiac cycle, cardiomyocytes

depend on their highly evolved and specialized cytoskeletal apparatus.

Defects in components of the cytoskeleton, in the long term,

affect the ability of the cell to compensate at both functional and structural levels.

In addition to the structural remodeling,

the myocardium becomes increasingly susceptible to altered electrical activity leading to arrhythmogenesis.

The development of arrhythmias secondary to structural remodeling defects has been noted, although the detailed molecular mechanisms are still elusive.

subjects with severe left ventricular chamber dilation such as in DCM can have left bundle branch block (LBBB), while right bundle branch block (RBBB) is more characteristic of right ventricular failure.  LBBB and RBBB have both been repeatedly associated with AV block in heart failure.

The impact of volume overload on structural and electro-cardiographic alterations has been noted in cardiomyopathy patients treated with left ventricular assist device (LVAD) therapy, which puts the heart at mechanical rest.

In LVAD-treated subjects,

QRS- and both QT- and QTc duration decreased,

suggesting that QRS- and QT-duration are significantly influenced by mechanical load and

that the shortening of the action potential duration contributes to the improved contractile performance after LVAD support.

An early postoperative period study after cardiac unloading therapy in 17 HF patients showed that in the first two weeks after LVAD implantation,

HF was associated with a relatively high incidence of ventricular arrhythmias associated with QTc interval prolongation.

In addition, a recent retrospective study of 100 adult patients with advanced HF, treated with an axial-flow HeartMate LVAD suggested that

  • the rate of new-onset monomorphic ventricular tachycardia (MVT) was increased in LVAD treated patients compared to patients given only medical treatment,

The myocardium is exposed to severe and continuous biomechanical stress during each contraction-relaxation cycle. When fiber tension remains uncompensated or simply unbalanced,

it may represent a trigger for arrhythmogenesis caused by cytoskeletal stretching,

which ultimately leads to altered ion channel localization, and subsequent action potential and conduction alterations.

Cytoskeletal proteins not only provide the backbone of the cellular structure, but they also

maintain the shape and flexibility of the different sub-cellular compartments, including the

1.plasma membrane,

2.the double lipid layer, which defines the boundaries of the cell and where

ion channels are mainly localized.

The interaction between the sarcomere, which is the basic for the passive force during diastole and for the restoring force during systole.

Sarcomeric Proteins and Ion Channels

besides fiber stretch associated with mechanical and hemodynamic impairment, cytoskeletal alterations due to primary genetic defects or indirectly to alterations in response to cellular injury can potentially

1.affect ion channel anchoring, and trafficking, as well as

2.functional regulation by second messenger pathways,

3.causing an imbalance in cardiac ionic homeostasis that will trigger arrhythmogenesis.

Intense investigation of

the sarcomeric actin network,

the Z-line structure, and

chaperone molecules docking in the plasma membrane,

has shed new light on the molecular basis of

  • cytoskeletal interactions in regulating ion channels

Actin disruption using cytochalasin D, an agent that interferes with actin polymerization, increased Na+ channel activity in 90% of excised patches tested within 2 min, which indicated that

the integrity of the filamentous actin (F-actin) network was essential for the maintenance of normal Na+ channel function

These data were the first to support a role for the cytoskeleton in cardiac arrhythmias.

Molecular interactions between the cytoskeleton and ion channels

The figure illustrates the interactions between the ion channels on the sarcolemma, and the sarcomere in cardiac myocytes. Note that the Z-line is connected to the cardiac T-tubules. The diagram illustrates the complex protein-protein interactions that occur between structural components of the cytoskeleton and ion channels. The cytoskeleton is involved in regulating the metabolism of ion channels, modifying their expression, localization, and electrical properties.

sarcomere structure

sarcomere structure

It is important to be aware of the enormous variety of clinical presentations that derive from distinct variants in the same pool of genetic factors. Knowledge of these variants could facilitate tailoring the therapy of choice for each patient. In particular,

the recent findings of structural and functional links between

the cytoskeleton and ion channels

could expand the therapeutic interventions in

arrhythmia management in structurally abnormal myocardium, where aberrant binding

between cytoskeletal proteins can directly or indirectly alter ion channel function.

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Pharmacological Action of Steroid Hormones

Curator: Larry H. Bernstein, MD, FCAP

 

Hormone Receptors

Steroid hormone receptors are found on the plasma membrane, in the cytosol and also in the nucleus of target cells. They are generally intracellular receptors (typically cytoplasmic) and initiate signal transduction for steroid hormones which lead to changes in gene expression over a time period of hours to days. The best studied steroid hormone receptors are members of the nuclear receptor subfamily 3 (NR3) that include receptors for estrogen (group NR3A)[1] and 3-ketosteroids (group NR3C).[2] In addition to nuclear receptors, several G protein-coupled receptors and ion channels act as cell surface receptors for certain steroid hormones.

 

Steroid Hormone Receptors and their Response Elements

Steroid hormone receptors are proteins that have a binding site for a particular steroid molecule. Their response elements are DNA sequences that are bound by the complex of the steroid bound to its Steroid receptor.

The response element is part of the promoter of a gene. Binding by the receptor activates or represses, as the case may be, the gene controlled by that promoter.

It is through this mechanism that steroid hormones turn genes on (or off).

 

steroid hormone receptor

steroid hormone receptor

http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/S/Sigler.jpg

 

This image (courtesy of P. B. Sigler) shows a stereoscopic view of the glucocorticoid response element (DNA, the double helix shown in yellow at the left of each panel) with the glucocorticoid receptor (a protein homodimer, right portion of each panel) bound to it.

 

The DNA sequence of the glucocorticoid response element is

  • 5′ AGAACAnnnTGTTCT 3′
  • 3′ TCTTGTnnnACAAGA 5′

where n represents any nucleotide. (Note the inverted repeats.)

 

The glucocorticoid receptor, like all steroid hormone receptors, is a zinc-finger transcription factor; the zinc atoms are the four yellow spheres. Each is attached to four cysteines.

 

For a steroid hormone to regulate (turn on or off) gene transcription, its receptor must:

  1. bind to the hormone (cortisol in the case of the glucocorticoid receptor)
  2. bind to a second copy of itself to form a homodimer
  3. be in the nucleus, moving from the cytosol if necessary
  4. bind to its response element
  5. bind to other protein cofactors

Each of these functions depend upon a particular region of the protein (e.g., the zinc fingers for binding DNA). Mutations in any one region may upset the function of that region without necessarily interfering with other functions of the receptor.

Positive and Negative Response Elements

Some of the hundreds of glucocorticoid response elements in the human genome activate gene transcription when bound by the hormone/receptor complex. Others inhibit gene transcription when bound by the hormone/receptor complex.

Example: When the stress hormone cortisol — bound to its receptor — enters the nucleus of a liver cell, the complex binds to

the positive response elements of the many genes needed for gluconeogenesis — the conversion of protein and fat into glucose resulting in a rise in the level of blood sugar.

the negative response element of the insulin receptor gene thus diminishing the ability of the cells to remove glucose from the blood. (This hyperglycemic effect is enhanced by the binding of the cortisol/receptor complex to a negative response element in the beta cells of the pancreas thus reducing the production of insulin.)

Note that every type of cell in the body contains the same response elements in its genome. What determines if a given cell responds to the arrival of a hormone depends on the presence of the hormone’s receptor in the cell.

Visual Evidence of Hormone Binding

This autoradiograph (courtesy of Madhabananda Sar and Walter E. Stumpf) shows the endometrial cells from the uterus of a guinea pig 15 minutes after an injection of radioactive progesterone. The radioactivity has concentrated within the nuclei of the endometrial cells as shown by the dark grains superimposed on the images of the nuclei. The same effect is seen when radioactive estrogens are administered.

The cells of the endometrium are target cells for both progesterone and estrogens, preparing the uterus for possible pregnancy. [Link to discussion]

 

Endometrium

Endometrium

http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/E/Endometrium.jpg

Nontarget cells (e.g. liver cells or lymphocytes) show no accumulation of female sex hormones. Although their DNA contains the response elements, their cells do not have the protein receptors needed.

 The Nuclear Receptor Superfamily

 

Retinoids

Retinoids

http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/R/Retinoids.png

 The zinc-finger proteins that serve as receptors for glucocorticoids and progesterone are members of a large family of similar proteins that serve as receptors for a variety of small, hydrophobic molecules. These include:

  1. other steroid hormones like
  2. the mineralocorticoid aldosterone
  3. estrogens
  4. the thyroid hormone, T3
  5. calcitriol, the active form of vitamin D
  6. retinoids: vitamin A (retinol) and its relatives
    1. retinal
    2. retinoic acid (tretinoin — also available as the drug Retin-A®); and its isomer
  7. isotretinoin (sold as Accutane® for the treatment of acne).
  8. bile acids
  9. fatty acids.
The three dimensional crystal structure of holo-retinol binding protein (RBP–ROH)

The three dimensional crystal structure of holo-retinol binding protein (RBP–ROH)

 

 

 

 

 

vitamin_d_synthesis

 

Chemical structures of vitamin A (retinol)

Chemical structures of vitamin A (retinol)

 

vit D and receptor complex

vit D and receptor complex

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

These bind members of the superfamily called peroxisome-proliferator-activated receptors (PPARs). They got their name from their initial discovery as the receptors for

  • drugs that increase the number and size of peroxisomes in cells.

In every case, the receptors consist of at least

  • three functional modules or domains.

From N-terminal to C-terminal, these are:

  1. a domain needed
  2. the zinc-finger domain needed for DNA binding (to the response element)
  3. the domain responsible for binding the particular hormone as well as the second unit of the dimer.
  4. for the receptor to activate the promoters of the genes being controlled

The Steroid Hormone Receptors

Klinge, C, Rao, C, Glob. libr. women’s med.,

(ISSN: 1756-2228) 2008;
http://dx.doi.org:/10.3843/GLOWM.10281
Structure of The Steroid Hormone Receptor Protein

In order to understand how steroid hormone receptors regulate gene function, it is important to know the structure of the receptor proteins as well as the identity and cellular function of the genes that they regulate. Members of the steroid receptor superfamily share direct amino acid homology and a common structure (Fig. 1).

Fig. 1 Relative lengths of several members of the steroid/nuclear hormone receptor superfamily, shown schematically as linearized proteins with common structural and functional domains. Variability between members of the steroid hormone receptor family is due primarily to differences in the length and amino acid sequence of the amino (N)-terminal domain. Adapted from Wahli W, Martinez E. Superfamily of steroid nuclear receptors: Positive and negative regulators of gene expression. FASEB J 1991;5:2243-2249.

lengths of steroid hormone receptor superfamily

lengths of steroid hormone receptor superfamily

http://resources.ama.uk.com/glowm_www/graphics/figures/v5/0040/001f.gif

Molecular cloning of the complementary DNA (cDNA) for each of the major steroid receptors has greatly enhanced our understanding of the structure–function relationships for these molecules. The receptor proteins have five or six domains called A–F from N- to C-terminus, encoded by 8–9 exons.  The receptors contain three major functional domains that have been shown experimentally to operate as independent “cassettes”,13 unrestricted as to position within the molecule. The three major functional domains (Fig. 2) of the receptor are:

 

  1. A variable N-terminus (domains A and B) that confers immunogenicity and modulates transcription in a gene and cell-specific manner through its N-terminal Activation Function-1 (AF-1);
  2. A central DNA-binding domain (DBD, consisting of the C domain), comprised of two functionally distinct zinc fingers through which the receptor physically interacts directly with the DNA helix;
  3. The ligand-binding domain (LBD, domains E and in some receptors F) that contains Activation Function-2 (AF-2).

 

Fig. 2 Schematic representation of the common structural and functional domains of the steroid hormone receptors. The horizontal lines indicate the domains of the receptor. Adapted from Wahli W, Martinez E. Superfamily of steroid nuclear receptors: Positive and negative regulators of gene expression. FASEB J 1991;5:2243-2249.

 

http://resources.ama.uk.com/glowm_www/graphics/figures/v5/0040/002f.gif

 

The F domain is thought to play a role in distinguishing estrogen agonists from antagonists, perhaps through interaction with cell-specific factors. Domain-swapping experiments in which the DBD of estrogen receptor α (ERα) was switched with that of the glucocorticoid receptor (GR), yielded a chimeric receptor that bound to specific DNA sequences bound by GR, but up-regulated transcription of glucocorticoid-responsive target genes when treated with estrogen, thus demonstrating the specificity of the DNA-binding domain in target gene regulation.

The amino (N)-terminal domain is hypervariable (less than 15% homology among steroid receptors) in both size and amino acid sequence, ranging in length from 25 amino acids to 603 amino acids and constituting the major source of size differences between receptors. The AF-1 domain in this region is involved in activation of gene transcription, but does not depend on ligand binding. In rat GR, the AF-1 region is called tau 1 or enh2 and constitutes aa 108–317. Tau 1 is necessary for transcriptional activation and repression. Deletion of the C-terminal LBD of GR yields constitutive (hormone-independent) transcriptional activation, implying that the N-terminal regions harbor autonomous transcriptional activation functions.

 

Some steroid receptors exist as isoforms, encoded by the same gene, but differing in their N-terminus. The progesterone and androgen receptors (PR and AR) exist in two distinct forms, A and B, synthesized from the same mRNA by alternate splicing. The two PR receptor isoforms differ by 128 amino acids in the N-terminal region, yielding PR-A = 90 kDa and PR-B = 120 kDa, that have strikingly differing capacities to regulate transcription. In contrast, AR-A and AR-B isoforms show minimal differences in activation of a reporter gene in response to androgen agonists or antagonists in transiently transfected cells.

Receptors in this superfamily contain several key structural elements which enable them to bind to their respective ligands with high affinity and specificity, recognize and bind to discrete response elements within the DNA sequence of target genes with high affinity and specificity, and regulate gene transcription.

The central core or DNA-binding domain (DBD) is highly conserved and shows 60–95% homology among steroid receptors.1 The DBD varies in size from 66 to 70 amino acids, and is hydrophilic due to its high content of basic amino acids. The major function of this region is to bind to specific hormone response elements (HREs) of the target gene. DNA-binding is achieved through the tetrahedral coordination of zinc (Zn) by four cysteine residues in each of two extensions, that form two structurally distinct “Zn fingers” (Fig. 3). Zn fingers are common among gene regulatory proteins. Specificity of HRE binding is determined by the more highly conserved hydrophilic first Zn finger (C1), while the second Zn finger (C2) is involved in dimerization and stabilizing DNA binding by ionic interactions with the phosphate backbone of the DNA.18 The D box is involved in HRE half-site spacing recognition. The highly conserved DBD shared by AR, GR, mineralocorticoid receptor (MR), and PR enables them to bind to the same HRE, called the glucocorticoid response element (GRE). The more C-terminal part of the C2 Zn finger and amino acids in the hinge region are involved in receptor dimerization in coordination with amino acids in the hinge region and the LBD.

 

Fig. 3 Schematic diagram of type II zinc finger proteins characteristic of the DNA-binding domain structure of members of the steroid hormone receptor superfamily. Zinc fingers are common features of many transcription factors, allowing proteins to bind to DNA. Each circle represents one amino acid. The CI zinc finger interacts specifically with five base pairs of DNA and determines the DNA sequence recognized by the particular steroid receptor. The three shaded amino acids indicated by the arrows in the knuckle of the CI zinc finger are in the “P box” that allows HRE sequence discrimination between the GR and ERα. The vertically striped aa within the knuckle of the CII zinc finger constitutes the “D box” that is important for dimerization and contacts with the DNA phosphate backbone. Adapted from Tsai M-J, O’Malley BW. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu Rev Biochem 1994;63:451-483; Gronemeyer H. Transcription activation by estrogen and progesterone receptors. Annu Rev Genet 1991;25:89-123.

type II zinc finger proteins

type II zinc finger proteins

http://resources.ama.uk.com/glowm_www/graphics/figures/v5/0040/003f.gif

The hinge region or D domain is a 40–50 amino acid sequence separating the DNA-binding and ligand-binding domains that contains sequences for receptor dimerization and ligand-dependent and independent nuclear localization sequences (NLSs). The hinge region interacts with nuclear corepressor proteins, and with L7/SPA, a 27 kDa protein that increases the partial agonist activity of certain antagonist-liganded steroid hormone receptors, i.e., tamoxifen-liganded ERα, RU486-occupied PR, or RU486-occupied GR. ….

The carboxy (C)-terminal or ligand-binding domain (LBD) is poorly conserved, ranging in size from 218 to 264 amino acids and is hydrophobic. This region contains the ligand-binding site and dictates hormone binding specificity.

Two human GR isoforms, GRα and GRβ, derived from the same gene by differential splicing at the C-terminus, have been reported. While GRα and GRβ share the first eight exons, they differ in their last two exons, i.e., exons 9α or 9β, spliced into the respective mRNA.40 GRβ was reported to localize in the cell nucleus in the absence of ligand and to block hGRα activity. …

Sequences within the LBD form the binding site for hsp90 that blocks the DBD in the cytosolic, nonliganded GR.40 The CII and CIII regions (Fig. 2) show homology among members of the steroid/nuclear receptor superfamily and are important in forming the ligand binding pocket. …

 

The Bifunctional Role of Steroid Hormones: Implications for Therapy in Prostate Cancer

Paul Mathew, MD
Review Article | May 15, 2014 | Oncology Journal, Genitourinary Cancers, Prostate Cancer

In a biomarker-driven study reported in 1941, Drs. Huggins and Hodges of the University of Chicago demonstrated reduction in elevated levels of serum acid phosphatase in five men with metastatic prostate cancer treated with estrogens and orchiectomy, whereas three men who received testosterone injections after orchiectomy exhibited increased serum levels of the enzyme. Hitherto, serum elevations of acid phosphatase had been associated strictly with prostate cancer, and Huggins and Hodges thus concluded that androgens activated prostate cancer. Nevertheless, in the years that followed, several investigators experimented with testosterone injections in prostate cancer. Pearson[3] of the Sloan-Kettering Institute reviewed the inconsistent biochemical and clinical responses to testosterone injections associated with these studies and puzzled over two case studies of his own, one of a hormone-naive patient, another of a castration-resistant patient, both of whom had responded to testosterone injection: “These observations invite the development of new concepts to explain the response of these prostatic cancers to alterations in the endocrine environment.”

Table 1: Sex Steroids as Tumor Suppressors (not shown)

ABSTRACT: Ablation of the androgen-signaling axis is currently a dominant theme in developmental therapeutics in prostate cancer. Highly potent inhibitors of androgen biosynthesis and androgen receptor (AR) function have formally improved survival in castration-resistant metastatic disease. Resistance to androgen-ablative strategies arises through diverse mechanisms. Strategies to preserve and extend the success of hormonal therapy while mitigating the emergence of resistance have long been of interest. In preclinical models, intermittent hormonal ablative strategies delay the emergence of resistant stem-cell–driven phenotypes, but clinical studies in hormone-naive disease have not observed more than noninferiority over continual androgen ablation. In castration-resistant disease, response and improvement in subjective quality of life with therapeutic testosterone has been observed, but so too has symptomatic and life-threatening disease acceleration. The multifunctional and paradoxical role of steroid hormones in regulating proliferation and differentiation, as well as cell death, requires deeper understanding. The lack of molecular biomarkers that predict the outcome of hormone supplementation in a particular clinical context remains an obstacle to individualized therapy. Biphasic patterns of response to hormones are identifiable in vitro, and endocrine-regulated neoplasms that proliferate after prolonged periods of hormone deprivation appear preferentially sex steroid–suppressible. This review examines the relevance of a translational framework for studying therapeutic androgens in prostate cancer.

 

Protection and Damage from Acute and Chronic Stress: Allostasis and Allostatic Overload and Relevance to the Pathophysiology of Psychiatric Disorders

Bruce S. Mcewen*

Annals of the New York Academy of Sciences 12 JAN 2006;
1032 (Biobehavioral Stress Response: Protective and Damaging Effects): Pp1–328

http://dx.doi.org:/10.1196/annals.1314.001

                                             

Keywords:

stress;psychiatric disorders;depression;allostasis;allostatic overload;homeostasis

Abstract: Stress promotes adaptation, but prolonged stress leads over time to wear-and-tear on the body (allostatic load). Neural changes mirror the pattern seen in other body systems, that is, short-term adaptation vs. long-term damage. Allostatic load leads to impaired immunity, atherosclerosis, obesity, bone demineralization, and atrophy of nerve cells in the brain. Many of these processes are seen in major depressive illness and may be expressed also in other chronic anxiety disorders. The brain controls the physiological and behavioral coping responses to daily events and stressors. The hippocampal formation expresses high levels of adrenal steroid receptors and is a malleable brain structure that is important for certain types of learning and memory. It is also vulnerable to the effects of stress and trauma. The amygdala mediates physiological and behavioral responses associated with fear. The prefrontal cortex plays an important role in working memory and executive function and is also involved in extinction of learning. All three regions are targets of stress hormones. In animal models, neurons in the hippocampus and prefrontal cortex respond to repeated stress by showing atrophy, whereas neurons in amygdala show a growth response. Yet, these are not necessarily “damaged” and may be treatable with the right medications.

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Antimalarial flow synthesis closer to commercialisation.

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Metabolomics Summary and Perspective

Metabolomics Summary and Perspective

Author and Curator: Larry H Bernstein, MD, FCAP 

 

This is the final article in a robust series on metabolism, metabolomics, and  the “-OMICS-“ biological synthesis that is creating a more holistic and interoperable view of natural sciences, including the biological disciplines, climate science, physics, chemistry, toxicology, pharmacology, and pathophysiology with as yet unforeseen consequences.

There have been impressive advances already in the research into developmental biology, plant sciences, microbiology, mycology, and human diseases, most notably, cancer, metabolic , and infectious, as well as neurodegenerative diseases.

Acknowledgements:

I write this article in honor of my first mentor, Harry Maisel, Professor and Emeritus Chairman of Anatomy, Wayne State University, Detroit, MI and to my stimulating mentors, students, fellows, and associates over many years:

Masahiro Chiga, MD, PhD, Averill A Liebow, MD, Nathan O Kaplan, PhD, Johannes Everse, PhD, Norio Shioura, PhD, Abraham Braude, MD, Percy J Russell, PhD, Debby Peters, Walter D Foster, PhD, Herschel Sidransky, MD, Sherman Bloom, MD, Matthew Grisham, PhD, Christos Tsokos, PhD,  IJ Good, PhD, Distinguished Professor, Raool Banagale, MD, Gustavo Reynoso, MD,Gustave Davis, MD, Marguerite M Pinto, MD, Walter Pleban, MD, Marion Feietelson-Winkler, RD, PhD,  John Adan,MD, Joseph Babb, MD, Stuart Zarich, MD,  Inder Mayall, MD, A Qamar, MD, Yves Ingenbleek, MD, PhD, Emeritus Professor, Bette Seamonds, PhD, Larry Kaplan, PhD, Pauline Y Lau, PhD, Gil David, PhD, Ronald Coifman, PhD, Emeritus Professor, Linda Brugler, RD, MBA, James Rucinski, MD, Gitta Pancer, Ester Engelman, Farhana Hoque, Mohammed Alam, Michael Zions, William Fleischman, MD, Salman Haq, MD, Jerard Kneifati-Hayek, Madeleine Schleffer, John F Heitner, MD, Arun Devakonda,MD, Liziamma George,MD, Suhail Raoof, MD, Charles Oribabor,MD, Anthony Tortolani, MD, Prof and Chairman, JRDS Rosalino, PhD, Aviva Lev Ari, PhD, RN, Rosser Rudolph, MD, PhD, Eugene Rypka, PhD, Jay Magidson, PhD, Izaak Mayzlin, PhD, Maurice Bernstein, PhD, Richard Bing, Eli Kaplan, PhD, Maurice Bernstein, PhD.

This article has EIGHT parts, as follows:

Part 1

Metabolomics Continues Auspicious Climb

Part 2

Biologists Find ‘Missing Link’ in the Production of Protein Factories in Cells

Part 3

Neuroscience

Part 4

Cancer Research

Part 5

Metabolic Syndrome

Part 6

Biomarkers

Part 7

Epigenetics and Drug Metabolism

Part 8

Pictorial

genome cartoon

genome cartoon

 iron metabolism

iron metabolism

personalized reference range within population range

personalized reference range within population range

Part 1.  MetabolomicsSurge

metagraph  _OMICS

metagraph _OMICS

Metabolomics Continues Auspicious Climb

Jeffery Herman, Ph.D.
GEN May 1, 2012 (Vol. 32, No. 9)

Aberrant biochemical and metabolite signaling plays an important role in

  • the development and progression of diseased tissue.

This concept has been studied by the science community for decades. However, with relatively

  1. recent advances in analytical technology and bioinformatics as well as
  2. the development of the Human Metabolome Database (HMDB),

metabolomics has become an invaluable field of research.

At the “International Conference and Exhibition on Metabolomics & Systems Biology” held recently in San Francisco, researchers and industry leaders discussed how

  • the underlying cellular biochemical/metabolite fingerprint in response to
  1. a specific disease state,
  2. toxin exposure, or
  3. pharmaceutical compound
  • is useful in clinical diagnosis and biomarker discovery and
  • in understanding disease development and progression.

Developed by BASF, MetaMap® Tox is

  • a database that helps identify in vivo systemic effects of a tested compound, including
  1. targeted organs,
  2. mechanism of action, and
  3. adverse events.

Based on 28-day systemic rat toxicity studies, MetaMap Tox is composed of

  • differential plasma metabolite profiles of rats
  • after exposure to a large variety of chemical toxins and pharmaceutical compounds.

“Using the reference data,

  • we have developed more than 110 patterns of metabolite changes, which are
  • specific and predictive for certain toxicological modes of action,”

said Hennicke Kamp, Ph.D., group leader, department of experimental toxicology and ecology at BASF.

With MetaMap Tox, a potential drug candidate

  • can be compared to a similar reference compound
  • using statistical correlation algorithms,
  • which allow for the creation of a toxicity and mechanism of action profile.

“MetaMap Tox, in the context of early pre-clinical safety enablement in pharmaceutical development,” continued Dr. Kamp,

  • has been independently validated “
  • by an industry consortium (Drug Safety Executive Council) of 12 leading biopharmaceutical companies.”

Dr. Kamp added that this technology may prove invaluable

  • allowing for quick and accurate decisions and
  • for high-throughput drug candidate screening, in evaluation
  1. on the safety and efficacy of compounds
  2. during early and preclinical toxicological studies,
  3. by comparing a lead compound to a variety of molecular derivatives, and
  • the rapid identification of the most optimal molecular structure
  • with the best efficacy and safety profiles might be streamlined.
Dynamic Construct of the –Omics

Dynamic Construct of the –Omics

Targeted Tandem Mass Spectrometry

Biocrates Life Sciences focuses on targeted metabolomics, an important approach for

  • the accurate quantification of known metabolites within a biological sample.

Originally used for the clinical screening of inherent metabolic disorders from dried blood-spots of newborn children, Biocrates has developed

  • a tandem mass spectrometry (MS/MS) platform, which allows for
  1. the identification,
  2. quantification, and
  3. mapping of more than 800 metabolites to specific cellular pathways.

It is based on flow injection analysis and high-performance liquid chromatography MS/MS.

Clarification of Pathway-Specific Inhibition by Fourier Transform Ion Cyclotron Resonance.Mass Spectrometry-Based Metabolic Phenotyping Studies F5.large

common drug targets

common drug targets

The MetaDisIDQ® Kit is a

  • “multiparamatic” diagnostic assay designed for the “comprehensive assessment of a person’s metabolic state” and
  • the early determination of pathophysiological events with regards to a specific disease.

MetaDisIDQ is designed to quantify

  • a diverse range of 181 metabolites involved in major metabolic pathways
  • from a small amount of human serum (10 µL) using isotopically labeled internal standards,

This kit has been demonstrated to detect changes in metabolites that are commonly associated with the development of

  • metabolic syndrome, type 2 diabetes, and diabetic nephropathy,

Dr. Dallman reports that data generated with the MetaDisIDQ kit correlates strongly with

  • routine chemical analyses of common metabolites including glucose and creatinine

Biocrates has also developed the MS/MS-based AbsoluteIDQ® kits, which are

  • an “easy-to-use” biomarker analysis tool for laboratory research.

The kit functions on MS machines from a variety of vendors, and allows for the quantification of 150-180 metabolites.

The SteroIDQ® kit is a high-throughput standardized MS/MS diagnostic assay,

  • validated in human serum, for the rapid and accurate clinical determination of 16 known steroids.

Initially focusing on the analysis of steroid ranges for use in hormone replacement therapy, the SteroIDQ Kit is expected to have a wide clinical application.

Hormone-Resistant Breast Cancer

Scientists at Georgetown University have shown that

  • breast cancer cells can functionally coordinate cell-survival and cell-proliferation mechanisms,
  • while maintaining a certain degree of cellular metabolism.

To grow, cells need energy, and energy is a product of cellular metabolism. For nearly a century, it was thought that

  1. the uncoupling of glycolysis from the mitochondria,
  2. leading to the inefficient but rapid metabolism of glucose and
  3. the formation of lactic acid (the Warburg effect), was

the major and only metabolism driving force for unchecked proliferation and tumorigenesis of cancer cells.

Other aspects of metabolism were often overlooked.

“.. we understand now that

  • cellular metabolism is a lot more than just metabolizing glucose,”

said Robert Clarke, Ph.D., professor of oncology and physiology and biophysics at Georgetown University. Dr. Clarke, in collaboration with the Waters Center for Innovation at Georgetown University (led by Albert J. Fornace, Jr., M.D.), obtained

  • the metabolomic profile of hormone-sensitive and -resistant breast cancer cells through the use of UPLC-MS.

They demonstrated that breast cancer cells, through a rather complex and not yet completely understood process,

  1. can functionally coordinate cell-survival and cell-proliferation mechanisms,
  2. while maintaining a certain degree of cellular metabolism.

This is at least partly accomplished through the upregulation of important pro-survival mechanisms; including

  • the unfolded protein response;
  • a regulator of endoplasmic reticulum stress and
  • initiator of autophagy.

Normally, during a stressful situation, a cell may

  • enter a state of quiescence and undergo autophagy,
  • a process by which a cell can recycle organelles
  • in order to maintain enough energy to survive during a stressful situation or,

if the stress is too great,

  • undergo apoptosis.

By integrating cell-survival mechanisms and cellular metabolism

  • advanced ER+ hormone-resistant breast cancer cells
  • can maintain a low level of autophagy
  • to adapt and resist hormone/chemotherapy treatment.

This adaptation allows cells

  • to reallocate important metabolites recovered from organelle degradation and
  • provide enough energy to also promote proliferation.

With further research, we can gain a better understanding of the underlying causes of hormone-resistant breast cancer, with

  • the overall goal of developing effective diagnostic, prognostic, and therapeutic tools.

NMR

Over the last two decades, NMR has established itself as a major tool for metabolomics analysis. It is especially adept at testing biological fluids. [Bruker BioSpin]

Historically, nuclear magnetic resonance spectroscopy (NMR) has been used for structural elucidation of pure molecular compounds. However, in the last two decades, NMR has established itself as a major tool for metabolomics analysis. Since

  • the integral of an NMR signal is directly proportional to
  • the molar concentration throughout the dynamic range of a sample,

“the simultaneous quantification of compounds is possible

  • without the need for specific reference standards or calibration curves,” according to Lea Heintz of Bruker BioSpin.

NMR is adept at testing biological fluids because of

  1.  high reproducibility,
  2. standardized protocols,
  3. low sample manipulation, and
  4. the production of a large subset of data,

Bruker BioSpin is presently involved in a project for the screening of inborn errors of metabolism in newborn children from Turkey, based on their urine NMR profiles. More than 20 clinics are participating to the project that is coordinated by INFAI, a specialist in the transfer of advanced analytical technology into medical diagnostics. The construction of statistical models are being developed

  • for the detection of deviations from normality, as well as
  • automatic quantification methods for indicative metabolites

Bruker BioSpin recently installed high-resolution magic angle spinning NMR (HRMAS-NMR) systems that can rapidly analyze tissue biopsies. The main objective for HRMAS-NMR is to establish a rapid and effective clinical method to assess tumor grade and other important aspects of cancer during surgery.

Combined NMR and Mass Spec

There is increasing interest in combining NMR and MS, two of the main analytical assays in metabolomic research, as a means

  • to improve data sensitivity and to
  • fully elucidate the complex metabolome within a given biological sample.
  •  to realize a potential for cancer biomarker discovery in the realms of diagnosis, prognosis, and treatment.

.

Using combined NMR and MS to measure the levels of nearly 250 separate metabolites in the patient’s blood, Dr. Weljie and other researchers at the University of Calgary were able to rapidly determine the malignancy of a  pancreatic lesion (in 10–15% of the cases, it is difficult to discern between benign and malignant), while avoiding unnecessary surgery in patients with benign lesions.

When performing NMR and MS on a single biological fluid, ultimately “we are,” noted Dr. Weljie,

  1. “splitting up information content, processing, and introducing a lot of background noise and error and
  2. then trying to reintegrate the data…
    It’s like taking a complex item, with multiple pieces, out of an IKEA box and trying to repackage it perfectly into another box.”

By improving the workflow between the initial splitting of the sample, they improved endpoint data integration, proving that

  • a streamlined approach to combined NMR/MS can be achieved,
  • leading to a very strong, robust and precise metabolomics toolset.

Metabolomics Research Picks Up Speed

Field Advances in Quest to Improve Disease Diagnosis and Predict Drug Response

John Morrow Jr., Ph.D.
GEN May 1, 2011 (Vol. 31, No. 9)

As an important discipline within systems biology, metabolomics is being explored by a number of laboratories for

  • its potential in pharmaceutical development.

Studying metabolites can offer insights into the relationships between genotype and phenotype, as well as between genotype and environment. In addition, there is plenty to work with—there are estimated to be some 2,900 detectable metabolites in the human body, of which

  1. 309 have been identified in cerebrospinal fluid,
  2. 1,122 in serum,
  3. 458 in urine, and
  4. roughly 300 in other compartments.

Guowang Xu, Ph.D., a researcher at the Dalian Institute of Chemical Physics.  is investigating the causes of death in China,

  • and how they have been changing over the years as the country has become a more industrialized nation.
  •  the increase in the incidence of metabolic disorders such as diabetes has grown to affect 9.7% of the Chinese population.

Dr. Xu,  collaborating with Rainer Lehman, Ph.D., of the University of Tübingen, Germany, compared urinary metabolites in samples from healthy individuals with samples taken from prediabetic, insulin-resistant subjects. Using mass spectrometry coupled with electrospray ionization in the positive mode, they observed striking dissimilarities in levels of various metabolites in the two groups.

“When we performed a comprehensive two-dimensional gas chromatography, time-of-flight mass spectrometry analysis of our samples, we observed several metabolites, including

  • 2-hydroxybutyric acid in plasma,
  •  as potential diabetes biomarkers,” Dr. Xu explains.

In other, unrelated studies, Dr. Xu and the German researchers used a metabolomics approach to investigate the changes in plasma metabolite profiles immediately after exercise and following a 3-hour and 24-hour period of recovery. They found that

  • medium-chain acylcarnitines were the most distinctive exercise biomarkers, and
  • they are released as intermediates of partial beta oxidation in human myotubes and mouse muscle tissue.

Dr. Xu says. “The traditional approach of assessment based on a singular biomarker is being superseded by the introduction of multiple marker profiles.”

Typical of the studies under way by Dr. Kaddurah-Daouk and her colleaguesat Duke University

  • is a recently published investigation highlighting the role of an SNP variant in
  • the glycine dehydrogenase gene on individual response to antidepressants.
  •  patients who do not respond to the selective serotonin uptake inhibitors citalopram and escitalopram
  • carried a particular single nucleotide polymorphism in the GD gene.

“These results allow us to pinpoint a possible

  • role for glycine in selective serotonin reuptake inhibitor response and
  • illustrate the use of pharmacometabolomics to inform pharmacogenomics.

These discoveries give us the tools for prognostics and diagnostics so that

  • we can predict what conditions will respond to treatment.

“This approach to defining health or disease in terms of metabolic states opens a whole new paradigm.

By screening hundreds of thousands of molecules, we can understand

  • the relationship between human genetic variability and the metabolome.”

Dr. Kaddurah-Daouk talks about statins as a current

  • model of metabolomics investigations.

It is now known that the statins  have widespread effects, altering a range of metabolites. To sort out these changes and develop recommendations for which individuals should be receiving statins will require substantial investments of energy and resources into defining the complex web of biochemical changes that these drugs initiate.
Furthermore, Dr. Kaddurah-Daouk asserts that,

  • “genetics only encodes part of the phenotypic response.

One needs to take into account the

  • net environment contribution in order to determine
  • how both factors guide the changes in our metabolic state that determine the phenotype.”

Interactive Metabolomics

Researchers at the University of Nottingham use diffusion-edited nuclear magnetic resonance spectroscopy to assess the effects of a biological matrix on metabolites. Diffusion-edited NMR experiments provide a way to

  • separate the different compounds in a mixture
  • based on the differing translational diffusion coefficients (which reflect the size and shape of the molecule).

The measurements are carried out by observing

  • the attenuation of the NMR signals during a pulsed field gradient experiment.

Clare Daykin, Ph.D., is a lecturer at the University of Nottingham, U.K. Her field of investigation encompasses “interactive metabolomics,”which she defines as

“the study of the interactions between low molecular weight biochemicals and macromolecules in biological samples ..

  • without preselection of the components of interest.

“Blood plasma is a heterogeneous mixture of molecules that

  1. undergo a variety of interactions including metal complexation,
  2. chemical exchange processes,
  3. micellar compartmentation,
  4. enzyme-mediated biotransformations, and
  5. small molecule–macromolecular binding.”

Many low molecular weight compounds can exist

  • freely in solution,
  • bound to proteins, or
  • within organized aggregates such as lipoprotein complexes.

Therefore, quantitative comparison of plasma composition from

  • diseased individuals compared to matched controls provides an incomplete insight to plasma metabolism.

“It is not simply the concentrations of metabolites that must be investigated,

  • but their interactions with the proteins and lipoproteins within this complex web.

Rather than targeting specific metabolites of interest, Dr. Daykin’s metabolite–protein binding studies aim to study

  • the interactions of all detectable metabolites within the macromolecular sample.

Such activities can be studied through the use of diffusion-edited nuclear magnetic resonance (NMR) spectroscopy, in which one can assess

  • the effects of the biological matrix on the metabolites.

“This can lead to a more relevant and exact interpretation

  • for systems where metabolite–macromolecule interactions occur.”

Diffusion-edited NMR experiments provide a way to separate the different compounds in a mixture based on

  • the differing translational diffusion coefficients (which reflect the size and shape of the molecule).

The measurements are carried out by observing

  • the attenuation of the NMR signals during a pulsed field gradient experiment.

Pushing the Limits

It is widely recognized that many drug candidates fail during development due to ancillary toxicity. Uwe Sauer, Ph.D., professor, and Nicola Zamboni, Ph.D., researcher, both at the Eidgenössische Technische Hochschule, Zürich (ETH Zürich), are applying

  • high-throughput intracellular metabolomics to understand
  • the basis of these unfortunate events and
  • head them off early in the course of drug discovery.

“Since metabolism is at the core of drug toxicity, we developed a platform for

  • measurement of 50–100 targeted metabolites by
  • a high-throughput system consisting of flow injection
  • coupled to tandem mass spectrometry.”

Using this approach, Dr. Sauer’s team focused on

  • the central metabolism of the yeast Saccharomyces cerevisiae, reasoning that
  • this core network would be most susceptible to potential drug toxicity.

Screening approximately 41 drugs that were administered at seven concentrations over three orders of magnitude, they observed changes in metabolome patterns at much lower drug concentrations without attendant physiological toxicity.

The group carried out statistical modeling of about

  • 60 metabolite profiles for each drug they evaluated.

This data allowed the construction of a “profile effect map” in which

  • the influence of each drug on metabolite levels can be followed, including off-target effects, which
  • provide an indirect measure of the possible side effects of the various drugs.

Dr. Sauer says.“We have found that this approach is

  • at least 100 times as fast as other omics screening platforms,”

“Some drugs, including many anticancer agents,

  • disrupt metabolism long before affecting growth.”
killing cancer cells

killing cancer cells

Furthermore, they used the principle of 13C-based flux analysis, in which

  • metabolites labeled with 13C are used to follow the utilization of metabolic pathways in the cell.

These 13C-determined intracellular responses of metabolic fluxes to drug treatment demonstrate

  • the functional performance of the network to be rather robust,
conformational changes leading to substrate efflux.

conformational changes leading to substrate efflux.

leading Dr. Sauer to the conclusion that

  • the phenotypic vigor he observes to drug challenges
  • is achieved by a flexible make up of the metabolome.

Dr. Sauer is confident that it will be possible to expand the scope of these investigations to hundreds of thousands of samples per study. This will allow answers to the questions of

  • how cells establish a stable functioning network in the face of inevitable concentration fluctuations.

Is Now the Hour?

There is great enthusiasm and agitation within the biotech community for

  • metabolomics approaches as a means of reversing the dismal record of drug discovery

that has accumulated in the last decade.

While the concept clearly makes sense and is being widely applied today, there are many reasons why drugs fail in development, and metabolomics will not be a panacea for resolving all of these questions. It is too early at this point to recognize a trend or a track record, and it will take some time to see how this approach can aid in drug discovery and shorten the timeline for the introduction of new pharmaceutical agents.

Degree of binding correlated with function

Degree of binding correlated with function

Diagram_of_a_two-photon_excitation_microscope_

Diagram_of_a_two-photon_excitation_microscope_

Part 2.  Biologists Find ‘Missing Link’ in the Production of Protein Factories in Cells

Biologists at UC San Diego have found

  • the “missing link” in the chemical system that
  • enables animal cells to produce ribosomes

—the thousands of protein “factories” contained within each cell that

  • manufacture all of the proteins needed to build tissue and sustain life.
‘Missing Link’

‘Missing Link’

Their discovery, detailed in the June 23 issue of the journal Genes & Development, will not only force

  • a revision of basic textbooks on molecular biology, but also
  • provide scientists with a better understanding of
  • how to limit uncontrolled cell growth, such as cancer,
  • that might be regulated by controlling the output of ribosomes.

Ribosomes are responsible for the production of the wide variety of proteins that include

  1. enzymes;
  2. structural molecules, such as hair,
  3. skin and bones;
  4. hormones like insulin; and
  5. components of our immune system such as antibodies.

Regarded as life’s most important molecular machine, ribosomes have been intensively studied by scientists (the 2009 Nobel Prize in Chemistry, for example, was awarded for studies of its structure and function). But until now researchers had not uncovered all of the details of how the proteins that are used to construct ribosomes are themselves produced.

In multicellular animals such as humans,

  • ribosomes are made up of about 80 different proteins
    (humans have 79 while some other animals have a slightly different number) as well as
  • four different kinds of RNA molecules.

In 1969, scientists discovered that

  • the synthesis of the ribosomal RNAs is carried out by specialized systems using two key enzymes:
  • RNA polymerase I and RNA polymerase III.

But until now, scientists were unsure if a complementary system was also responsible for

  • the production of the 80 proteins that make up the ribosome.

That’s essentially what the UC San Diego researchers headed by Jim Kadonaga, a professor of biology, set out to examine. What they found was the missing link—the specialized

  • system that allows ribosomal proteins themselves to be synthesized by the cell.

Kadonaga says that he and coworkers found that ribosomal proteins are synthesized via

  • a novel regulatory system with the enzyme RNA polymerase II and
  • a factor termed TRF2,”

“For the production of most proteins,

  1. RNA polymerase II functions with
  2. a factor termed TBP,
  3. but for the synthesis of ribosomal proteins, it uses TRF2.”
  •  this specialized TRF2-based system for ribosome biogenesis
  • provides a new avenue for the study of ribosomes and
  • its control of cell growth, and

“it should lead to a better understanding and potential treatment of diseases such as cancer.”

Coordination of the transcriptome and metabolome

Coordination of the transcriptome and metabolome

the potential advantages conferred by distal-site protein synthesis

the potential advantages conferred by distal-site protein synthesis

Other authors of the paper were UC San Diego biologists Yuan-Liang Wang, Sascha Duttke and George Kassavetis, and Kai Chen, Jeff Johnston, and Julia Zeitlinger of the Stowers Institute for Medical Research in Kansas City, Missouri. Their research was supported by two grants from the National Institutes of Health (1DP2OD004561-01 and R01 GM041249).

Turning Off a Powerful Cancer Protein

Scientists have discovered how to shut down a master regulatory transcription factor that is

  • key to the survival of a majority of aggressive lymphomas,
  • which arise from the B cells of the immune system.

The protein, Bcl6, has long been considered too complex to target with a drug since it is also crucial

  • to the healthy functioning of many immune cells in the body, not just B cells gone bad.

The researchers at Weill Cornell Medical College report that it is possible

  • to shut down Bcl6 in diffuse large B-cell lymphoma (DLBCL)
  • while not affecting its vital function in T cells and macrophages
  • that are needed to support a healthy immune system.

If Bcl6 is completely inhibited, patients might suffer from systemic inflammation and atherosclerosis. The team conducted this new study to help clarify possible risks, as well as to understand

  • how Bcl6 controls the various aspects of the immune system.

The findings in this study were inspired from

  • preclinical testing of two Bcl6-targeting agents that Dr. Melnick and his Weill Cornell colleagues have developed
  • to treat DLBCLs.

These experimental drugs are

  • RI-BPI, a peptide mimic, and
  • the small molecule agent 79-6.

“This means the drugs we have developed against Bcl6 are more likely to be

  • significantly less toxic and safer for patients with this cancer than we realized,”

says Ari Melnick, M.D., professor of hematology/oncology and a hematologist-oncologist at NewYork-Presbyterian Hospital/Weill Cornell Medical Center.

Dr. Melnick says the discovery that

  • a master regulatory transcription factor can be targeted
  • offers implications beyond just treating DLBCL.

Recent studies from Dr. Melnick and others have revealed that

  • Bcl6 plays a key role in the most aggressive forms of acute leukemia, as well as certain solid tumors.

Bcl6 can control the type of immune cell that develops in the bone marrow—playing many roles

  • in the development of B cells, T cells, macrophages, and other cells—including a primary and essential role in
  • enabling B-cells to generate specific antibodies against pathogens.

According to Dr. Melnick, “When cells lose control of Bcl6,

  • lymphomas develop in the immune system.

Lymphomas are ‘addicted’ to Bcl6, and therefore

  • Bcl6 inhibitors powerfully and quickly destroy lymphoma cells,” .

The big surprise in the current study is that rather than functioning as a single molecular machine,

  • Bcl6 functions like a Swiss Army knife,
  • using different tools to control different cell types.

This multifunction paradigm could represent a general model for the functioning of other master regulatory transcription factors.

“In this analogy, the Swiss Army knife, or transcription factor, keeps most of its tools folded,

  • opening only the one it needs in any given cell type,”

He makes the following analogy:

  • “For B cells, it might open and use the knife tool;
  • for T cells, the cork screw;
  • for macrophages, the scissors.”

“this means that you only need to prevent the master regulator from using certain tools to treat cancer. You don’t need to eliminate the whole knife,” . “In fact, we show that taking out the whole knife is harmful since

  • the transcription factor has many other vital functions that other cells in the body need.”

Prior to these study results, it was not known that a master regulator could separate its functions so precisely. Researchers hope this will be a major benefit to the treatment of DLBCL and perhaps other disorders that are influenced by Bcl6 and other master regulatory transcription factors.

The study is published in the journal Nature Immunology, in a paper titled “Lineage-specific functions of Bcl-6 in immunity and inflammation are mediated by distinct biochemical mechanisms”.

Part 3. Neuroscience

Vesicles influence function of nerve cells 
Oct, 06 2014        source: http://feeds.sciencedaily.com

Neurons (blue) which have absorbed exosomes (green) have increased levels of the enzyme catalase (red), which helps protect them against peroxides.

Neurons (blue) which have absorbed exosomes (green) have increased levels of the enzyme catalase (red), which helps protect them against peroxides.

Neurons (blue) which have absorbed exosomes (green) have increased levels of the enzyme catalase (red), which helps protect them against peroxides.

Tiny vesicles containing protective substances

  • which they transmit to nerve cells apparently
  • play an important role in the functioning of neurons.

As cell biologists at Johannes Gutenberg University Mainz (JGU) have discovered,

  • nerve cells can enlist the aid of mini-vesicles of neighboring glial cells
  • to defend themselves against stress and other potentially detrimental factors.

These vesicles, called exosomes, appear to stimulate the neurons on various levels:

  • they influence electrical stimulus conduction,
  • biochemical signal transfer, and
  • gene regulation.

Exosomes are thus multifunctional signal emitters

  • that can have a significant effect in the brain.
Exosome

Exosome

The researchers in Mainz already observed in a previous study that

  • oligodendrocytes release exosomes on exposure to neuronal stimuli.
  • these are absorbed by the neurons and improve neuronal stress tolerance.

Oligodendrocytes, a type of glial cell, form an

  • insulating myelin sheath around the axons of neurons.

The exosomes transport protective proteins such as

  • heat shock proteins,
  • glycolytic enzymes, and
  • enzymes that reduce oxidative stress from one cell type to another,
  • but also transmit genetic information in the form of ribonucleic acids.

“As we have now discovered in cell cultures, exosomes seem to have a whole range of functions,” explained Dr. Eva-Maria Krmer-Albers. By means of their transmission activity, the small bubbles that are the vesicles

  • not only promote electrical activity in the nerve cells, but also
  • influence them on the biochemical and gene regulatory level.

“The extent of activities of the exosomes is impressive,” added Krmer-Albers. The researchers hope that the understanding of these processes will contribute to the development of new strategies for the treatment of neuronal diseases. Their next aim is to uncover how vesicles actually function in the brains of living organisms.

http://labroots.com/user/news/article/id/217438/title/vesicles-influence-function-of-nerve-cells

The above story is based on materials provided by Universitt Mainz.

Universitt Mainz. “Vesicles influence function of nerve cells.” ScienceDaily. ScienceDaily, 6 October 2014. www.sciencedaily.com/releases/2014/10/141006174214.htm

Neuroscientists use snail research to help explain “chemo brain”

10/08/2014
It is estimated that as many as half of patients taking cancer drugs experience a decrease in mental sharpness. While there have been many theories, what causes “chemo brain” has eluded scientists.

In an effort to solve this mystery, neuroscientists at The University of Texas Health Science Center at Houston (UTHealth) conducted an experiment in an animal memory model and their results point to a possible explanation. Findings appeared in The Journal of Neuroscience.

In the study involving a sea snail that shares many of the same memory mechanisms as humans and a drug used to treat a variety of cancers, the scientists identified

  • memory mechanisms blocked by the drug.

Then, they were able to counteract or

  • unblock the mechanisms by administering another agent.

“Our research has implications in the care of people given to cognitive deficits following drug treatment for cancer,” said John H. “Jack” Byrne, Ph.D., senior author, holder of the June and Virgil Waggoner Chair and Chairman of the Department of Neurobiology and Anatomy at the UTHealth Medical School. “There is no satisfactory treatment at this time.”

Byrne’s laboratory is known for its use of a large snail called Aplysia californica to further the understanding of the biochemical signaling among nerve cells (neurons).  The snails have large neurons that relay information much like those in humans.

When Byrne’s team compared cell cultures taken from normal snails to

  • those administered a dose of a cancer drug called doxorubicin,

the investigators pinpointed a neuronal pathway

  • that was no longer passing along information properly.

With the aid of an experimental drug,

  • the scientists were able to reopen the pathway.

Unfortunately, this drug would not be appropriate for humans, Byrne said. “We want to identify other drugs that can rescue these memory mechanisms,” he added.

According the American Cancer Society, some of the distressing mental changes cancer patients experience may last a short time or go on for years.

Byrne’s UT Health research team includes co-lead authors Rong-Yu Liu, Ph.D., and Yili Zhang, Ph.D., as well as Brittany Coughlin and Leonard J. Cleary, Ph.D. All are affiliated with the W.M. Keck Center for the Neurobiology of Learning and Memory.

Byrne and Cleary also are on the faculty of The University of Texas Graduate School of Biomedical Sciences at Houston. Coughlin is a student at the school, which is jointly operated by UT Health and The University of Texas MD Anderson Cancer Center.

The study titled “Doxorubicin Attenuates Serotonin-Induced Long-Term Synaptic Facilitation by Phosphorylation of p38 Mitogen-Activated Protein Kinase” received support from National Institutes of Health grant (NS019895) and the Zilkha Family Discovery Fellowship.

Doxorubicin Attenuates Serotonin-Induced Long-Term Synaptic Facilitation by Phosphorylation of p38 Mitogen-Activated Protein Kinase

Source: Univ. of Texas Health Science Center at Houston

http://www.rdmag.com/news/2014/10/neuroscientists-use-snail-research-help-explain-E2_9_Cchemo-brain

Doxorubicin Attenuates Serotonin-Induced Long-Term Synaptic Facilitation by Phosphorylation of p38 Mitogen-Activated Protein Kinase

Rong-Yu Liu*,  Yili Zhang*,  Brittany L. Coughlin,  Leonard J. Cleary, and  John H. Byrne   +Show Affiliations
The Journal of Neuroscience, 1 Oct 2014, 34(40): 13289-13300;
http://dx.doi.org:/10.1523/JNEUROSCI.0538-14.2014

Doxorubicin (DOX) is an anthracycline used widely for cancer chemotherapy. Its primary mode of action appears to be

  • topoisomerase II inhibition, DNA cleavage, and free radical generation.

However, in non-neuronal cells, DOX also inhibits the expression of

  • dual-specificity phosphatases (also referred to as MAPK phosphatases) and thereby
  1. inhibits the dephosphorylation of extracellular signal-regulated kinase (ERK) and
  2. p38 mitogen-activated protein kinase (p38 MAPK),
  3. two MAPK isoforms important for long-term memory (LTM) formation.

Activation of these kinases by DOX in neurons, if present,

  • could have secondary effects on cognitive functions, such as learning and memory.

The present study used cultures of rat cortical neurons and sensory neurons (SNs) of Aplysia

  • to examine the effects of DOX on levels of phosphorylated ERK (pERK) and
  • phosphorylated p38 (p-p38) MAPK.

In addition, Aplysia neurons were used to examine the effects of DOX on

  • long-term enhanced excitability, long-term synaptic facilitation (LTF), and
  • long-term synaptic depression (LTD).

DOX treatment led to elevated levels of

  • pERK and p-p38 MAPK in SNs and cortical neurons.

In addition, it increased phosphorylation of

  • the downstream transcriptional repressor cAMP response element-binding protein 2 in SNs.

DOX treatment blocked serotonin-induced LTF and enhanced LTD induced by the neuropeptide Phe-Met-Arg-Phe-NH2. The block of LTF appeared to be attributable to

  • overriding inhibitory effects of p-p38 MAPK, because
  • LTF was rescued in the presence of an inhibitor of p38 MAPK
    (SB203580 [4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)-1H-imidazole]) .

These results suggest that acute application of DOX might impair the formation of LTM via the p38 MAPK pathway.
Terms: Aplysia chemotherapy ERK  p38 MAPK serotonin synaptic plasticity

Technology that controls brain cells with radio waves earns early BRAIN grant

10/08/2014

bright spots = cells with increased calcium after treatment with radio waves,  allows neurons to fire

bright spots = cells with increased calcium after treatment with radio waves, allows neurons to fire

BRAIN control: The new technology uses radio waves to activate or silence cells remotely. The bright spots above represent cells with increased calcium after treatment with radio waves, a change that would allow neurons to fire.

A proposal to develop a new way to

  • remotely control brain cells

from Sarah Stanley, a research associate in Rockefeller University’s Laboratory of Molecular Genetics, headed by Jeffrey M. Friedman, is

  • among the first to receive funding from U.S. President Barack Obama’s BRAIN initiative.

The project will make use of a technique called

  • radiogenetics that combines the use of radio waves or magnetic fields with
  • nanoparticles to turn neurons on or off.

The National Institutes of Health is one of four federal agencies involved in the BRAIN (Brain Research through Advancing Innovative Neurotechnologies) initiative. Following in the ambitious footsteps of the Human Genome Project, the BRAIN initiative seeks

  • to create a dynamic map of the brain in action,

a goal that requires the development of new technologies. The BRAIN initiative working group, which outlined the broad scope of the ambitious project, was co-chaired by Rockefeller’s Cori Bargmann, head of the Laboratory of Neural Circuits and Behavior.

Stanley’s grant, for $1.26 million over three years, is one of 58 projects to get BRAIN grants, the NIH announced. The NIH’s plan for its part of this national project, which has been pitched as “America’s next moonshot,” calls for $4.5 billion in federal funds over 12 years.

The technology Stanley is developing would

  • enable researchers to manipulate the activity of neurons, as well as other cell types,
  • in freely moving animals in order to better understand what these cells do.

Other techniques for controlling selected groups of neurons exist, but her new nanoparticle-based technique has a

  • unique combination of features that may enable new types of experimentation.
  • it would allow researchers to rapidly activate or silence neurons within a small area of the brain or
  • dispersed across a larger region, including those in difficult-to-access locations.

Stanley also plans to explore the potential this method has for use treating patients.

“Francis Collins, director of the NIH, has discussed

  • the need for studying the circuitry of the brain,
  • which is formed by interconnected neurons.

Our remote-control technology may provide a tool with which researchers can ask new questions about the roles of complex circuits in regulating behavior,” Stanley says.
Rockefeller University’s Laboratory of Molecular Genetics
Source: Rockefeller Univ.

Part 4.  Cancer

Two Proteins Found to Block Cancer Metastasis

Why do some cancers spread while others don’t? Scientists have now demonstrated that

  • metastatic incompetent cancers actually “poison the soil”
  • by generating a micro-environment that blocks cancer cells
  • from settling and growing in distant organs.

The “seed and the soil” hypothesis proposed by Stephen Paget in 1889 is now widely accepted to explain how

  • cancer cells (seeds) are able to generate fertile soil (the micro-environment)
  • in distant organs that promotes cancer’s spread.

However, this concept had not explained why some tumors do not spread or metastasize.

The researchers, from Weill Cornell Medical College, found that

  • two key proteins involved in this process work by
  • dramatically suppressing cancer’s spread.

The study offers hope that a drug based on these

  • potentially therapeutic proteins, prosaposin and Thrombospondin 1 (Tsp-1),

might help keep human cancer at bay and from metastasizing.

Scientists don’t understand why some tumors wouldn’t “want” to spread. It goes against their “job description,” says the study’s senior investigator, Vivek Mittal, Ph.D., an associate professor of cell and developmental biology in cardiothoracic surgery and director of the Neuberger Berman Foundation Lung Cancer Laboratory at Weill Cornell Medical College. He theorizes that metastasis occurs when

  • the barriers that the body throws up to protect itself against cancer fail.

But there are some tumors in which some of the barriers may still be intact. “So that suggests

  • those primary tumors will continue to grow, but that
  • an innate protective barrier still exists that prevents them from spreading and invading other organs,”

The researchers found that, like typical tumors,

  • metastasis-incompetent tumors also send out signaling molecules
  • that establish what is known as the “premetastatic niche” in distant organs.

These niches composed of bone marrow cells and various growth factors have been described previously by others including Dr. Mittal as the fertile “soil” that the disseminated cancer cell “seeds” grow in.

Weill Cornell’s Raúl Catena, Ph.D., a postdoctoral fellow in Dr. Mittal’s laboratory, found an important difference between the tumor types. Metastatic-incompetent tumors

  • systemically increased expression of Tsp-1, a molecule known to fight cancer growth.
  • increased Tsp-1 production was found specifically in the bone marrow myeloid cells
  • that comprise the metastatic niche.

These results were striking, because for the first time Dr. Mittal says

  • the bone marrow-derived myeloid cells were implicated as
  • the main producers of Tsp-1,.

In addition, Weill Cornell and Harvard researchers found that

  • prosaposin secreted predominantly by the metastatic-incompetent tumors
  • increased expression of Tsp-1 in the premetastatic lungs.

Thus, Dr. Mittal posits that prosaposin works in combination with Tsp-1

  • to convert pro-metastatic bone marrow myeloid cells in the niche
  • into cells that are not hospitable to cancer cells that spread from a primary tumor.
  • “The very same myeloid cells in the niche that we know can promote metastasis
  • can also be induced under the command of the metastatic incompetent primary tumor to inhibit metastasis,”

The research team found that

  • the Tsp-1–inducing activity of prosaposin
  • was contained in only a 5-amino acid peptide region of the protein, and
  • this peptide alone induced Tsp-1 in the bone marrow cells and
  • effectively suppressed metastatic spread in the lungs
  • in mouse models of breast and prostate cancer.

This 5-amino acid peptide with Tsp-1–inducing activity

  • has the potential to be used as a therapeutic agent against metastatic cancer,

The scientists have begun to test prosaposin in other tumor types or metastatic sites.

Dr. Mittal says that “The clinical implications of the study are:

  • “Not only is it theoretically possible to design a prosaposin-based drug or drugs
  • that induce Tsp-1 to block cancer spread, but
  • you could potentially create noninvasive prognostic tests
  • to predict whether a cancer will metastasize.”

The study was reported in the April 30 issue of Cancer Discovery, in a paper titled “Bone Marrow-Derived Gr1+ Cells Can Generate a Metastasis-Resistant Microenvironment Via Induced Secretion of Thrombospondin-1”.

Disabling Enzyme Cripples Tumors, Cancer Cells

First Step of Metastasis

First Step of Metastasis

Published: Sep 05, 2013  http://www.technologynetworks.com/Metabolomics/news.aspx?id=157138

Knocking out a single enzyme dramatically cripples the ability of aggressive cancer cells to spread and grow tumors.

The paper, published in the journal Proceedings of the National Academy of Sciences, sheds new light on the importance of lipids, a group of molecules that includes fatty acids and cholesterol, in the development of cancer.

Researchers have long known that cancer cells metabolize lipids differently than normal cells. Levels of ether lipids – a class of lipids that are harder to break down – are particularly elevated in highly malignant tumors.

“Cancer cells make and use a lot of fat and lipids, and that makes sense because cancer cells divide and proliferate at an accelerated rate, and to do that,

  • they need lipids, which make up the membranes of the cell,”

said study principal investigator Daniel Nomura, assistant professor in UC Berkeley’s Department of Nutritional Sciences and Toxicology. “Lipids have a variety of uses for cellular structure, but what we’re showing with our study is that

  • lipids can send signals that fuel cancer growth.”

In the study, Nomura and his team tested the effects of reducing ether lipids on human skin cancer cells and primary breast tumors. They targeted an enzyme,

  • alkylglycerone phosphate synthase, or AGPS,
  • known to be critical to the formation of ether lipids.

The researchers confirmed that

  1. AGPS expression increased when normal cells turned cancerous.
  2. inactivating AGPS substantially reduced the aggressiveness of the cancer cells.

“The cancer cells were less able to move and invade,” said Nomura.

The researchers also compared the impact of

  • disabling the AGPS enzyme in mice that had been injected with cancer cells.

Nomura. observes -“Among the mice that had the AGPS enzyme inactivated,

  • the tumors were nonexistent,”

“The mice that did not have this enzyme

  • disabled rapidly developed tumors.”

The researchers determined that

  • inhibiting AGPS expression depleted the cancer cells of ether lipids.
  • AGPS altered levels of other types of lipids important to the ability of the cancer cells to survive and spread, including
    • prostaglandins and acyl phospholipids.

“What makes AGPS stand out as a treatment target is that the enzyme seems to simultaneously

  • regulate multiple aspects of lipid metabolism
  • important for tumor growth and malignancy.”

Future steps include the

  • development of AGPS inhibitors for use in cancer therapy,

“This study sheds considerable light on the important role that AGPS plays in ether lipid metabolism in cancer cells, and it suggests that

  • inhibitors of this enzyme could impair tumor formation,”

said Benjamin Cravatt, Professor and Chair of Chemical Physiology at The Scripps Research Institute, who is not part of the UC.

Agilent Technologies Thought Leader Award Supports Translational Research Program
Published: Mon, March 04, 2013

The award will support Dr DePinho’s research into

  • metabolic reprogramming in the earliest stages of cancer.

Agilent Technologies Inc. announces that Dr. Ronald A. DePinho, a world-renowned oncologist and researcher, has received an Agilent Thought Leader Award.

DePinho is president of the University of Texas MD Anderson Cancer Center. DePinho and his team hope to discover and characterize

  • alterations in metabolic flux during tumor initiation and maintenance, and to identify biomarkers for early detection of pancreatic cancer together with
  • novel therapeutic targets.

Researchers on his team will work with scientists from the university’s newly formed Institute of Applied Cancer Sciences.

The Agilent Thought Leader Award provides funds to support personnel as well as a state-of-the-art Agilent 6550 iFunnel Q-TOF LC/MS system.

“I am extremely pleased to receive this award for metabolomics research, as the survival rates for pancreatic cancer have not significantly improved over the past 20 years,” DePinho said. “This technology will allow us to

  • rapidly identify new targets that drive the formation, progression and maintenance of pancreatic cancer.

Discoveries from this research will also lead to

  • the development of effective early detection biomarkers and novel therapeutic interventions.”

“We are proud to support Dr. DePinho’s exciting translational research program, which will make use of

  • metabolomics and integrated biology workflows and solutions in biomarker discovery,”

said Patrick Kaltenbach, Agilent vice president, general manager of the Liquid Phase Division, and the executive sponsor of this award.

The Agilent Thought Leader Program promotes fundamental scientific advances by support of influential thought leaders in the life sciences and chemical analysis fields.

The covalent modifier Nedd8 is critical for the activation of Smurf1 ubiquitin ligase in tumorigenesis

Ping Xie, Minghua Zhang, Shan He, Kefeng Lu, Yuhan Chen, Guichun Xing, et al.
Nature Communications
  2014; 5(3733).  http://dx.doi.org:/10.1038/ncomms4733

Neddylation, the covalent attachment of ubiquitin-like protein Nedd8, of the Cullin-RING E3 ligase family

  • regulates their ubiquitylation activity.

However, regulation of HECT ligases by neddylation has not been reported to date. Here we show that

  • the C2-WW-HECT ligase Smurf1 is activated by neddylation.

Smurf1 physically interacts with

  1. Nedd8 and Ubc12,
  2. forms a Nedd8-thioester intermediate, and then
  3. catalyses its own neddylation on multiple lysine residues.

Intriguingly, this autoneddylation needs

  • an active site at C426 in the HECT N-lobe.

Neddylation of Smurf1 potently enhances

  • ubiquitin E2 recruitment and
  • augments the ubiquitin ligase activity of Smurf1.

The regulatory role of neddylation

  • is conserved in human Smurf1 and yeast Rsp5.

Furthermore, in human colorectal cancers,

  • the elevated expression of Smurf1, Nedd8, NAE1 and Ubc12
  • correlates with cancer progression and poor prognosis.

These findings provide evidence that

  • neddylation is important in HECT ubiquitin ligase activation and
  • shed new light on the tumour-promoting role of Smurf1.
 Swinging domains in HECT E3

Swinging domains in HECT E3

Subject terms: Biological sciences Cancer Cell biology

Figure 1: Smurf1 expression is elevated in colorectal cancer tissues.

Smurf1 expression is elevated in colorectal cancer tissues.

Smurf1 expression is elevated in colorectal cancer tissues.

(a) Smurf1 expression scores are shown as box plots, with the horizontal lines representing the median; the bottom and top of the boxes representing the 25th and 75th percentiles, respectively; and the vertical bars representing the ra

Figure 2: Positive correlation of Smurf1 expression with Nedd8 and its interacting enzymes in colorectal cancer.

Positive correlation of Smurf1 expression with Nedd8 and its interacting enzymes in colorectal cancer

Positive correlation of Smurf1 expression with Nedd8 and its interacting enzymes in colorectal cancer

(a) Representative images from immunohistochemical staining of Smurf1, Ubc12, NAE1 and Nedd8 in the same colorectal cancer tumour. Scale bars, 100 μm. (bd) The expression scores of Nedd8 (b, n=283 ), NAE1 (c, n=281) and Ubc12 (d, n=19…

Figure 3: Smurf1 interacts with Ubc12.

Smurf1 interacts with Ubc12

Smurf1 interacts with Ubc12

(a) GST pull-down assay of Smurf1 with Ubc12. Both input and pull-down samples were subjected to immunoblotting with anti-His and anti-GST antibodies. Smurf1 interacted with Ubc12 and UbcH5c, but not with Ubc9. (b) Mapping the regions…

Figure 4: Nedd8 is attached to Smurf1through C426-catalysed autoneddylation.

Nedd8 is attached to Smurf1through C426-catalysed autoneddylation

Nedd8 is attached to Smurf1through C426-catalysed autoneddylation

(a) Covalent neddylation of Smurf1 in vitro.Purified His-Smurf1-WT or C699A proteins were incubated with Nedd8 and Nedd8-E1/E2. Reactions were performed as described in the Methods section. Samples were analysed by western blotting wi…

Figure 5: Neddylation of Smurf1 activates its ubiquitin ligase activity.

Neddylation of Smurf1 activates its ubiquitin ligase activity.

Neddylation of Smurf1 activates its ubiquitin ligase activity.

(a) In vivo Smurf1 ubiquitylation assay. Nedd8 was co-expressed with Smurf1 WT or C699A in HCT116 cells (left panels). Twenty-four hours post transfection, cells were treated with MG132 (20 μM, 8 h). HCT116 cells were transfected with…

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The deubiquitylase USP33 discriminates between RALB functions in autophagy and innate immune response

M Simicek, S Lievens, M Laga, D Guzenko, VN. Aushev, et al.
Nature Cell Biology 2013; 15, 1220–1230    http://dx.doi.org:/10.1038/ncb2847

The RAS-like GTPase RALB mediates cellular responses to nutrient availability or viral infection by respectively

  • engaging two components of the exocyst complex, EXO84 and SEC5.
  1. RALB employs SEC5 to trigger innate immunity signalling, whereas
  2. RALB–EXO84 interaction induces autophagocytosis.

How this differential interaction is achieved molecularly by the RAL GTPase remains unknown.

We found that whereas GTP binding

  • turns on RALB activity,

ubiquitylation of RALB at Lys 47

  • tunes its activity towards a particular effector.

Specifically, ubiquitylation at Lys 47

  • sterically inhibits RALB binding to EXO84, while
  • facilitating its interaction with SEC5.

Double-stranded RNA promotes

  • RALB ubiquitylation and
  • SEC5–TBK1 complex formation.

In contrast, nutrient starvation

  • induces RALB deubiquitylation
  • by accumulation and relocalization of the deubiquitylase USP33
  • to RALB-positive vesicles.

Deubiquitylated RALB

  • promotes the assembly of the RALB–EXO84–beclin-1 complexes
  • driving autophagosome formation. Thus,
  • ubiquitylation within the effector-binding domain
  • provides the switch for the dual functions of RALB in
    • autophagy and innate immune responses.

Part 5. Metabolic Syndrome

Single Enzyme is Necessary for Development of Diabetes

Published: Aug 20, 2014 http://www.technologynetworks.com/Metabolomics/news.aspx?ID=169416

12-LO enzyme promotes the obesity-induced oxidative stress in the pancreatic cells.

An enzyme called 12-LO promotes the obesity-induced oxidative stress in the pancreatic cells that leads

  • to pre-diabetes, and diabetes.

12-LO’s enzymatic action is the last step in

  • the production of certain small molecules that harm the cell,

according to a team from Indiana University School of Medicine, Indianapolis.

The findings will enable the development of drugs that can interfere with this enzyme, preventing or even reversing diabetes. The research is published ahead of print in the journal Molecular and Cellular Biology.

In earlier studies, these researchers and their collaborators at Eastern Virginia Medical School showed that

  • 12-LO (which stands for 12-lipoxygenase) is present in these cells
  • only in people who become overweight.

The harmful small molecules resulting from 12-LO’s enzymatic action are known as HETEs, short for hydroxyeicosatetraenoic acid.

  1. HETEs harm the mitochondria, which then
  2. fail to produce sufficient energy to enable
  3. the pancreatic cells to manufacture the necessary quantities of insulin.

For the study, the investigators genetically engineered mice that

  • lacked the gene for 12-LO exclusively in their pancreas cells.

Mice were either fed a low-fat or high-fat diet.

Both the control mice and the knockout mice on the high fat diet

  • developed obesity and insulin resistance.

The investigators also examined the pancreatic beta cells of both knockout and control mice, using both microscopic studies and molecular analysis. Those from the knockout mice were intact and healthy, while

  • those from the control mice showed oxidative damage,
  • demonstrating that 12-LO and the resulting HETEs
  • caused the beta cell failure.

Mirmira notes that fatty diet used in the study was the Western Diet, which comprises mostly saturated-“bad”-fats. Based partly on a recent study of related metabolic pathways, he says that

  • the unsaturated and mono-unsaturated fats-which comprise most fats in the healthy,
  • relatively high fat Mediterranean diet-are unlikely to have the same effects.

“Our research is the first to show that 12-LO in the beta cell

  • is the culprit in the development of pre-diabetes, following high fat diets,” says Mirmira.

“Our work also lends important credence to the notion that

  • the beta cell is the primary defective cell in virtually all forms of diabetes and pre-diabetes.”

A New Player in Lipid Metabolism Discovered

Published: Aug18, 2014  http://www.technologynetworks.com/Metabolomics/news.aspx?ID=169356

Specially engineered mice gained no weight, and normal counterparts became obese

  • on the same high-fat, obesity-inducing Western diet.

Specially engineered mice that lacked a particular gene did not gain weight

  • when fed a typical high-fat, obesity-inducing Western diet.

Yet, these mice ate the same amount as their normal counterparts that became obese.

The mice were engineered with fat cells that lacked a gene called SEL1L,

  • known to be involved in the clearance of mis-folded proteins
  • in the cell’s protein making machinery called the endoplasmic reticulum (ER).

When mis-folded proteins are not cleared but accumulate,

  • they destroy the cell and contribute to such diseases as
  1. mad cow disease,
  2. Type 1 diabetes and
  3. cystic fibrosis.

“The million-dollar question is why don’t these mice gain weight? Is this related to its inability to clear mis-folded proteins in the ER?” said Ling Qi, associate professor of molecular and biochemical nutrition and senior author of the study published online July 24 in Cell Metabolism. Haibo Sha, a research associate in Qi’s lab, is the paper’s lead author.

Interestingly, the experimental mice developed a host of other problems, including

  • postprandial hypertriglyceridemia,
  • and fatty livers.

“Although we are yet to find out whether these conditions contribute to the lean phenotype, we found that

  • there was a lipid partitioning defect in the mice lacking SEL1L in fat cells,
  • where fat cells cannot store fat [lipids], and consequently
  • fat goes to the liver.

During the investigation of possible underlying mechanisms, we discovered

  • a novel function for SEL1L as a regulator of lipid metabolism,” said Qi.

Sha said “We were very excited to find that

  • SEL1L is required for the intracellular trafficking of
  • lipoprotein lipase (LPL), acting as a chaperone,” .

and added that “Using several tissue-specific knockout mouse models,

  • we showed that this is a general phenomenon,”

Without LPL, lipids remain in the circulation;

  • fat and muscle cells cannot absorb fat molecules for storage and energy combustion,

People with LPL mutations develop

  • postprandial hypertriglyceridemia similar to
  • conditions found in fat cell-specific SEL1L-deficient mice, said Qi.

Future work will investigate the

  • role of SEL1L in human patients carrying LPL mutations and
  • determine why fat cell-specific SEL1L-deficient mice remain lean under Western diets, said Sha.

Co-authors include researchers from Cedars-Sinai Medical Center in Los Angeles; Wageningen University in the Netherlands; Georgia State University; University of California, Los Angeles; and the Medical College of Soochow University in China.

The study was funded by the U.S. National Institutes of Health, the Netherlands Organization for Health Research and Development National Institutes of Health, the Cedars-Sinai Medical Center, Chinese National Science Foundation, the American Diabetes Association, Cornell’s Center for Vertebrate Genomics and the Howard Hughes Medical Institute.

Part 6. Biomarkers

Biomarkers Take Center Stage

Josh P. Roberts
GEN May 1, 2013 (Vol. 33, No. 9)  http://www.genengnews.com/

While work with biomarkers continues to grow, scientists are also grappling with research-related bottlenecks, such as

  1. affinity reagent development,
  2. platform reproducibility, and
  3. sensitivity.

Biomarkers by definition indicate some state or process that generally occurs

  • at a spatial or temporal distance from the marker itself, and

it would not be an exaggeration to say that biomedicine has become infatuated with them:

  1. where to find them,
  2. when they may appear,
  3. what form they may take, and
  4. how they can be used to diagnose a condition or
  5. predict whether a therapy may be successful.

Biomarkers are on the agenda of many if not most industry gatherings, and in cases such as Oxford Global’s recent “Biomarker Congress” and the GTC “Biomarker Summit”, they hold the naming rights. There, some basic principles were built upon, amended, and sometimes challenged.

In oncology, for example, biomarker discovery is often predicated on the premise that

  • proteins shed from a tumor will traverse to and persist in, and be detectable in, the circulation.

By quantifying these proteins—singularly or as part of a larger “signature”—the hope is

  1. to garner information about the molecular characteristics of the cancer
  2. that will help with cancer detection and
  3. personalization of the treatment strategy.

Yet this approach has not yet turned into the panacea that was hoped for. Bottlenecks exist in

  • affinity reagent development,
  • platform reproducibility, and
  • sensitivity.

There is also a dearth of understanding of some of the

  • fundamental principles of biomarker biology that we need to know the answers to,

said Parag Mallick, Ph.D., whose lab at Stanford University is “working on trying to understand where biomarkers come from.”

There are dogmas saying that

  • circulating biomarkers come solely from secreted proteins.

But Dr. Mallick’s studies indicate that fully

  • 50% of circulating proteins may come from intracellular sources or
  • proteins that are annotated as such.

“We don’t understand the processes governing

  • which tumor-derived proteins end up in the blood.”

Other questions include “how does the size of a tumor affect how much of a given protein will be in the blood?”—perhaps

  • the tumor is necrotic at the center, or
  • it’s hypervascular or hypovascular.

He points out “The problem is that these are highly nonlinear processes at work, and

  • there is a large number of factors that might affect the answer to that question,” .

Their research focuses on using

  1. mass spectrometry and
  2. computational analysis
  • to characterize the biophysical properties of the circulating proteome, and
  • relate these to measurements made of the tumor itself.

Furthermore, he said – “We’ve observed that the proteins that are likely to

  • first show up and persist in the circulation, ..
  • are more stable than proteins that don’t,”
  • “we can quantify how significant the effect is.”

The goal is ultimately to be able to

  1. build rigorous, formal mathematical models that will allow something measured in the blood
  2. to be tied back to the molecular biology taking place in the tumor.

And conversely, to use those models

  • to predict from a tumor what will be found in the circulation.

“Ultimately, the models will allow you to connect the dots between

  • what you measure in the blood and the biology of the tumor.”

Bound for Affinity Arrays

Affinity reagents are the main tools for large-scale protein biomarker discovery. And while this has tended to mean antibodies (or their derivatives), other affinity reagents are demanding a place in the toolbox.

Affimers, a type of affinity reagent being developed by Avacta, consist of

  1. a biologically inert, biophysically stable protein scaffold
  2. containing three variable regions into which
  3. distinct peptides are inserted.

The resulting three-dimensional surface formed by these peptides

  • interacts and binds to proteins and other molecules in solution,
  • much like the antigen-binding site of antibodies.

Unlike antibodies, Affimers are relatively small (13 KDa),

  • non-post-translationally modified proteins
  • that can readily be expressed in bacterial culture.

They may be made to bind surfaces through unique residues

  • engineered onto the opposite face of the Affimer,
  • allowing the binding site to be exposed to the target in solution.

“We don’t seem to see in what we’ve done so far

  • any real loss of activity or functionality of Affimers when bound to surfaces—

they’re very robust,” said CEO Alastair Smith, Ph.D.

Avacta is taking advantage of this stability and its large libraries of Affimers to develop

  • very large affinity microarrays for
  • drug and biomarker discovery.

To date they have printed arrays with around 20–25,000 features, and Dr. Smith is “sure that we can get toward about 50,000 on a slide,” he said. “There’s no real impediment to us doing that other than us expressing the proteins and getting on with it.”

Customers will be provided with these large, complex “naïve” discovery arrays, readable with standard equipment. The plan is for the company to then “support our customers by providing smaller arrays with

  • the Affimers that are binding targets of interest to them,” Dr. Smith foretold.

And since the intellectual property rights are unencumbered,

  • Affimers in those arrays can be licensed to the end users
  • to develop diagnostics that can be validated as time goes on.

Around 20,000-Affimer discovery arrays were recently tested by collaborator Professor Ann Morgan of the University of Leeds with pools of unfractionated serum from patients with symptoms of inflammatory disease. The arrays

  • “rediscovered” elevated C-reactive protein (CRP, the clinical gold standard marker)
  • as well as uncovered an additional 22 candidate biomarkers.
  • other candidates combined with CRP, appear able to distinguish between different diseases such as
  1. rheumatoid arthritis,
  2. psoriatic arthritis,
  3. SLE, or
  4. giant cell arteritis.

Epigenetic Biomarkers

Methylation of adenine

Sometimes biomarkers are used not to find disease but

  • to distinguish healthy human cell types, with
  •  examples being found in flow cytometry and immunohistochemistry.

These widespread applications, however, are difficult to standardize, being

  • subject to arbitrary or subjective gating protocols and other imprecise criteria.

Epiontis instead uses an epigenetic approach. “What we need is a unique marker that is

  • demethylated only in one cell type and
  • methylated in all the other cell types,”

Each cell of the right cell type will have

  • two demethylated copies of a certain gene locus,
  • allowing them to be enumerated by quantitative PCR.

The biggest challenge is finding that unique epigenetic marker. To do so they look through the literature for proteins and genes described as playing a role in the cell type’s biology, and then

  • look at the methylation patterns to see if one can be used as a marker,

They also “use customized Affymetrix chips to look at the

  • differential epigenetic status of different cell types on a genomewide scale.”

explained CBO and founder Ulrich Hoffmueller, Ph.D.

The company currently has a panel of 12 assays for 12 immune cell types. Among these is an assay for

  • regulatory T (Treg) cells that queries the Foxp3 gene—which is uniquely demethylated in Treg
  • even though it is transiently expressed in activated T cells of other subtypes.

Also assayed are Th17 cells, difficult to detect by flow cytometry because

  • “the cells have to be stimulated in vitro,” he pointed out.

Developing New Assays for Cancer Biomarkers

Researchers at Myriad RBM and the Cancer Prevention Research Institute of Texas are collaborating to develop

  • new assays for cancer biomarkers on the Myriad RBM Multi-Analyte Profile (MAP) platform.

The release of OncologyMAP 2.0 expanded Myriad RBM’s biomarker menu to over 250 analytes, which can be measured from a small single sample, according to the company. Using this menu, L. Stephen et al., published a poster, “Analysis of Protein Biomarkers in Prostate and Colorectal Tumor Lysates,” which showed the results of

  • a survey of proteins relevant to colorectal (CRC) and prostate (PC) tumors
  • to identify potential proteins of interest for cancer research.

The study looked at CRC and PC tumor lysates and found that 102 of the 115 proteins showed levels above the lower limit of quantification.

  • Four markers were significantly higher in PC and 10 were greater in CRC.

For most of the analytes, duplicate sections of the tumor were similar, although some analytes did show differences. In four of the CRC analytes, tumor number four showed differences for CEA and tumor number 2 for uPA.

Thirty analytes were shown to be

  • different in CRC tumor compared to its adjacent tissue.
  • Ten of the analytes were higher in adjacent tissue compared to CRC.
  • Eighteen of the markers examined demonstrated  —-

significant correlations of CRC tumor concentration to serum levels.

“This suggests.. that the Oncology MAP 2.0 platform “provides a good method for studying changes in tumor levels because many proteins can be assessed with a very small sample.”

Clinical Test Development with MALDI-ToF

While there have been many attempts to translate results from early discovery work on the serum proteome into clinical practice, few of these efforts have progressed past the discovery phase.

Matrix-assisted laser desorption/ionization-time of flight (MALDI-ToF) mass spectrometry on unfractionated serum/plasma samples offers many practical advantages over alternative techniques, and does not require

  • a shift from discovery to development and commercialization platforms.

Biodesix claims it has been able to develop the technology into

  • a reproducible, high-throughput tool to
  • routinely measure protein abundance from serum/plasma samples.

“.. we improved data-analysis algorithms to

  • reproducibly obtain quantitative measurements of relative protein abundance from MALDI-ToF mass spectra.

Heinrich Röder, CTO points out that the MALDI-ToF measurements

  • are combined with clinical outcome data using
  • modern learning theory techniques
  • to define specific disease states
  • based on a patient’s serum protein content,”

The clinical utility of the identification of these disease states can be investigated through a retrospective analysis of differing sample sets. For example, Biodesix clinically validated its first commercialized serum proteomic test, VeriStrat®, in 85 different retrospective sample sets.

Röder adds that “It is becoming increasingly clear that

  • the patients whose serum is characterized as VeriStrat Poor show
  • consistently poor outcomes irrespective of
  1. tumor type,
  2. histology, or
  3. molecular tumor characteristics,”

MALDI-ToF mass spectrometry, in its standard implementation,

  • allows for the observation of around 100 mostly high-abundant serum proteins.

Further, “while this does not limit the usefulness of tests developed from differential expression of these proteins,

  • the discovery potential would be greatly enhanced
  • if we could probe deeper into the proteome
  • while not giving up the advantages of the MALDI-ToF approach,”

Biodesix reports that its new MALDI approach, Deep MALDI™, can perform

  • simultaneous quantitative measurement of more than 1,000 serum protein features (or peaks) from 10 µL of serum in a high-throughput manner.
  • it increases the observable signal noise ratio from a few hundred to over 50,000,
  • resulting in the observation of many lower-abundance serum proteins.

Breast cancer, a disease now considered to be a collection of many complexes of symptoms and signatures—the dominant ones are labeled Luminal A, Luminal B, Her2, and Basal— which suggests different prognose, and

  • these labels are considered too simplistic for understanding and managing a woman’s cancer.

Studies published in the past year have looked at

  1. somatic mutations,
  2. gene copy number aberrations,
  3. gene expression abnormalities,
  4. protein and miRNA expression, and
  5. DNA methylation,

coming up with a list of significantly mutated genes—hot spots—in different categories of breast cancers. Targeting these will inevitably be the focus of much coming research.

“We’ve been taking these large trials and profiling these on a variety of array or sequence platforms. We think we’ll get

  1. prognostic drivers
  2. predictive markers for taxanes and
  3. monoclonal antibodies and
  4. tamoxifen and aromatase inhibitors,”
    explained Brian Leyland-Jones, Ph.D., director of Edith Sanford Breast Cancer Research. “We will end up with 20–40 different diseases, maybe more.”

Edith Sanford Breast Cancer Research is undertaking a pilot study in collaboration with The Scripps Research Institute, using a variety of tests on 25 patients to see how the information they provide complements each other, the overall flow, and the time required to get and compile results.

Laser-captured tumor samples will be subjected to low passage whole-genome, exome, and RNA sequencing (with targeted resequencing done in parallel), and reverse-phase protein and phosphorylation arrays, with circulating nucleic acids and circulating tumor cells being queried as well. “After that we hope to do a 100- or 150-patient trial when we have some idea of the best techniques,” he said.

Dr. Leyland-Jones predicted that ultimately most tumors will be found

  • to have multiple drivers,
  • with most patients receiving a combination of two, three, or perhaps four different targeted therapies.

Reduce to Practice

According to Randox, the evidence Investigator is a sophisticated semi-automated biochip sys­tem designed for research, clinical, forensic, and veterinary applications.

Once biomarkers that may have an impact on therapy are discovered, it is not always routine to get them into clinical practice. Leaving regulatory and financial, intellectual property and cultural issues aside, developing a diagnostic based on a biomarker often requires expertise or patience that its discoverer may not possess.

Andrew Gribben is a clinical assay and development scientist at Randox Laboratories, based in Northern Ireland, U.K. The company utilizes academic and industrial collaborators together with in-house discovery platforms to identify biomarkers that are

  • augmented or diminished in a particular pathology
  • relative to appropriate control populations.

Biomarkers can be developed to be run individually or

  • combined into panels of immunoassays on its multiplex biochip array technology.

Specificity can also be gained—or lost—by the affinity of reagents in an assay. The diagnostic potential of Heart-type fatty acid binding protein (H-FABP) abundantly expressed in human myocardial cells was recognized by Jan Glatz of Maastricht University, The Netherlands, back in 1988. Levels rise quickly within 30 minutes after a myocardial infarction, peaking at 6–8 hours and return to normal within 24–30 hours. Yet at the time it was not known that H-FABP was a member of a multiprotein family, with which the polyclonal antibodies being used in development of an assay were cross-reacting, Gribben related.

Randox developed monoclonal antibodies specific to H-FABP, funded trials investigating its use alone, and multiplexed with cardiac biomarker assays, and, more than 30 years after the biomarker was identified, in 2011, released a validated assay for H-FABP as a biomarker for early detection of acute myocardial infarction.

Ultrasensitive Immunoassays for Biomarker Development

Research has shown that detection and monitoring of biomarker concentrations can provide

  • insights into disease risk and progression.

Cytokines have become attractive biomarkers and candidates

  • for targeted therapies for a number of autoimmune diseases, including rheumatoid arthritis (RA), Crohn’s disease, and psoriasis, among others.

However, due to the low-abundance of circulating cytokines, such as IL-17A, obtaining robust measurements in clinical samples has been difficult.

Singulex reports that its digital single-molecule counting technology provides

  • increased precision and detection sensitivity over traditional ELISA techniques,
  • helping to shed light on biomarker verification and validation programs.

The company’s Erenna® immunoassay system, which includes optimized immunoassays, offers LLoQ to femtogram levels per mL resolution—even in healthy populations, at an improvement of 1-3 fold over standard ELISAs or any conventional technology and with a dynamic range of up to 4-logs, according to a Singulex official, who adds that

  • this sensitivity improvement helps minimize undetectable samples that
  • could otherwise delay or derail clinical studies.

The official also explains that the Singulex solution includes an array of products and services that are being applied to a number of programs and have enabled the development of clinically relevant biomarkers, allowing translation from discovery to the clinic.

In a poster entitled “Advanced Single Molecule Detection: Accelerating Biomarker Development Utilizing Cytokines through Ultrasensitive Immunoassays,” a case study was presented of work performed by Jeff Greenberg of NYU to show how the use of the Erenna system can provide insights toward

  • improving the clinical utility of biomarkers and
  • accelerating the development of novel therapies for treating inflammatory diseases.

A panel of inflammatory biomarkers was examined in DMARD (disease modifying antirheumatic drugs)-naïve RA (rheumatoid arthritis) vs. knee OA (osteoarthritis) patient cohorts. Markers that exhibited significant differences in plasma concentrations between the two cohorts included

  • CRP, IL-6R alpha, IL-6, IL-1 RA, VEGF, TNF-RII, and IL-17A, IL-17F, and IL-17A/F.

Among the three tested isoforms of IL-17,

  • the magnitude of elevation for IL-17F in RA patients was the highest.

“Singulex provides high-resolution monitoring of baseline IL-17A concentrations that are present at low levels,” concluded the researchers. “The technology also enabled quantification of other IL-17 isoforms in RA patients, which have not been well characterized before.”

The Singulex Erenna System has also been applied to cardiovascular disease research, for which its

  • cardiac troponin I (cTnI) digital assay can be used to measure circulating
  • levels of cTnI undetectable by other commercial assays.

Recently presented data from Brigham and Women’s Hospital and the TIMI-22 study showed that

  • using the Singulex test to serially monitor cTnI helps
  • stratify risk in post-acute coronary syndrome patients and
  • can identify patients with elevated cTnI
  • who have the most to gain from intensive vs. moderate-dose statin therapy,

according to the scientists involved in the research.

The study poster, “Prognostic Performance of Serial High Sensitivity Cardiac Troponin Determination in Stable Ischemic Heart Disease: Analysis From PROVE IT-TIMI 22,” was presented at the 2013 American College of Cardiology (ACC) Annual Scientific Session & Expo by R. O’Malley et al.

Biomarkers Changing Clinical Medicine

Better Diagnosis, Prognosis, and Drug Targeting Are among Potential Benefits

  1. John Morrow Jr., Ph.D.

Researchers at EMD Chemicals are developing biomarker immunoassays

  • to monitor drug-induced toxicity including kidney damage.

The pace of biomarker development is accelerating as investigators report new studies on cancer, diabetes, Alzheimer disease, and other conditions in which the evaluation and isolation of workable markers is prominently featured.

Wei Zheng, Ph.D., leader of the R&D immunoassay group at EMD Chemicals, is overseeing a program to develop biomarker immunoassays to

  • monitor drug-induced toxicity, including kidney damage.

“One of the principle reasons for drugs failing during development is because of organ toxicity,” says Dr. Zheng.
“proteins liberated into the serum and urine can serve as biomarkers of adverse response to drugs, as well as disease states.”

Through collaborative programs with Rules-Based Medicine (RBM), the EMD group has released panels for the profiling of human renal impairment and renal toxicity. These urinary biomarker based products fit the FDA and EMEA guidelines for assessment of drug-induced kidney damage in rats.

The group recently performed a screen for potential protein biomarkers in relation to

  • kidney toxicity/damage on a set of urine and plasma samples
  • from patients with documented renal damage.

Additionally, Dr. Zheng is directing efforts to move forward with the multiplexed analysis of

  • organ and cellular toxicity.

Diseases thought to involve compromised oxidative phosphorylation include

  • diabetes, Parkinson and Alzheimer diseases, cancer, and the aging process itself.

Good biomarkers allow Dr. Zheng to follow the mantra, “fail early, fail fast.” With robust, multiplexible biomarkers, EMD can detect bad drugs early and kill them before they move into costly large animal studies and clinical trials. “Recognizing the severe liability that toxicity presents, we can modify the structure of the candidate molecule and then rapidly reassess its performance.”

Scientists at Oncogene Science a division of Siemens Healthcare Diagnostics, are also focused on biomarkers. “We are working on a number of antibody-based tests for various cancers, including a test for the Ca-9 CAIX protein, also referred to as carbonic anhydrase,” Walter Carney, Ph.D., head of the division, states.

CAIX is a transmembrane protein that is

  • overexpressed in a number of cancers, and, like Herceptin and the Her-2 gene,
  • can serve as an effective and specific marker for both diagnostic and therapeutic purposes.
  • It is liberated into the circulation in proportion to the tumor burden.

Dr. Carney and his colleagues are evaluating patients after tumor removal for the presence of the Ca-9 CAIX protein. If

  • the levels of the protein in serum increase over time,
  • this suggests that not all the tumor cells were removed and the tumor has metastasized.

Dr. Carney and his team have developed both an immuno-histochemistry and an ELISA test that could be used as companion diagnostics in clinical trials of CAIX-targeted drugs.

The ELISA for the Ca-9 CAIX protein will be used in conjunction with Wilex’ Rencarex®, which is currently in a

  • Phase III trial as an adjuvant therapy for non-metastatic clear cell renal cancer.

Additionally, Oncogene Science has in its portfolio an FDA-approved test for the Her-2 marker. Originally approved for Her-2/Neu-positive breast cancer, its indications have been expanded over time, and was approved

  • for the treatment of gastric cancer last year.

It is normally present on breast cancer epithelia but

  • overexpressed in some breast cancer tumors.

“Our products are designed to be used in conjunction with targeted therapies,” says Dr. Carney. “We are working with companies that are developing technology around proteins that are

  • overexpressed in cancerous tissues and can be both diagnostic and therapeutic targets.”

The long-term goal of these studies is to develop individualized therapies, tailored for the patient. Since the therapies are expensive, accurate diagnostics are critical to avoid wasting resources on patients who clearly will not respond (or could be harmed) by the particular drug.

“At this time the rate of response to antibody-based therapies may be very poor, as

  • they are often employed late in the course of the disease, and patients are in such a debilitated state
  • that they lack the capacity to react positively to the treatment,” Dr. Carney explains.

Nanoscale Real-Time Proteomics

Stanford University School of Medicine researchers, working with Cell BioSciences, have developed a

  • nanofluidic proteomic immunoassay that measures protein charge,
  • similar to immunoblots, mass spectrometry, or flow cytometry.
  • unlike these platforms, this approach can measure the amount of individual isoforms,
  • specifically, phosphorylated molecules.

“We have developed a nanoscale device for protein measurement, which I believe could be useful for clinical analysis,” says Dean W. Felsher, M.D., Ph.D., associate professor at Stanford University School of Medicine.

Critical oncogenic transformations involving

  • the activation of the signal-related kinases ERK-1 and ERK-2 can now be followed with ease.

“The fact that we measure nanoquantities with accuracy means that

  • we can interrogate proteomic profiles in clinical patients,

by drawing tiny needle aspirates from tumors over the course of time,” he explains.

“This allows us to observe the evolution of tumor cells and

  • their response to therapy
  • from a baseline of the normal tissue as a standard of comparison.”

According to Dr. Felsher, 20 cells is a large enough sample to obtain a detailed description. The technology is easy to automate, which allows

  • the inclusion of hundreds of assays.

Contrasting this technology platform with proteomic analysis using microarrays, Dr. Felsher notes that the latter is not yet workable for revealing reliable markers.

Dr. Felsher and his group published a description of this technology in Nature Medicine. “We demonstrated that we could take a set of human lymphomas and distinguish them from both normal tissue and other tumor types. We can

  • quantify changes in total protein, protein activation, and relative abundance of specific phospho-isoforms
  • from leukemia and lymphoma patients receiving targeted therapy.

Even with very small numbers of cells, we are able to show that the results are consistent, and

  • our sample is a random profile of the tumor.”

Splice Variant Peptides

“Aberrations in alternative splicing may generate

  • much of the variation we see in cancer cells,”

says Gilbert Omenn, Ph.D., director of the center for computational medicine and bioinformatics at the University of Michigan School of Medicine. Dr. Omenn and his colleague, Rajasree Menon, are

  • using this variability as a key to new biomarker identification.

It is becoming evident that splice variants play a significant role in the properties of cancer cells, including

  • initiation, progression, cell motility, invasiveness, and metastasis.

Alternative splicing occurs through multiple mechanisms

  • when the exons or coding regions of the DNA transcribe mRNA,
  • generating initiation sites and connecting exons in protein products.

Their translation into protein can result in numerous protein isoforms, and

  • these isoforms may reflect a diseased or cancerous state.

Regulatory elements within the DNA are responsible for selecting different alternatives; thus

  • the splice variants are tempting targets for exploitation as biomarkers.
Analyses of the splice-site mutation

Analyses of the splice-site mutation

Despite the many questions raised by these observations, splice variation in tumor material has not been widely studied. Cancer cells are known for their tremendous variability, which allows them to

  • grow rapidly, metastasize, and develop resistance to anticancer drugs.

Dr. Omenn and his collaborators used

  • mass spec data to interrogate a custom-built database of all potential mRNA sequences
  • to find alternative splice variants.

When they compared normal and malignant mammary gland tissue from a mouse model of Her2/Neu human breast cancers, they identified a vast number (608) of splice variant proteins, of which

  • peptides from 216 were found only in the tumor sample.

“These novel and known alternative splice isoforms

  • are detectable both in tumor specimens and in plasma and
  • represent potential biomarker candidates,” Dr. Omenn adds.

Dr. Omenn’s observations and those of his colleague Lewis Cantley, Ph.D., have also

  • shed light on the origins of the classic Warburg effect,
  • the shift to anaerobic glycolysis in tumor cells.

The novel splice variant M2, of muscle pyruvate kinase,

  • is observed in embryonic and tumor tissue.

It is associated with this shift, the result of

  • the expression of a peptide splice variant sequence.

It is remarkable how many different areas of the life sciences are tied into the phenomenon of splice variation. The changes in the genetic material can be much greater than point mutations, which have been traditionally considered to be the prime source of genetic variability.

“We now have powerful methods available to uncover a whole new category of variation,” Dr. Omenn says. “High-throughput RNA sequencing and proteomics will be complementary in discovery studies of splice variants.”

Splice variation may play an important role in rapid evolutionary changes, of the sort discussed by Susumu Ohno and Stephen J. Gould decades ago. They, and other evolutionary biologists, argued that

  • gene duplication, combined with rapid variability, could fuel major evolutionary jumps.

At the time, the molecular mechanisms of variation were poorly understood, but today

  • the tools are available to rigorously evaluate the role of
  • splice variation and other contributors to evolutionary change.

“Biomarkers derived from studies of splice variants, could, in the future, be exploited

  • both for diagnosis and prognosis and
  • for drug targeting of biological networks,
  • in situations such as the Her-2/Neu breast cancers,” Dr. Omenn says.

Aminopeptidase Activities

“By correlating the proteolytic patterns with disease groups and controls, we have shown that

  • exopeptidase activities contribute to the generation of not only cancer-specific
  • but also cancer type specific serum peptides.

according to Paul Tempst, Ph.D., professor and director of the Protein Center at the Memorial Sloan-Kettering Cancer Center.

So there is a direct link between peptide marker profiles of disease and differential protease activity.” For this reason Dr. Tempst argues that “the patterns we describe may have value as surrogate markers for detection and classification of cancer.”

To investigate this avenue, Dr. Tempst and his colleagues have followed

  • the relationship between exopeptidase activities and metastatic disease.

“We monitored controlled, de novo peptide breakdown in large numbers of biological samples using mass spectrometry, with relative quantitation of the metabolites,” Dr. Tempst explains. This entailed the use of magnetic, reverse-phase beads for analyte capture and a MALDI-TOF MS read-out.

“In biomarker discovery programs, functional proteomics is usually not pursued,” says Dr. Tempst. “For putative biomarkers, one may observe no difference in quantitative levels of proteins, while at the same time, there may be substantial differences in enzymatic activity.”

In a preliminary prostate cancer study, the team found a significant difference

  • in activity levels of exopeptidases in serum from patients with metastatic prostate cancer
  • as compared to primary tumor-bearing individuals and normal healthy controls.

However, there were no differences in amounts of the target protein, and this potential biomarker would have been missed if quantitative levels of protein had been the only criterion of selection.

It is frequently stated that “practical fusion energy is 30 years in the future and always will be.” The same might be said of functional, practical biomarkers that can pass muster with the FDA. But splice variation represents a new handle on this vexing problem. It appears that we are seeing the emergence of a new approach that may finally yield definitive diagnostic tests, detectable in serum and urine samples.

Part 7. Epigenetics and Drug Metabolism

DNA Methylation Rules: Studying Epigenetics with New Tools

The tools to unravel the epigenetic control mechanisms that influence how cells control access of transcriptional proteins to DNA are just beginning to emerge.

Patricia Fitzpatrick Dimond, Ph.D.

http://www.genengnews.com/media/images/AnalysisAndInsight/Feb7_2013_24454248_GreenPurpleDNA_EpigeneticsToolsII3576166141.jpg

New tools may help move the field of epigenetic analysis forward and potentially unveil novel biomarkers for cellular development, differentiation, and disease.

DNA sequencing has had the power of technology behind it as novel platforms to produce more sequencing faster and at lower cost have been introduced. But the tools to unravel the epigenetic control mechanisms that influence how cells control access of transcriptional proteins to DNA are just beginning to emerge.

Among these mechanisms, DNA methylation, or the enzymatically mediated addition of a methyl group to cytosine or adenine dinucleotides,

  • serves as an inherited epigenetic modification that
  • stably modifies gene expression in dividing cells.

The unique methylomes are largely maintained in differentiated cell types, making them critical to understanding the differentiation potential of the cell.

In the DNA methylation process, cytosine residues in the genome are enzymatically modified to 5-methylcytosine,

  • which participates in transcriptional repression of genes during development and disease progression.

5-methylcytosine can be further enzymatically modified to 5-hydroxymethylcytosine by the TET family of methylcytosine dioxygenases. DNA methylation affects gene transcription by physically

  • interfering with the binding of proteins involved in gene transcription.

Methylated DNA may be bound by methyl-CpG-binding domain proteins (MBDs) that can

  • then recruit additional proteins. Some of these include histone deacetylases and other chromatin remodeling proteins that modify histones, thereby
  • forming compact, inactive chromatin, or heterochromatin.

While DNA methylation doesn’t change the genetic code,

  • it influences chromosomal stability and gene expression.

Epigenetics and Cancer Biomarkers

multistage chemical carcinogenesis

multistage chemical carcinogenesis

And because of the increasing recognition that DNA methylation changes are involved in human cancers, scientists have suggested that these epigenetic markers may provide biological markers for cancer cells, and eventually point toward new diagnostic and therapeutic targets. Cancer cell genomes display genome-wide abnormalities in DNA methylation patterns,

  • some of which are oncogenic and contribute to genome instability.

In particular, de novo methylation of tumor suppressor gene promoters

  • occurs frequently in cancers, thereby silencing them and promoting transformation.

Cytosine hydroxymethylation (5-hydroxymethylcytosine, or 5hmC), the aforementioned DNA modification resulting from the enzymatic conversion of 5mC into 5-hydroxymethylcytosine by the TET family of oxygenases, has been identified

  • as another key epigenetic modification marking genes important for
  • pluripotency in embryonic stem cells (ES), as well as in cancer cells.

The base 5-hydroxymethylcytosine was recently identified as an oxidation product of 5-methylcytosine in mammalian DNA. In 2011, using sensitive and quantitative methods to assess levels of 5-hydroxymethyl-2′-deoxycytidine (5hmdC) and 5-methyl-2′-deoxycytidine (5mdC) in genomic DNA, scientists at the Department of Cancer Biology, Beckman Research Institute of the City of Hope, Duarte, California investigated

  • whether levels of 5hmC can distinguish normal tissue from tumor tissue.

They showed that in squamous cell lung cancers, levels of 5hmdC showed

  • up to five-fold reduction compared with normal lung tissue.

In brain tumors,5hmdC showed an even more drastic reduction

  • with levels up to more than 30-fold lower than in normal brain,
  • but 5hmdC levels were independent of mutations in isocitrate dehydrogenase-1, the enzyme that converts 5hmC to 5hmdC.

Immunohistochemical analysis indicated that 5hmC is “remarkably depleted” in many types of human cancer.

  • there was an inverse relationship between 5hmC levels and cell proliferation with lack of 5hmC in proliferating cells.

Their data suggest that 5hmdC is strongly depleted in human malignant tumors,

  • a finding that adds another layer of complexity to the aberrant epigenome found in cancer tissue.

In addition, a lack of 5hmC may become a useful biomarker for cancer diagnosis.

Enzymatic Mapping

But according to New England Biolabs’ Sriharsa Pradhan, Ph.D., methods for distinguishing 5mC from 5hmC and analyzing and quantitating the cell’s entire “methylome” and “hydroxymethylome” remain less than optimal.

The protocol for bisulphite conversion to detect methylation remains the “gold standard” for DNA methylation analysis. This method is generally followed by PCR analysis for single nucleotide resolution to determine methylation across the DNA molecule. According to Dr. Pradhan, “.. bisulphite conversion does not distinguish 5mC and 5hmC,”

Recently we found an enzyme, a unique DNA modification-dependent restriction endonuclease, AbaSI, which can

  • decode the hydryoxmethylome of the mammalian genome.

You easily can find out where the hydroxymethyl regions are.”

AbaSI, recognizes 5-glucosylatedmethylcytosine (5gmC) with high specificity when compared to 5mC and 5hmC, and

  • cleaves at narrow range of distances away from the recognized modified cytosine.

By mapping the cleaved ends, the exact 5hmC location can, the investigators reported, be determined.

Dr. Pradhan and his colleagues at NEB; the Department of Biochemistry, Emory University School of Medicine, Atlanta; and the New England Biolabs Shanghai R&D Center described use of this technique in a paper published in Cell Reports this month, in which they described high-resolution enzymatic mapping of genomic hydroxymethylcytosine in mouse ES cells.

In the current report, the authors used the enzyme technology for the genome-wide high-resolution hydroxymethylome, describing simple library construction even with a low amount of input DNA (50 ng) and the ability to readily detect 5hmC sites with low occupancy.

As a result of their studies, they propose that

factors affecting the local 5mC accessibility to TET enzymes play important roles in the 5hmC deposition

  • including include chromatin compaction, nucleosome positioning, or TF binding.
  •  the regularly oscillating 5hmC profile around the CTCF-binding sites, suggests 5hmC ‘‘writers’’ may be sensitive to the nucleosomal environment.
  • some transiently stable 5hmCs may indicate a poised epigenetic state or demethylation intermediate, whereas others may suggest a locally accessible chromosomal environment for the TET enzymatic apparatus.

“We were able to do complete mapping in mouse embryonic cells and are pleased about what this enzyme can do and how it works,” Dr. Pradhan said.

And the availability of novel tools that make analysis of the methylome and hypomethylome more accessible will move the field of epigenetic analysis forward and potentially novel biomarkers for cellular development, differentiation, and disease.

Patricia Fitzpatrick Dimond, Ph.D. (pdimond@genengnews.com), is technical editor at Genetic Engineering & Biotechnology News.

Epigenetic Regulation of ADME-Related Genes: Focus on Drug Metabolism and Transport

Published: Sep 23, 2013

Epigenetic regulation of gene expression refers to heritable factors that are functionally relevant genomic modifications but that do not involve changes in DNA sequence.

Examples of such modifications include

  • DNA methylation, histone modifications, noncoding RNAs, and chromatin architecture.

Epigenetic modifications are crucial for

packaging and interpreting the genome, and they have fundamental functions in regulating gene expression and activity under the influence of physiologic and environmental factors.

In this issue of Drug Metabolism and Disposition, a series of articles is presented to demonstrate the role of epigenetic factors in regulating

  • the expression of genes involved in drug absorption, distribution, metabolism, and excretion in organ development, tissue-specific gene expression, sexual dimorphism, and in the adaptive response to xenobiotic exposure, both therapeutic and toxic.

The articles also demonstrate that, in addition to genetic polymorphisms, epigenetics may also contribute to wide inter-individual variations in drug metabolism and transport. Identification of functionally relevant epigenetic biomarkers in human specimens has the potential to improve prediction of drug responses based on patient’s epigenetic profiles.

http://www.technologynetworks.com/Metabolomics/news.aspx?ID=157804

This study is published online in Drug Metabolism and Disposition

Part 8.  Pictorial Maps

 Prediction of intracellular metabolic states from extracellular metabolomic data

MK Aurich, G Paglia, Ottar Rolfsson, S Hrafnsdottir, M Magnusdottir, MM Stefaniak, BØ Palsson, RMT Fleming &

Ines Thiele

Metabolomics Aug 14, 2014;

http://dx.doi.org:/10.1007/s11306-014-0721-3

http://link.springer.com/article/10.1007/s11306-014-0721-3/fulltext.html#Sec1

http://link.springer.com/static-content/images/404/art%253A10.1007%252Fs11306-014-0721-3/MediaObjects/11306_2014_721_Fig1_HTML.gif

Metabolic models can provide a mechanistic framework

  • to analyze information-rich omics data sets, and are
  • increasingly being used to investigate metabolic alternations in human diseases.

An expression of the altered metabolic pathway utilization is the selection of metabolites consumed and released by cells. However, methods for the

  • inference of intracellular metabolic states from extracellular measurements in the context of metabolic models remain underdeveloped compared to methods for other omics data.

Herein, we describe a workflow for such an integrative analysis

  • emphasizing on extracellular metabolomics data.

We demonstrate,

  • using the lymphoblastic leukemia cell lines Molt-4 and CCRF-CEM,

how our methods can reveal differences in cell metabolism. Our models explain metabolite uptake and secretion by predicting

  • a more glycolytic phenotype for the CCRF-CEM model and
  • a more oxidative phenotype for the Molt-4 model,
  • which was supported by our experimental data.

Gene expression analysis revealed altered expression of gene products at

  • key regulatory steps in those central metabolic pathways, and

literature query emphasized the role of these genes in cancer metabolism.

Moreover, in silico gene knock-outs identified unique

  •  control points for each cell line model, e.g., phosphoglycerate dehydrogenase for the Molt-4 model.

Thus, our workflow is well suited to the characterization of cellular metabolic traits based on

  • -extracellular metabolomic data, and it allows the integration of multiple omics data sets
  • into a cohesive picture based on a defined model context.

Keywords Constraint-based modeling _ Metabolomics _ Multi-omics _ Metabolic network _ Transcriptomics

1 Introduction

Modern high-throughput techniques have increased the pace of biological data generation. Also referred to as the ‘‘omics avalanche’’, this wealth of data provides great opportunities for metabolic discovery. Omics data sets

  • contain a snapshot of almost the entire repertoire of mRNA, protein, or metabolites at a given time point or

under a particular set of experimental conditions. Because of the high complexity of the data sets,

  • computational modeling is essential for their integrative analysis.

Currently, such data analysis is a bottleneck in the research process and methods are needed to facilitate the use of these data sets, e.g., through meta-analysis of data available in public databases [e.g., the human protein atlas (Uhlen et al. 2010) or the gene expression omnibus (Barrett et al.  2011)], and to increase the accessibility of valuable information for the biomedical research community.

Constraint-based modeling and analysis (COBRA) is

  • a computational approach that has been successfully used to
  • investigate and engineer microbial metabolism through the prediction of steady-states (Durot et al.2009).

The basis of COBRA is network reconstruction: networks are assembled in a bottom-up fashion based on

  • genomic data and extensive
  • organism-specific information from the literature.

Metabolic reconstructions capture information on the

  • known biochemical transformations taking place in a target organism
  • to generate a biochemical, genetic and genomic knowledge base (Reed et al. 2006).

Once assembled, a

  • metabolic reconstruction can be converted into a mathematical model (Thiele and Palsson 2010), and
  • model properties can be interrogated using a great variety of methods (Schellenberger et al. 2011).

The ability of COBRA models

  • to represent genotype–phenotype and environment–phenotype relationships arises
  • through the imposition of constraints, which
  • limit the system to a subset of possible network states (Lewis et al. 2012).

Currently, COBRA models exist for more than 100 organisms, including humans (Duarte et al. 2007; Thiele et al. 2013).

Since the first human metabolic reconstruction was described [Recon 1 (Duarte et al. 2007)],

  • biomedical applications of COBRA have increased (Bordbar and Palsson 2012).

One way to contextualize networks is to

  • define their system boundaries according to the metabolic states of the system, e.g., disease or dietary regimes.

The consequences of the applied constraints can

  • then be assessed for the entire network (Sahoo and Thiele 2013).

Additionally, omics data sets have frequently been used

  • to generate cell-type or condition-specific metabolic models.

Models exist for specific cell types, such as

  1. enterocytes (Sahoo and Thiele2013),
  2. macrophages (Bordbar et al. 2010),
  3. adipocytes (Mardinoglu et al. 2013),
  4. even multi-cell assemblies that represent the interactions of brain cells (Lewis et al. 2010).

All of these cell type specific models, except the enterocyte reconstruction

  • were generated based on omics data sets.

Cell-type-specific models have been used to study

  • diverse human disease conditions.

For example, an adipocyte model was generated using

  • transcriptomic, proteomic, and metabolomics data.

This model was subsequently used to investigate metabolic alternations in adipocytes

  • that would allow for the stratification of obese patients (Mardinoglu et al. 2013).

The biomedical applications of COBRA have been

  1. cancer metabolism (Jerby and Ruppin, 2012).
  2. predicting drug targets (Folger et al. 2011; Jerby et al. 2012).

A cancer model was generated using

  • multiple gene expression data sets and subsequently used
  • to predict synthetic lethal gene pairs as potential drug targets
  • selective for the cancer model, but non-toxic to the global model (Recon 1),

a consequence of the reduced redundancy in the cancer specific model (Folger et al. 2011).

In a follow up study, lethal synergy between FH and enzymes of the heme metabolic pathway

  • were experimentally validated and resolved the mechanism by which FH deficient cells,
    e.g., in renal-cell cancer cells survive a non-functional TCA cycle (Frezza et al. 2011).

Contextualized models, which contain only the subset of reactions active in a particular tissue (or cell-) type,

  • can be generated in different ways (Becker and Palsson, 2008; Jerby et al. 2010).

However, the existing algorithms mainly consider

  • gene expression and proteomic data
  • to define the reaction sets that comprise the contextualized metabolic models.

These subset of reactions are usually defined

  • based on the expression or absence of expression of the genes or proteins (present and absent calls),
  • or inferred from expression values or differential gene expression.

Comprehensive reviews of the methods are available (Blazier and Papin, 2012; Hyduke et al. 2013). Only the compilation of a large set of omics data sets

  • can result in a tissue (or cell-type) specific metabolic model, whereas

the representation of one particular experimental condition is achieved

  • through the integration of omics data set generated from one experiment only (condition-specific cell line model).

Recently, metabolomic data sets have become more comprehensive and

  • using these data sets allow direct determination of the metabolic network components (the metabolites).

Additionally, metabolomics has proven to be stable, relatively inexpensive, and highly reproducible (Antonucci et al. 2012). These factors make metabolomic data sets particularly valuable for

  • interrogation of metabolic phenotypes.

Thus, the integration of these data sets is now an active field of research (Li et al. 2013; Mo et al. 2009; Paglia et al. 2012b; Schmidt et al. 2013).

Generally, metabolomic data can be incorporated into metabolic networks as

  • qualitative, quantitative, and thermodynamic constraints (Fleming et al. 2009; Mo et al. 2009).

Mo et al. used metabolites detected in the

  • spent medium of yeast cells to determine intracellular flux states through a sampling analysis (Mo et al. 2009),
  • which allowed unbiased interrogation of the possible network states (Schellenberger and Palsson 2009) and
  • prediction of internal pathway use.
Modes of transcriptional regulation during the YMC

Modes of transcriptional regulation during the YMC

Such analyses have also been used to reveal the effects of

  1. enzymopathies on red blood cells (Price et al. 2004),
  2. to study effects of diet on diabetes (Thiele et al. 2005) and
  3. to define macrophage metabolic states (Bordbar et al. 2010).

This type of analysis is available as a function in the COBRA toolbox (Schellenberger et al. 2011).

In this study, we established a workflow

  • for the generation and analysis of condition-specific metabolic cell line models
  • that can facilitate the interpretation of metabolomic data.

Our modeling yields meaningful predictions regarding

  • metabolic differences between two lymphoblastic leukemia cell lines (Fig. 1A).

Fig. 1

metabol leukem cell lines11306_2014_721_Fig1_HTML

metabol leukem cell lines11306_2014_721_Fig1_HTML

A Combined experimental and computational pipeline to study human metabolism.

  1. Experimental work and omics data analysis steps precede computational modeling.
  2. Model predictions are validated based on targeted experimental data.
  3. Metabolomic and transcriptomic data are used for model refinement and submodel extraction.
  4. Functional analysis methods are used to characterize the metabolism of the cell-line models and compare it to additional experimental data.
  5. The validated models are subsequently used for the prediction of drug targets.

B Uptake and secretion pattern of model metabolites. All metabolite uptakes and secretions that were mapped during model generation are shown.

  • Metabolite uptakes are depicted on the left, and
  • secreted metabolites are shown on the right.
  1. A number of metabolite exchanges mapped to the model were unique to one cell line.
  2. Differences between cell lines were used to set quantitative constraints for the sampling analysis.

C Statistics about the cell line-specific network generation.

D Quantitative constraints.

For the sampling analysis, an additional set of constraints was imposed on the cell line specific models,

  • emphasizing the differences in metabolite uptake and secretion between cell lines.

Higher uptake of a metabolite was allowed

  • in the model of the cell line that consumed more of the metabolite in vitro, whereas
  • the supply was restricted for the model with lower in vitro uptake.

This was done by establishing the same ratio between the models bounds as detected in vitro.

X denotes the factor (slope ratio) that distinguishes the bounds, and

  • which was individual for each metabolite.

(a) The uptake of a metabolite could be x times higher in CCRF-CEM cells,

(b) the metabolite uptake could be x times higher in Molt-4,

(c) metabolite secretion could be x times higher in CCRF-CEM, or

(d) metabolite secretion could be x times higher in Molt-4 cells.LOD limit of detection.

The consequence of the adjustment was, in case of uptake, that one model was constrained to a lower metabolite uptake (A, B), and the difference depended on the ratio detected in vitro. In case of secretion, one model

  • had to secrete more of the metabolite, and again
  • the difference depended on the experimental difference detected between the cell lines

2 Results

We set up a pipeline that could be used to infer intracellular metabolic states

  • from semi-quantitative data regarding metabolites exchanged between cells and their environment.

Our pipeline combined the following four steps:

  1. data acquisition,
  2. data analysis,
  3. metabolic modeling and
  4. experimental validation of the model predictions (Fig. 1A).

We demonstrated the pipeline and the predictive potential to predict metabolic alternations in diseases such as cancer based on

^two lymphoblastic leukemia cell lines.

The resulting Molt-4 and CCRF-CEM condition-specific cell line models could explain

^  metabolite uptake and secretion
^  by predicting the distinct utilization of central metabolic pathways by the two cell lines.
^  the CCRF-CEM model resembled more a glycolytic, commonly referred to as ‘Warburg’ phenotype,
^  our model predicted a more respiratory phenotype for the Molt-4 model.

We found these predictions to be in agreement with measured gene expression differences

  • at key regulatory steps in the central metabolic pathways, and they were also
  • consistent with additional experimental data regarding the energy and redox states of the cells.

After a brief discussion of the data generation and analysis steps, the results derived from model generation and analysis will be described in detail.

2.1 Pipeline for generation of condition-specific metabolic cell line models

integration of exometabolomic (EM) data

integration of exometabolomic (EM) data

2.1.1 Generation of experimental data

We monitored the growth and viability of lymphoblastic leukemia cell lines in serum-free medium (File S2, Fig. S1). Multiple omics data sets were derived from these cells.Extracellular metabolomics (exo-metabolomic) data,

integration of exometabolomic (EM) data

integration of exometabolomic (EM) data

^  comprising measurements of the metabolites in the spent medium of the cell cultures (Paglia et al. 2012a),
^ were collected along with transcriptomic data, and these data sets were used to construct the models.

2.1.4 Condition-specific models for CCRF-CEM and Molt-4 cells

To determine whether we had obtained two distinct models, we evaluated the reactions, metabolites, and genes of the two models. Both the Molt-4 and CCRF-CEM models contained approximately half of the reactions and metabolites present in the global model (Fig. 1C). They were very similar to each other in terms of their reactions, metabolites, and genes (File S1, Table S5A–C).

(1) The Molt-4 model contained seven reactions that were not present in the CCRF-CEM model (Co-A biosynthesis pathway and exchange reactions).
(2) The CCRF-CEM contained 31 unique reactions (arginine and proline metabolism, vitamin B6 metabolism, fatty acid activation, transport, and exchange reactions).
(3) There were 2 and 15 unique metabolites in the Molt-4 and CCRF-CEM models, respectively (File S1, Table S5B).
(4) Approximately three quarters of the global model genes remained in the condition-specific cell line models (Fig. 1C).
(5) The Molt-4 model contained 15 unique genes, and the CCRF-CEM model had 4 unique genes (File S1, Table S5C).
(6) Both models lacked NADH dehydrogenase (complex I of the electron transport chain—ETC), which was determined by the absence of expression of a mandatory subunit (NDUFB3, Entrez gene ID 4709).

Rather, the ETC was fueled by FADH2 originating from succinate dehydrogenase and from fatty acid oxidation, which through flavoprotein electron transfer

FADH2

FADH2

  • could contribute to the same ubiquinone pool as complex I and complex II (succinate dehydrogenase).

Despite their different in vitro growth rates (which differed by 11 %, see File S2, Fig. S1) and
^^^ differences in exo-metabolomic data (Fig. 1B) and transcriptomic data,
^^^ the internal networks were largely conserved in the two condition-specific cell line models.

2.1.5 Condition-specific cell line models predict distinct metabolic strategies

Despite the overall similarity of the metabolic models, differences in their cellular uptake and secretion patterns suggested distinct metabolic states in the two cell lines (Fig. 1B and see “Materials and methods” section for more detail). To interrogate the metabolic differences, we sampled the solution space of each model using an Artificial Centering Hit-and-Run (ACHR) sampler (Thiele et al. 2005). For this analysis, additional constraints were applied, emphasizing the quantitative differences in commonly uptaken and secreted metabolites. The maximum possible uptake and maximum possible secretion flux rates were reduced
^^^ according to the measured relative differences between the cell lines (Fig. 1D, see “Materials and methods” section).

We plotted the number of sample points containing a particular flux rate for each reaction. The resulting binned histograms can be understood as representing the probability that a particular reaction can have a certain flux value.

A comparison of the sample points obtained for the Molt-4 and CCRF-CEM models revealed

  • a considerable shift in the distributions, suggesting a higher utilization of glycolysis by the CCRF-CEM model
    (File S2, Fig. S2).

This result was further supported by differences in medians calculated from sampling points (File S1, Table S6).
The shift persisted throughout all reactions of the pathway and was induced by the higher glucose uptake (34 %) from the extracellular medium in CCRF-CEM cells.

The sampling median for glucose uptake was 34 % higher in the CCRF-CEM model than in Molt-4 model (File S2, Fig. S2).

The usage of the TCA cycle was also distinct in the two condition-specific cell-line models (Fig. 2). Interestingly,
the models used succinate dehydrogenase differently (Figs. 2, 3).

TCA_reactions

TCA_reactions

The Molt-4 model utilized an associated reaction to generate FADH2, whereas

  • in the CCRF-CEM model, the histogram was shifted in the opposite direction,
  • toward the generation of succinate.

Additionally, there was a higher efflux of citrate toward amino acid and lipid metabolism in the CCRF-CEM model (Fig. 2). There was higher flux through anaplerotic and cataplerotic reactions in the CCRF-CEM model than in the Molt-4 model (Fig. 2); these reactions include

(1) the efflux of citrate through ATP-citrate lyase,
(2) uptake of glutamine,
(3) generation of glutamate from glutamine,
(4) transamination of pyruvate and glutamate to alanine and to 2-oxoglutarate,
(5) secretion of nitrogen, and
(6) secretion of alanine.

energetics-of-cellular-respiration

energetics-of-cellular-respiration

The Molt-4 model showed higher utilization of oxidative phosphorylation (Fig. 3), again supported by
elevated median flux through ATP synthase (36 %) and other enzymes, which contributed to higher oxidative metabolism. The sampling analysis therefore revealed different usage of central metabolic pathways by the condition-specific models.

Fig. 2

Differences in the use of  the TCA cycle by the CCRF-CEM model (red) and the Molt-4 model (blue).

Differences in the use of the TCA cycle by the CCRF-CEM model (red) and the Molt-4 model (blue).

Differences in the use of the TCA cycle by the CCRF-CEM model (red) and the Molt-4 model (blue).

The table provides the median values of the sampling results. Negative values in histograms and in the table describe reversible reactions with flux in the reverse direction. There are multiple reversible reactions for the transformation of isocitrate and α-ketoglutarate, malate and fumarate, and succinyl-CoA and succinate. These reactions are unbounded, and therefore histograms are not shown. The details of participating cofactors have been removed.

Figure 3.

Molt-4 has higher median flux through ETC reactions II–IV 11306_2014_721_Fig3_HTML

Molt-4 has higher median flux through ETC reactions II–IV 11306_2014_721_Fig3_HTML

Atp ATP, cit citrate, adp ADP, pi phosphate, oaa oxaloacetate, accoa acetyl-CoA, coa coenzyme-A, icit isocitrate, αkg α-ketoglutarate, succ-coa succinyl-CoA, succ succinate, fumfumarate, mal malate, oxa oxaloacetate,
pyr pyruvate, lac lactate, ala alanine, gln glutamine, ETC electron transport chain

Ingenuity network analysis showing up (red) and downregulation (green) of miRNAs involved in PC and their target genes

Ingenuity network analysis showing up (red) and downregulation (green) of miRNAs involved in PC and their target genes

metabolic pathways 1476-4598-10-70-1

metabolic pathways 1476-4598-10-70-1

Metabolic Systems Research Team fig2

Metabolic Systems Research Team fig2

Metabolic control analysis of respiration in human cancer tissue. fphys-04-00151-g001

Metabolic control analysis of respiration in human cancer tissue. fphys-04-00151-g001

Metabolome Informatics Research fig1

Metabolome Informatics Research fig1

Modelling of Central Metabolism network3

Modelling of Central Metabolism network3

N. gaditana metabolic pathway map ncomms1688-f4

N. gaditana metabolic pathway map ncomms1688-f4

protein changes in biological mechanisms

protein changes in biological mechanisms

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Development Of Super-Resolved Fluorescence Microscopy

 

Author and Curator: Larry H. Bernstein, MD, FCAP

CSO, Leaders in Pharmaceutical Business Intelligence

Article ID #153: Development Of Super-Resolved Fluorescence Microscopy. Published on 10/12/2014

WordCloud Image Produced by Adam Tubman

Development Of Super-Resolved Fluorescence Microscopy

 

Part I. Nobel Prize For Chemistry 2014: Eric Betzig, Stefan W. Hell
and William E. Moerner Honored For Development Of Super-
Resolved Fluorescence Microscopy

The 2014 Nobel Prize in Chemistry was awarded on 10/08/2014 to
Eric Betzig, Stefan W. Hell and William E. Moerner for
“the development of super-resolved fluorescence microscopy.”

The invention of the electron microscope by Max Knoll and Ernst Ruska at the
Berlin Technische Hochschule in 1931 finally overcame the barrier to higher
resolution that had been imposed by the limitations of visible light. Since then
resolution has defined the progress of the technology.

The ultimate goal was atomic resolution – the ability to see atoms – but this would
have to be approached incrementally over the course of decades. The earliest microscopes merely proved the concept: electron beams could, indeed, be tamed
to provide visible images of matter. By the late 1930s electron microscopes with theoretical resolutions of 10 nm were being designed and produced, and by 1944
this was further reduced to 2 nm. (The theoretical resolution of a an optical light microscope is 200 nm.)

Increases in the accelerating voltage of the electron beam accounted for much of
the improvement in resolution. But voltage was not everything. Improvements in electron lens technology minimized aberrations and provided a clearer picture,
which also contributed to improved resolution, as did better vacuum systems and brighter electron guns. So increasing the resolution of electron microscopes was a main driving force throughout the instrument’s development.

With nanoscopy, scientists could observe viruses, proteins and molecules there
are smaller than 0.0000002 metres.

Three researchers won the 2014 Nobel Prize in Chemistry on Wednesday,
October 8, for giving microscopes much sharper vision than was thought possible, letting scientists peer into living cells with unprecedented detail to seek the roots
of disease.  It was awarded to U.S. researchers Eric Betzig and William Moerner
and German scientist Stefan Hell. They found ways to use molecules that glow on demand to overcome what was considered a fundamental limitation for optical microscopes.

Hell, 52, of Germany, is the director at the Max Planck Institute for Biophysical Chemistry and the division head at the German Cancer Research Center in
Heidelberg. He was honored for his work on fluorescence microscopy, a kind
of nano-flashlight where scientists use fluorescent molecules to see parts of a
cell. Later in his career, he developed the STED microscope, which collects light
from “a multitude of small volumes to create a whole.”

Moerner, a 61-year-old professor in chemistry and applied physics at Stanford University in California, is the recipient of the 2008 Wolf Prize in Chemistry, the
2009 Irving Langmuir Award and the 2013 Peter Debye Award. In 1989, he
was the first scientist to be able to measure the light absorption of a single molecule.
This inspired many chemists to begin focusing on single molecules, including Betzig.

Betzig, 54, the group leader at Janelia Farm Research campus at the Howard
Hughes Medical Institute in Virginia, developed new optical imaging tools for
biology. His work involved taking images of the same area multiple times, and illuminating just a few molecules each time. These images were then
superimposed to create a dense super image at the nano level,

The limitation of optical microscopy was thought to have been determined in a calculation published in 1873 that defined the limit of how tiny a detail could be revealed by optical microscopes. Based on experimental evidence and basic principles of physics, Ernst Abbe and Lord Rayleigh defined and formulated
this diffraction-limited resolution in the late 19th century (Abbe, 1873; Rayleigh,
1896
).  However, only cellular structure and objects that were at least 200 to
350 nm apart could be resolved by light microscopy because, the optical resolution
of light microscopy was limited to approximately half of the wavelength of the light used.  Later key innovations—including fluorescence and confocal laser scanning microscopy (CLSM)—made optical microscopy one of the most powerful and
versatile diagnostic tools in modern cell biology. Using highly specific fluorescent labeling techniques such as immunocytochemistry, in situ hybridization, or
fluorescent protein tags, the spatial distribution and dynamics of virtually every subcellular structure, protein, or genomic sequence of interest can be analyzed in chemically fixed or living samples (Conchello and Lichtman, 2005; Giepmans et al., 2006).

The result of their advance is “really a window into the cell which we didn’t have before,” said Catherine Lewis, director of the cell biology and biophysics division
of the National Institute of General Medical Sciences in Bethesda, Maryland.

“You can observe the behavior of individual molecules in living cells in real time.
You can see … molecules moving around inside the cell. You can see them interacting with each other.”

The research of the three men has let scientists study diseases such as
Parkinson’s, Alzheimer’s and Huntington’s at a molecular level, the Royal
Swedish Academy of Sciences said.

Part II. Electron microscopy limitations

Manfred Von Ardenne in Berlin produced the earliest scanning-transmission
electron microscope in 1937. At the University of Toronto in Canada, Cecil Hall, James Hillier, and Albert Prebus, working under the direction of Eli Burton,
produced an advanced 1938 Toronto Model electron microscope that would
later become the basis for Radio Corporation of America’s Model B, the first commercial electron microscope in North America. Ruska at Siemens in
Germany produced the first commercial electron microscope in the world in 938.

Starting in 1939, scientists in Japan gathered to decide on the best way to build
an electron microscope. This group evolved into the Japan Electron Optics Laboratory (JEOL) that would eventually produce more models and varieties
of electron microscopes than any other company. Hitachi and Toshiba in Japan
also played a major role in the early development process.

The 1960s through the 1990s produced many innovative instruments and trends.
The introduction of the first commercial scanning electron microscopes (SEMs)
in 1965 opened up a new world of analysis for materials scientists. Ultrahigh
voltage TEM instruments (up to 3 MeV at CEMES-LOE/CNRS in Toulouse,
France, and at Hitachi in Tokyo, Japan), in the 1960s and 1970s gave electrons higher energy to penetrate more deeply into thick samples. The evolution and incorporation of other detectors (electron microprobes, electron energy loss spectroscopy (EELS), etc.) made the SEM into a true analytical electron
microscope (AEM) beginning in the 1970s. The development of brighter
electron sources, such as the lanthanum hexaboride filament (LAB6) and the
field emission gun in the 1960s, and their commercialization in the 1970s
brought researchers a brighter source of electrons and with it better imaging
and resolution. Tilting specimen stages permitting examination of the specimen
from different angles aided significantly in the determination of crystal structure.
In the late 1980s and throughout the 1990s, the environmental electron
microscopes that allow scientists to examine samples under more natural
conditions of temperature and pressure have dramatically expanded the
types of samples that can be examined.

In medicine, the EM made a unique contribution to diagnostic anatomic
pathology in renal biopsy analysis. However, the small sample had to be
embedded, and in the early days one cut the specimen by breaking glass
for the cutting of the specimen. But even though EM ushered in a new era of molecular pathology, the contribution was limited, despite incremental
improvements.

In the past, the use of microscopes was limited by a physical restriction;
scientists could only see items that were larger than roughly half the
wavelength of light (.2 micrometers)
. However, the groundbreaking work
of the Nobel laureates bypassed the maximum resolution of traditional
microscopes and launched optical microscopy into the nanodimension.

Part III. Super resolution fluorescence microscopy

Bo Huang,1,2 Mark Bates,3 and Xiaowei Zhuang1,2,4
Author information ► Copyright and License information ►
Annu Rev Biochem. 2009; 78: 993–1016.
http://dx.doi.org:/10.1146/annurev.biochem.77.061906.092014
PMCID: PMC2835776  NIHMSID: NIHMS179491

Achieving a spatial resolution that is not limited by the diffraction of
light, recent developments of super-resolution fluorescence microscopy
techniques allow the observation of many biological structures not
resolvable in conventional fluorescence microscopy. New advances
in these techniques now give them the ability to image three-dimensional
(3D) structures, measure interactions by multicolor colocalization, and
record dynamic processes in living cells at the nanometer scale. It is
anticipated that super-resolution fluorescence microscopy will become
a widely used tool for cell and tissue imaging to provide previously
unobserved details of biological structures and processes.

Keywords: Sub-diffraction limit, single-molecule, multicolor imaging,
three-dimensional imaging, live cell imaging, single-particle tracking,
photoswitchable probe

Among the various microscopy techniques, fluorescence microscopy is
one of the most widely used because of its two principal advantages:
Specific cellular components may be observed through molecule-specific
labeling, and light microscopy allows the observation of structures inside
a live sample in real time. Compared to other imaging techniques such
as electron microscopy (EM), however, conventional fluorescence
microscopy is limited by relatively low spatial resolution because of the
diffraction of light. This diffraction limit, about 200–300 nm in the lateral
direction and 500–700 nm in the axial direction, is comparable to or larger
than many subcellular structures, leaving them too small to be observed in
detail. In recent years, a number of “super-resolution” fluorescence microscopy techniques have been invented to overcome the diffraction barrier, including techniques that employ nonlinear effects to sharpen the point-spread function
of the microscope, such as stimulated emission depletion (STED) microscopy
(1, 2), related methods using other reversible saturable optically linear
fluorescence transitions (RESOLFTs) (3), and saturated structured-illumination microscopy (SSIM) (4), as well as techniques that are based on the localization
of individual fluorescent molecules, such as stochastic optical reconstruction microscopy (STORM) (5), photoactivated localization microscopy (PALM) (6),
and fluorescence photoactivation localization microscopy (FPALM) (7). These methods have yielded an order of magnitude improvement in spatial resolution
in all three dimensions over conventional light microscopy.

THE RESOLUTION LIMIT IN OPTICAL MICROSCOPY

Microscopes can be used to visualize fine structures in a sample by providing
a magnified image. However, even an arbitrarily high magnification does not
translate into the ability to see infinitely small details. Instead, the resolution
of light microscopy is limited because light is a wave and is subject to diffraction.

The diffraction limit

An optical microscope can be thought of as a lens system that produces a
magnified image of a small object. In this imaging process, light rays from
each point on the object converge to a single point at the image plane. However,
the diffraction of light prevents exact convergence of the rays, causing a sharp
point on the object to blur into a finite-sized spot in the image. The three-
dimensional (3D) intensity distribution of the image of a point object is called
the point spread function (PSF). The size of the PSF determines the resolution
of the microscope: Two points closer than the full width at half-maximum
(FWHM) of the PSF will be difficult to resolve because their images overlap substantially.

The FWHM of the PSF in the lateral directions (the x–y directions perpendicular
to the optical axis) can be approximated as Δxy ≈ 0.61λ / NA, where λ is the wavelength of the light, and NA is the numerical aperture of the objective
defined as NA = n sinα, with n being the refractive index of the medium and
α being the half-cone angle of the focused light produced by the objective.
The axial width of the PSF is about 2–3 times as large as the lateral width
for ordinary high NA objectives. When imaging with visible light (λ ≈ 550 nm),
the commonly used oil immersion objective with NA = 1.40 yields a PSF with
a lateral size of ~200 nm and an axial size of ~500 nm in a refractive index-
matched medium (Figure 1) (8).

Figure 1

The PSF of a common oil immersion objective with NA = 1.40, showing the
focal spot of 550 nm light in a medium with refractive index n = 1.515. The
intensity distribution in the x-z plane of the focus spot is computed numerically.

PFS of oil immersion microscope

PFS of oil immersion microscope

Because the loss of high-frequency spatial information in optical microscopy
results from the diffraction of light when it propagates through a distance larger
than the wavelength of the light (far field), near-field microscopy is one of the
earliest approaches sought to achieve high spatial resolution. By exciting the fluorophores or detecting the signal through the nonpropagating light near the fluorophore, high-resolution information be retained. Near-field scanning optical microscopy (NSOM) acquires an image by scanning a sharp probe tip across
the sample, typically providing a resolution of 20–50 nm (911). Wide-field
imaging has also been recently demonstrated in the near-field regime using
a super lens with negative refractive index (12, 13). However, the short range
of the near-field region (tens of nanometers) compromises the ability of light microscopy to look into a sample, limiting the application of near-field microscopy
to near-surface features only. This limit highlights the need to develop far-field
high-resolution imaging methods.

Among far-field fluorescence microscopy techniques, confocal and multiphoton microscopy are among the most widely used to moderately enhance the spatial resolution (14, 15). By combining a focused laser for excitation and a pinhole for detection, confocal microscopy can, in principle, have a factor of √2 improvement
in the spatial resolution. In multiphoton microscopy, nonlinear absorption processes reduce the effective size of the excitation PSF. However, this gain in the PSF size
is counteracted by the increased wavelength of the excitation light. Thus, instead
of improving the resolution, the main advantage of confocal and multi-photon microscopy over wide-field microscopy is the reduction of out-of-focus fluorescence background, allowing optical sectioning in 3D imaging.

Two techniques, 4Pi and I5M microscopy, approach this ideal situation by using
two opposing objectives for excitation and/or detection (16, 17). By acquiring
multiple images with illumination patterns of different phases and orientations,
a high-resolution image can be reconstructed. Because the illumination pattern
itself is also limited by the diffraction of light, structured illumination microscopy
(SIM) is only capable of doubling the spatial resolution by combining two diffraction-limited sources of information.  The best achievable result using these methods
would be an isotropic PSF with an additional factor of 2 in resolution improvement. This would correspond to ~100-nm image resolution in all three dimensions, as
has been demonstrated by the I5S technique, which combines I5M and SIM (22). Albeit a significant improvement, this resolution is still fundamentally limited by
the diffraction of light.

SUPER RESOLUTION FLUORESCENCE MICROSCOPY BY SPATIALLY PATTERNED EXCITATION

One approach to attain a resolution far beyond the limit of diffraction, i.e., to
realize super-resolution microscopy, is to introduce sub-diffraction-limit features
in the excitation pattern so that small-length-scale information can be read out.
We refer to this approach, including STED, RESOLFT, and SSIM, as super-
resolution microscopy by spatially patterned excitation or the “patterned excitation” approach.

The concept of STED microscopy was first proposed in 1994 (1) and subsequently demonstrated experimentally (2). Simply speaking, it uses a second laser (STED laser) to suppress the fluorescence emission from the fluorophores located off the center of the excitation. This suppression is achieved through stimulated emission: When an excited-state fluorophores encounters a photon that matches the energy difference between the excited and the ground state, it can be brought back to
the ground state through stimulated emission before spontaneous fluorescence emission occurs. This process effectively depletes excited-state fluorophores
capable of fluorescence emission (Figure 2a,b).

Figure 2

The principle of STED microscopy. (a) The process of stimulated emission. A
ground state (S0) fluorophore can absorb a photon from the excitation light and
jump to the excited state (S1).

STED microsopy

STED microsopy

The pattern of the STED laser is typically generated by inserting a phase mask
into the light path to modulate its phase-spatial distribution (Figure 2b). One such phase mask generates a donut-shaped STED pattern in the xy plane (Figure 2c)
and has provided an xy resolution of ~30 nm (24). STED can also be employed
in 4Pi microscopy (STED-4Pi), resulting in an axial resolution of 30–40 nm (25). STED has been applied to biological samples either immuno-stained with
fluorophore labeled antibodies (26) or genetically tagged with fluorescent
proteins (FPs) (27). Dyes with high photostability under STED conditions and
large stimulated emission cross sections in the visible to near infrared (IR) range
are preferred. Atto 532 and Atto 647N are among the most often used dyes for
STED microscopy.

Stimulated emission is not the only mechanism capable of suppressing
undesired fluorescence emission. A more general scheme using saturable
depletion to achieve super resolution has been formalized with the name
RESOLFT microscopy (3). This scheme employs fluorescent probes that
can be reversibly photoswitched between a fluorescent on state and a dark
off state. The off state can be the ground state of a fluorophores as in the
case of STED, the triplet state as in ground-state-depletion microscopy
(28, 29), or the dark state of a reversibly photoswitchable fluorophore (30).  RESOLFT has been demonstrated using a reversibly photoswitchable
fluorescent protein as FP595 which leads to a resolution better than 100 nm
at a depletion laser intensity of 600 W/cm2(30).

The same concept of employing saturable processes can also be applied
to SIM by introducing sub-diffraction-limit spatial features into the excitation
pattern. SSIM has been demonstrated using the saturation of fluorescence
emission, which occurs when a fluorophore is illuminated by a very high
intensity of excitation light (4). Under this strong excitation, it is immediately
pumped to the excited state each time it returns to the ground state. In SSIM,
where the sample is illuminated with a sinusoidal pattern of strong excitation
light, the peaks of the excitation pattern can be clipped by fluorescence
saturation and become flat, whereas fluorescence emission is still absent
from the zero points in the valleys (Figure 3a). These effects add higher order
spatial frequencies to the excitation pattern. Mixing this excitation pattern with
the high-frequency spatial features in the sample can effectively bring the sub-diffraction-limit spatial features into the detection range of the microscopy
(Figure 3b).

Figure 3

The principle of SSIM. (a) The generation of the illumination pattern. A
diffractive grating in the excitation path splits the light into two beams. Their interference after emerging from the objective and reaching the sample creates
a sinusoidal illumination

SSIM

SSIM

Although the image of a single fluorophore, which resembles the PSF, is a
finite-sized spot, the precision of determining the fluorophores position from
its image can be much higher than the diffraction limit, as long as the image
results from multiple photons emitted from the fluorophore. Fitting an image
consisting of N photons can be viewed as N measurements of the fluorophore position, each with an uncertainty determined by the PSF (8), thus leading to
a localization precision approximated by:

Δloc≈ΔN−−√

where Δloc is the localization precision and Δ is the size of the PSF. This
scaling of the localization precision with the photon number allows super-
resolution microscopy with a resolution not limited by the diffraction of light.

High-precision localization of bright light has reached a precision as high
as ~1 Å (33). Taking advantage of single-molecule detection and imaging
(34, 35), nanometer localization precision has been achieved for single
fluorescent molecules (36).

Using fluorescent probes that can switch between a fluorescent and a dark
state, a recent invention overcomes this barrier by separating in the time
domain the otherwise spatially overlapping fluorescent images. In this approach, molecules within a diffraction limited region can be activated at different time
points so that they can be individually imaged, localized, and subsequently deactivated (Figure 4). Massively parallel localization is achieved through
wide-field imaging, so that the coordinates of many fluorophores can be
mapped and a super-resolution images subsequently reconstructed. This
concept has been independently conceived and implemented by three labs,
and it was given the names STORM (5), PALM (6), and FPALM (7), respectively.

Iterating the activation and imaging process allows the locations of many
fluorophores to be mapped and a super-resolution image to be constructed
from these fluorophore locations. In the following, we refer to this approach
as super-resolution microscopy by single-molecule localization.

Figure 4

The principle of stochastic optical reconstruction microscopy (STORM), photoactivated localization microscopy (PALM), and fluorescence photo-
activation localization microscopy (FPALM). Different fluorescent probes
marking the sample structure are activated.

STORM

STORM

After capturing the images with a digital camera, the point-spread functions
of the individual molecules are localized with high precision based on the
photon output before the probes spontaneously photo-bleach or switch to
a dark state. The positions of localized molecular centers are indicated with
black crosses. The process is repeated in Figures (c) through (e) until all of
the fluorescent probes are exhausted due to photo-bleaching or because the background fluorescence becomes too high. The final super-resolution image
(Figure (f)) is constructed by plotting the measured positions of the fluorescent probes.
http://microscopyu.com/tutorials/flash/superresolution/storm/index.html

The resolution of this technique is limited by the number of photons detected
per photoactivation event, which varies from several hundred for FPs (6) to
several thousand for cyanine dyes such as Cy5 (5, 46). These numbers
theoretically allow more than an order of magnitude improvement in spatial
resolution according to the √N scaling rule. In practice, a lateral resolution
of ~20 nm has been established experimentally using the photoswitchable
cyanine dyes (5, 46). Super-resolution images of biological samples have
been reported with directly labeled DNA structures and immunostained DNA-
protein complexes in vitro (5) as well as with FPtagged or immunostained
cellular structures (6, 44, 46).

Table 1   Photoswitchable fluorophores used in super resolution
fluorescence microscopy

Photoswitchable fluorophores

Photoswitchable fluorophores

Recent advances in super-resolution fluorescence microscopy
(including the capability for 3D, multicolor, live-cell imaging) enable
new applications in biological samples. These technical advances
were made possible through the development of both imaging optics
and fluorescent probes.

  • 3D imaging using the single-molecule localization approach
  • 3D imaging using the patterned excitation approach
  • Multicolor imaging
  • Multicolor imaging using the patterned excitation approach
  • Multicolor imaging using the single-molecule localization approach
  • Live cell imaging

Fluorescence imaging of a live cell has two requirements: specific labeling
of the cell and a time resolution that is high enough to record relevant
dynamics in the cell.  Many fluorescent proteins and organic dyes, including
cyanine dyes (46) and caged dyes, have been shown switchable in live cells.

Because STED has a much smaller PSF than scanning confocal microscopy,
STED would inherently take more time to scan though the same size of image
field. By increasing the scanning speed and limiting the field of view to a few µm, Westphal and coworkers have observed Brownian motion of a dense suspension
of nanoparticles with an impressive rate of 80 frames per second (fps) using
STED microscopy (63). More recently, they have demonstrated video-rate
(28 fps) imaging of live hippocampal neurons and observed the movement of individual synaptic vesicles with 60–80-nm resolution (64).

Sub-diffraction-limit imaging of focal adhesion proteins in live cells has recently
been demonstrated (65). Photoswitchable fluorescent protein, EosFP, was used
to label the focal adhesion protein paxillin. A time resolution of ~25–60 seconds
per frame was obtained, and during this time interval, approximately 103
fluorophores were activated and localized per square micrometer, providing
an effective resolution of 60–70 nm by the Nyquist criterion (65). More recently, super-resolution imaging has also been demonstrated in live bacteria with photoswitchable enhanced yellow fluorescent protein (EYFP), allowing the
MreB structure in the cell to be traced (66).

The optical resolution

Optical resolution is the intrinsic ability of a given method to resolve a structure
and can be defined as the ability to distinguish two point sources in proximity.
For the patterned excitation approaches, such as STED, SSIM, and RESOLFT,
the optical resolution is represented by the size of the effective PSF. For the
single-molecule localization approach, such as STORM/PALM/FPALM, the
precision of determining the positions of individual fluorescent probes is the
principal measure of optical resolution.

By using a spatially patterned excitation profile, this approach achieves super resolution by generating an effective excitation volume with dimensions far
below the diffraction limit. Taking STED as an example, the sharpness of the
PSF results from the saturation of depletion of excited-state fluorophores in
the region neighboring the zero point of the STED laser (which coincide with
the focal point of the excitation laser). With an increasing STED laser power,
the saturated region expands toward the zero point, but fluorophores at the
zero point are not affected by the STED laser if the zero point is strictly kept
at zero intensity. Therefore, a theoretically unlimited gain in spatial resolution
may be achieved if the zero point in the depletion pattern is ideal.

The single-molecule localization approach achieves super resolution through
high precision localization of individual fluorophores. The number of photons
collected from a fluorophore is a principal factor limiting the localization
precision and hence the resolution of the final image.

Several photoswitchable fluorophores have been reported to give thousands
of photons detected per activation event [e.g., 6000 from Cy5 (46)].With the
PSF fitting procedure and the mechanical stability of the system optimized,
the background signal suppressed, and the nonuniformity of camera pixels
corrected, optical resolution of just a few nanometers could potentially be
achieved, reaching the molecular scale. As in the case of the patterned
excitation approach, the optical resolution here is also unlimited, in principle,
given a sufficient number of photons detected from the fluorescent probes.

Part III. A guide to super-resolution fluorescence microscopy

L Schermelleh1R Heintzmann2,3,4, and H Leonhardt1
JCB Jul 19, 2010 // 190(2): 165-175
The Rockefeller University Press,
http://dx.doi.org:/10.1083/jcb.201002018

Based on experimental evidence and basic principles of physics, Ernst Abbe
and Lord Rayleigh defined and formulated this diffraction-limited resolution in
the late 19th century (Abbe, 1873Rayleigh, 1896). Later key innovations—including fluorescence and confocal laser scanning microscopy (CLSM)—made optical microscopy one of the most powerful and versatile diagnostic
tools in modern cell biology.

The optical resolution defines the physical limit of the smallest structure it
can resolve. When imaging a biological sample, the effective resolution is
also affected by several sample-specific factors, including the labeling density,
probe size, and how well the ultrastructures are preserved during sample
preparation.

The diffraction (Abbe) limit of detection

Resolution is often defined as the largest distance at which the image of
two point-like objects seems to amalgamate. Thus, most resolution criteria
(Rayleigh limit,Sparrow limit, full width at half maximum of the PSF) directly
relate to properties of the PSF. These are useful resolution criteria for visible
observation of specimen, but there are several shortcomings of such a definition
of resolution: (1) Knowing that the image is an image of two particles, these
can in fact be discriminated with the help of a computer down to arbitrary
smaller distances. Determining the positions of two adjacent particles thus
becomes a question of experimental precision and most notably photon statistics
rather than being described by the Rayleigh limit. (2) These limits do not
necessarily correspond well to what level of detail can be seen in images or
real world objects; e.g., the Rayleigh limit is defined as the distance from the
center to the first minimum of the point spread function, which can be made
arbitrarily small with the help of ordinary linear optics (e.g., Toraldo-filters),
albeit at the expense of the side lobes becoming much higher than the central
maximum. (3)

Abbe’s formulation of a resolution limit avoids all of the above shortcomings
at the expense of a less direct interpretation. The process of imaging can be
described by a convolution operation. With the help of a Fourier transformation,
every object (whether periodic or not) can uniquely be described as a sum of
sinusoidal curves with different spatial frequencies (where higher frequencies
represent fine object details and lower frequencies represent coarse details).
The rather complex process of convolution can be greatly simplified by looking
at the equivalent operation in Fourier space: The Fourier-transformed object
just needs to be multiplied with the
Fourier-transformed PSF to yield the Fourier-transformed ideal image (without
the noise). Because the Fourier-transformed PSF now describes how well each
spatial frequency of the Fourier-transformed object gets transferred to appear in the
image, this Fourier-transformed PSF is called the optical transfer function, OTF
(right panel). Its strength at each spatial frequency (e.g., measured in oscillations
per meter) conveniently describes the contrast that a sinusoidal object would
achieve in an image.

Abbe limit

Abbe limit

Interestingly, the detection OTF of a microscope has a fixed frequency
border (Abbe limit frequency, right panel). The maximum-to-maximum
distance Λmin of the corresponding sine curve is commonly referred to
as Abbe’s limit (left panel). In other words: The Abbe limit is the smallest
periodicity in a structure, which can be discriminated in its image. As a
point object contains all spatial frequencies, this Abbe limit sine curve
needs to also be present in the PSF. A standard wide-field microscope
creates an image of a point object (e.g., an emitting molecule) by capturing
the light from that molecule at various places of the objective lens, and
processing it with further lenses to then interfere at the image plane.
Conveniently due to the reciprocity principle in optics, the Abbe limit Λmin
along an in-plane direction in fluorescence imaging corresponds to the
maximum-to-maximum distance of the intensity structure one would get by
interfering two waves at extreme angles captured by the objective lens:
where λ/n is the wavelength of light in the medium of refractive index n.
The term NA = n sin(α) conveniently combines the half opening angle α
of the objective and the refractive index n of the embedding medium.

Abbe’s famous resolution limit is so attractive because it simply depends
on the maximal relative angle between different waves leaving the
object and being captured by the objective lens to be sent to the image.
It describes the smallest level of detail that can possibly be imaged with
this PSF “brush”. No periodic object detail smaller than this shortest
wavelength can possibly be transferred to the image.

Confocal laser scanning microscopy employs a redesigned optical
path and specialized hardware. A tightly focused spot of laser light is
used to scan the sample and a small aperture (or pinhole) in the
confocal image plane of the light path allows only light originating
from the nominal focus to pass (Cremer and Cremer, 1978Sheppard
and Wilson, 1981
Brakenhoff et al., 1985). The emitted light is
detected by a photomultiplier tube (PMT) or an avalanche photodiode
(APD) and the image is then constructed by mapping the detected
light in dependence of the position of the scanning spot. CLSM can
achieve a better resolution than wide-field fluorescence microscopy
but, to obtain a significant practical advantage, the pinhole needs to
be closed to an extent where most of the light is discarded
(Heintzmann et al., 2003).

Wide-field deconvolution and CLSM have long been the gold standards
in optical bioimaging, but we are now witnessing a revolution in light
microscopy that will fundamentally expand our perception of the cell.
Recently, several new technologies,collectively termed super-resolution
microscopy or nanoscopy, have been developed that break or bypass
the classical diffraction limit and shift the optical resolution down to
macromolecular or even molecular levels (Table I).

Super-resolution light microscopy methods

super resolution microscopy

super resolution microscopy

http://zeiss-campus.magnet.fsu.edu/articles/superresolution/introduction.html

Conceptually, one can discern near-field from far-field methods and
whether the subdiffraction resolution is based on a linear or nonlinear
response of the sample to its locally illuminating (exciting or depleting) irradiance. The required nonlinearity is currently achieved by using reversible saturable optical fluorescence transitions (RESOLFT) between molecular states (Hofmann et al., 2005Hell, 2007).

Besides these saturable optical fluorescence transitions also other
approaches, e.g., Rabi oscillations, could be used to generate the
required nonlinear response.

Note that each of the novel imaging modes has its individual signal-
to-noise consideration depending on various factors.  A full
discussion of this issue is beyond the scope of this review, but as a
general rule, single-point scanning systems, albeit fundamentally limited
in speed by fluorescence saturation effects, can have better signal-
to-noise performance for thicker samples.

With three-dimensional SIM (3D-SIM), an additional twofold increase
in the axial resolution can be achieved by generating an excitation
light modulation along the z-axis using three-beam interference
(Gustafsson et al., 2008Schermelleh et al.,2008) and processing a
z-stack of images accordingly. Thus, with 3D-SIM an approximately eightfold smaller volume can be resolved in comparison to conventional microscopy (Fig. 2). To computationally reconstruct a three-dimensional dataset of a typical mammalian cell of 8-µm height with a
z-spacing of 125 nm, roughly 1,000 raw images (512 × 512 pixels) are
recorded. Because no special photophysics is needed, virtually all modern fluorescent labels can be used provided they are sufficiently photostable
to accommodate the additional exposure cycles.

Resolvable volumes obtained with current commercial super-resolution microscopes.

A schematic 3D representation of focal volumes is shown for the indicated
emission maxima. The approximate lateral (x,y) and axial (z) resolution
and resolvable volumes are listed. Note that STED/CW-STED and 3D-SIM
can reach up to 20 µm into the sample, whereas PALM/STORM is usually
confined to the evanescent wave field near the sample bottom. It should be
noted that deconvolution approaches can further improve STED resolution.
For comparison the “focal volume” for PALM/STORM was estimated based
on the localization precision in combination with the z-range of TIRF.

Resolvable volumes obtained

Resolvable volumes obtained

Super-resolution microscopy of biological samples.

(A) Conventional wide-field image (left) and 3D-SIM image of a mouse
C2C12 prometaphase cell stained with primary antibodies against
lamin B and tubulin, and secondary antibodies conjugated to Alexa 488
(green) and Alexa 594 (red), respectively. Nuclear chromatin was stained
with DAPI (blue). 3D image stacks were acquired with a DeltaVision OMX
prototype system (Applied Precision). The bottom panel shows the
respective orthogonal cross sections. (B) HeLa cell stained with primary
antibodies against the nuclear pore complex protein Nup153 and
secondary antibodies conjugated with ATTO647N. The image was
acquired with a TCS STED confocal microscope (Leica). (C) TdEosFP-
paxillin expressed in a Hep G2 cell to label adhesion complexes at
the lower surface. The image was acquired on an ELYRA P.1
prototype system (Carl Zeiss, Inc.) using TIRF illumination. Single
molecule positional information was projected from 10,000 frames
recorded at 30 frames per second. On the left, signals were summed
up to generate a TIRF image with conventional wide-field lateral
resolution. Bars: 5 µm (insets, 0.5 µm).

biological images

biological images

APPLICATIONS IN BIOLOGICAL SYSTEMS

The cytoskeleton of mammalian cells, especially microtubules
(Figure 5a) (29444652), is the most commonly used benchmark
structure for super-resolution imaging. Other cytoskeletal structures
imaged so far include actin filaments in the lamellipodium (6),
keratin intermediate filaments (59), neurofilaments (2683) and
MreB in Caulobacter (66).

Figure 5

cytoskeleton. f5.

cytoskeleton. f5.

Examples of super-resolution images of biological samples.
(a) Two-color STORM imaging of immunostained microtubule (green)
and clathrin-coated pits (red) (From Reference 46. Reprinted with
permission from AAAS).

Organelles, such as the endoplasmic reticulum (27), lysosome (6),
endocytic and exocytic vesicles (465264), and mitochondria
(65356), have also been imaged. For example, using the single-molecule localization approach, 3D STORM imaging has clearly
resolved the ~150-nm diameter, hemispherical cage shape of clathrin-coated pits (4652), which only appear as diffraction-limited spots
without any feature in conventional fluorescence microscopy (Figure 5a,b).
Two-color 3D STED has resolved the hollow shape of the mitochondrial
outer membrane (marked by the translocase protein Tom20), enclosing
a matrix protein Hsp60 (56), even though the diameter of mitochondria is
only about 300–500 nm (Figure 5c). The outer membrane structure of
mitochondria and their interactions with microtubules have been resolved
by two-color 3D STORM (53). The transport of synaptic vesicles
has been recorded at video rate using 2D STED (Figure 5d ) (64).

Many plasma membrane proteins or membrane associated protein
complexes have also been studied by super-resolution fluorescence
microscopy. For example, synaptotagmin clusters after exocytosis in
primary cultured hippocampal neurons (84), the donut-shaped
clusters of Drosophila protein Bruchpilot at the neuromuscular
synaptic active zone (85), and the size distribution of syntaxin clusters
have all been imaged (8687). Photoactivation has enabled the tracking
of the influenza protein hemagglutinin and the retroviral protein Gag in
live cells, revealing the membrane microdomains (67) and the spatial
heterogeneity of membrane diffusion (68). The morphology and transport
of the focal adhension complex has also been observed using live-cell
PALM (Figure 5e) (65).

Summary points

  1. Super resolution fluorescence microscopy with a spatial resolution not limited by the diffraction of
    light has been implemented using saturated depletion/excitation or single-molecule localization
    of switchable fluorophores.
  2. Three-dimensional imaging with an optical resolution as high as ~20 nm in the lateral direction
    and 40–50 nm in axial dimension has been achieved.
  3. The resolution of these super-resolution fluorescence microscopy techniques can in principle
    reach molecular scale.
  4. In practice, the resolution of the images are not only limited by the intrinsic optical resolution,
    but also by sample specific factors including the labeling density, probe size and sample preservation.
  5. Multicolor super resolution imaging has been implemented, allowing colocalization measurements
    to be performed at nanometer scale resolution and molecular interaction to be more précisely
    identified in cells.
  6. Super-resolution fluorescence imaging allows dynamic processes to be investigated at the tens of
    nanometer resolution in living cells.
  7. Many cellular structures have been imaged at sub-diffraction-limit resolution.

Future issues

  1. Achieving molecular scale resolution (a few nanometers or less).
  2. Fast super resolution imaging of a large view field by multi-point scanning or high-speed single-molecule switching/localization.
  3. Developing new fluorescent probes that are brighter, more photostable and switchable fluorophores
    that have high on-off contrast and fast switching rate.
  4. Developing fluorescent labeling methods that can stain the target with small molecules at high specificity,
    high density and good ultrastructure preservation.
  5. Application of super resolution microscopy to provide novel biological insights

Acronyms

FP

Fluorescent Protein

FPALM

Fluorescence PhotoActivation Localization Microscopy

I5M

Combination of I2M (Illumination Interference Microscopy) and I3M
(Incoherent Imaging Interference Microscopy)

PALM

PhotoActivated Localization Microscopy

PSF

Point Spread Function

RESOLFT

REversible Saturable Optically Linear Fluorescence Transition

SIM

Structured Illumination Microscopy

SSIM

Saturated Structured Illumination Microscopy

STED

STimulated Emission Depletion

STORM

STochastic Optical Reconstruction Microscopy

glossary

Numerical aperture (NA)

The numerical aperture of an objective characterizes the solid angle
of light collected from a point light source at the focus of the objective.

Stimulated emission

The process that an excited state molecule or atom jumps to the
ground state by emitting another photon that is identical to the incoming
photon. It is the basis of laser.

Fluorescence saturation

At high excitation intensity, the fluorescence lifetime instead of the excitation
rate becomes the rate limiting step of fluorescence emission, causing the
fluorescence signal not to increase proportionally with the excitation intensity.

Nyquist criterion

To determine a structure, the sampling interval needs to be no larger than
half of the feature size.

Mitochondria

Organelles in eukaryotic cells for APT generation, consisting of two
membrane (inner and outer) enclosing the inter membrane space and
the matrix inside the inner membrane.

Clathrin-coated pit

Vesicle forming machinery involved in endocytosis and intracellular
vesicle transport, consisting of clathrin coats, adapter proteins, and
other regulatory proteins.

Focal adhesion

The macromolecular complex serving as the mechanical connection
and signaling hub between a cell and the extracellular matrix or other cells.

Selected references with abstract

Near-Field Optics: Microscopy, Spectroscopy, and Surface
Modification Beyond the Diffraction Limit
Eric Betzig,  Jay K. Trautman
AT&T Bell Laboratories, Murray Hill, NJ 07974
Science 10 Jul 1992; 257(5067) pp. 189-195
http://dx.doi.org:/0.1126/science.257.5067.189

 The near-field optical interaction between a sharp probe and a sample
of interest can be exploited to image, spectroscopically probe, or modify
surfaces at a resolution (down to ∼12 nm) inaccessible by traditional far-field
techniques. Many of the attractive features of conventional optics are
retained, including noninvasiveness, reliability, and low cost. In addition, most
optical contrast mechanisms can be extended to the near-field regime,
resulting in a technique of considerable versatility. This versatility
is demonstrated by several examples, such as the imaging of nanometric-scale features in mammalian tissue sections and the creation of ultrasmall,
magneto-optic domains having implications for high density data storage.
Although the technique may find uses in many diverse fields, two of the
most exciting possibilities are localized optical spectroscopy of semiconductors
and the fluorescence imaging of living cells.

Imaging Intracellular Fluorescent Proteins at Nanometer Resolution

 E Betzig1,2,*,†, GH. Patterson3, R Sougrat3, O.W Lindwasser3,
S Olenych4, JS. Bonifacino3, MW. Davidson4, JL Schwartz3, HF. Hess5,*  1 Howard Hughes Medical Institute, Janelia Farm Research Campus,
Ashburn, VA   2 New Millennium Research, LLC, Okemos, MI.   3 Cell Biology and Metabolism Branch, National Institute of Child Health
and Human Development (NICHD), Bethesda, MD.  4 National High
Magnetic Field Laboratory, Florida State University, Tallahassee, FL.
5 NuQuest Research, LLC, La Jolla, CA.
Science 15 Sep 2006; 313(5793): pp. 1642-1645
http://dx.doi.org:/10.1126/science.1127344

We introduce a method for optically imaging intracellular proteins at
nanometer spatial resolution. Numerous sparse subsets of photo-activatable fluorescent protein molecules were activated, localized
(to ∼2 to 25 nanometers), and then bleached. The
aggregate position information from all subsets was then assembled
into a super-resolution image. We used this method—termed photo-
activated localization microscopy to image specific target proteins
in thin sections of lysosomes and mitochondria; in fixed whole cells,
we imaged vinculin at focal adhesions, actin within a lamellipodium,
and the distribution of the retroviral protein Gag at the plasma
membrane.

Toward fluorescence nanoscopy.

Hell SW.   Author information 
Nat Biotechnol. 2003 Nov; 21(11):1347-55.
http://www.ncbi.nlm.nih.gov/pubmed/14595362

For more than a century, the resolution of focusing light microscopy
has been limited by diffraction to 180 nm in the focal plane and to
500 nm along the optic axis. Recently, microscopes have been
reported that provide three- to seven-fold improved axial
resolution in live cells. Moreover, a family of concepts has emerged
that overcomes the diffraction barrier altogether. Its first exponent,
stimulated emission depletion microscopy, has so far displayed a
resolution down to 28 nm. Relying on saturated optical transitions,
these concepts are limited only by the attainable saturation level.
As strong saturation should be feasible at low light intensities,
nanoscale imaging with focused light may be closer than ever.
PMID: 14595362

Far-field optical nanoscopy.

Hell SW.  Author information 
Science. 2007 May 25;316(5828):1153-8.
http://www.ncbi.nlm.nih.gov/pubmed/17525330

In 1873, Ernst Abbe discovered what was to become a well-known
paradigm: the inability of a lens-based optical microscope to
discern details that are closer together than half of the wavelength
for its most popular imaging mode, fluorescence microscopy, the
diffraction barrier is crumbling. Here, I discuss the physical concepts
that have pushed fluorescence microscopy to the nanoscale, once
the prerogative of electron and scanning probe microscopes. Initial
applications indicate that emergent far-field optical nanoscopy will
have a strong impact in the life sciences and in other areas benefiting
from nanoscale visualization.
PMID:  17525330

Imaging intracellular fluorescent proteins at nanometer resolution.

Betzig E1, Patterson GHSougrat RLindwasser OWOlenych S,
Bonifacino JSDavidson MWLippincott-Schwartz JHess HF.
Author information
Science. 2006 Sep 15;313(5793):1642-5. Epub 2006 Aug 10
http://www.ncbi.nlm.nih.gov/pubmed/16902090

We introduce a method for optically imaging intracellular proteins at
nanometer spatial resolution. Numerous sparse subsets of photo-ctivatable fluorescent protein molecules were activated, localized
(to approximately 2 to 25 nanometers), and then bleached. The
aggregate position information from all subsets was then assembled
into a super-resolution image. We used this method–termed photo-activated localization microscopy–to image specific target proteins in
thin sections of lysosomes and mitochondria; in fixed whole cells,
we imaged vinculin at focal adhesions, actin within a lamellipodium,
and the distribution of the retroviral protein Gag at the plasma
membrane.

Comment in

PMID:  16902090  [PubMed – indexed for MEDLINE]

Illuminating single molecules in condensed matter.

Moerner WE1, Orrit M.  Author information 
Science. 1999 Mar 12;283(5408):1670-6.
http://www.ncbi.nlm.nih.gov/pubmed/10073924

Efficient collection and detection of fluorescence coupled with careful
minimization of background from impurities and Raman scattering
now enable routine optical microscopy and study of single molecules
in complex condensed matter environments. This ultimate method
for unraveling ensemble averages leads to the observation of
new effects and to direct measurements of stochastic fluctuations.
Experiments at cryogenic temperatures open new directions in
molecular spectroscopy, quantum optics, and solid-state dynamics.
Room-emperature investigations apply several techniques
(polarization microscopy, single-molecule imaging, emission time
dependence, energy transfer, lifetime studies, and the like) to a
growing array of biophysical problems where new insight may be
gained from direct observations of hidden static and dynamic
inhomogeneity.  PMID: 10073924

Fluorescence microscopy with super-resolved optical sections.

Egner A1, Hell SW.  Author information 
Trends Cell Biol. 2005 Apr;15(4):207-15.
http://www.ncbi.nlm.nih.gov/pubmed/15817377

The fluorescence microscope, especially its confocal variant, has
become a standard tool in cell biology research for delivering
3D-images of intact cells. However, the resolution of any standard
optical microscope is atleast 3 times poorer along the axis of the
lens that in its focal plane. Here, we review principles and applications
of an emerging family of fluorescence microscopes, such as 4Pi
microscopes, which improve axial resolution by a factor of seven by
employing two opposing lenses. Noninvasive axial sections of 80-160 nm
thickness deliver more faithful 3D-images of subcellular features,
providing a new opportunity to significantly enhance our understanding
of cellular structure and function. PMID: 15817377

4Pi-confocal microscopy provides three-dimensional images of the
microtubule network with 100- to 150-nm resolution.

Nagorni M1, Hell SW.  Author information 
J Struct Biol. 1998 Nov;123(3):236-47.

We show the applicability of 4Pi-confocal microscopy to three-dimensional imaging of the microtubule network in a fixed mouse
fibroblast cell.Comparison with two-photon confocal resolution
reveals a fourfold better axial resolution in the 4Pi-confocal case.
By combining 4Pi-confocal microscopy with Richardson-Lucy
image restoration a further resolution increase is achieved.
Featuring a three-dimensional resolution in the range 100-150 nm,
the 4Pi-confocal (restored) images are intrinsically more detailed
than their confocal counterparts. Our images constitute what
to our knowledge are the best-resolved three-dimensional
images of entangled cellular microtubules obtained with light
to date.  PMID: 9878578

Part IV. Super-resolution microscopy

Super-resolution microscopy is a form of light microscopy. Due
to the diffraction of light, the resolution of conventional light
microscopy is limited as stated by Ernst Abbe in 1873.[1]
A good approximation of the resolution attainable is the full
width at half maximum 
 (FWHM) of the point spread function,
and a precise wide-field microscope with high numerical
aperture
 and visible light usually reaches a resolution of ~250 nm.

Super-resolution techniques allow the capture of images with
a higher resolution than the diffraction limit. They fall into
two broad categories,
“true” super-resolution techniques, which capture information
contained in evanescent waves, and “functional” super-
resolution techniques, which use clever experimental
techniques and known limitations on the matter being
imaged to reconstruct a super-resolution image.[2]

True subwavelength imaging techniques include those that
utilize the Pendry Superlens and near field scanning optical
microscopy
, the 4Pi Microscope and structured illumination
microscopy technologies like SIM and SMI. However, the
majority of techniques of importance in biological imaging
fall into the functional category.

Groups of methods for functional super-resolution microscopy:

  1. Deterministic super-resolution: The most commonly used emitters in biological
    microscopy, fluorophores, show a nonlinear response to excitation, and this
    nonlinear response can be exploited to enhance resolution. These
    methods include STEDGSDRESOLFTand SSIM.
  2. Stochastic super-resolution: The chemical complexity of many molecular
    light sources gives them a complex temporal behaviour, which can be used
    to make several close-by fluorophores emit light at separate times and
    thereby become resolvable in time.  These methods include SOFI and all
    single-molecule localization methods (SMLM) such as SPDM,
    SPDMphymodPALM, FPALM, STORM and dSTORM.

Part V. HIV-1

Conformational dynamics of single HIV-1 envelope
trimers on the surface of native virions

James B. Munro1,*,Jason Gorman2Xiaochu Ma1,
Zhou Zhou3James Arthos4,
Dennis R. Burton5,6, et al.
1Department of Microbial Pathogenesis, Yale University
School of Medicine, New Haven, CT. 2Vaccine Research
Center, National Institute of Allergy and Infectious
Diseases, National Institutes of Health, Bethesda, MD .
3Department of Physiology and Biophysics, Weill
Cornell Medical College of Cornell University, New York, NY .
4Laboratory of Immunoregulation, National Institute of Allergy
and Infectious Diseases, National Institutes of Health, Bethesda,
MD . 5Department of Immunology and Microbial Science, and
IAVI Neutralizing Antibody Center, The Scripps Research
Institute, La Jolla, CA . 6Ragon Institute of MGH, MIT, and
Harvard, Cambridge, MA. 7International AIDS Vaccine Initiative
(IAVI), New York, NY . 8Department of
Chemistry, University of Pennsylvania, Philadelphia, PA.

The HIV-1 envelope (Env) mediates viral entry into host cells.
To enable the direct imaging of conformational dynamics
within Env we introduced fluorophores into variable
regions of the gp120 subunit and measured single-molecule
fluorescence resonance energy transfer (smFRET) within
the context of native trimers on the surface of HIV-1 virions.
Our observations revealed unliganded HIV-1 Env to be
intrinsically dynamic, transitioning between three distinct
pre-fusion conformations, whose relative occupancies
were remodeled by receptor CD4 and antibody binding.
The distinct properties of neutralization-sensitive and
neutralization-resistant HIV-1 isolates support a dynamics-based mechanism of immune evasion and ligand recognition.

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Imaging-guided cancer treatment

Imaging-guided cancer treatment

Writer & reporter: Dror Nir, PhD

It is estimated that the medical imaging market will exceed $30 billion in 2014 (FierceMedicalImaging). To put this amount in perspective; the global pharmaceutical market size for the same year is expected to be ~$1 trillion (IMS) while the global health care spending as a percentage of Gross Domestic Product (GDP) will average 10.5% globally in 2014 (Deloitte); it will reach ~$3 trillion in the USA.

Recent technology-advances, mainly miniaturization and improvement in electronic-processing components is driving increased introduction of innovative medical-imaging devices into critical nodes of major-diseases’ management pathways. Consequently, in contrast to it’s very small contribution to global health costs, medical imaging bears outstanding potential to reduce the future growth in spending on major segments in this market mainly: Drugs development and regulation (e.g. companion diagnostics and imaging surrogate markers); Disease management (e.g. non-invasive diagnosis, guided treatment and non-invasive follow-ups); and Monitoring aging-population (e.g. Imaging-based domestic sensors).

In; The Role of Medical Imaging in Personalized Medicine I discussed in length the role medical imaging assumes in drugs development.  Integrating imaging into drug development processes, specifically at the early stages of drug discovery, as well as for monitoring drug delivery and the response of targeted processes to the therapy is a growing trend. A nice (and short) review highlighting the processes, opportunities, and challenges of medical imaging in new drug development is: Medical imaging in new drug clinical development.

The following is dedicated to the role of imaging in guiding treatment.

Precise treatment is a major pillar of modern medicine. An important aspect to enable accurate administration of treatment is complementing the accurate identification of the organ location that needs to be treated with a system and methods that ensure application of treatment only, or mainly to, that location. Imaging is off-course, a major component in such composite systems. Amongst the available solution, functional-imaging modalities are gaining traction. Specifically, molecular imaging (e.g. PET, MRS) allows the visual representation, characterization, and quantification of biological processes at the cellular and subcellular levels within intact living organisms. In oncology, it can be used to depict the abnormal molecules as well as the aberrant interactions of altered molecules on which cancers depend. Being able to detect such fundamental finger-prints of cancer is key to improved matching between drugs-based treatment and disease. Moreover, imaging-based quantified monitoring of changes in tumor metabolism and its microenvironment could provide real-time non-invasive tool to predict the evolution and progression of primary tumors, as well as the development of tumor metastases.

A recent review-paper: Image-guided interventional therapy for cancer with radiotherapeutic nanoparticles nicely illustrates the role of imaging in treatment guidance through a comprehensive discussion of; Image-guided radiotherapeutic using intravenous nanoparticles for the delivery of localized radiation to solid cancer tumors.

 Graphical abstract

 Abstract

One of the major limitations of current cancer therapy is the inability to deliver tumoricidal agents throughout the entire tumor mass using traditional intravenous administration. Nanoparticles carrying beta-emitting therapeutic radionuclides [DN: radioactive isotops that emits electrons as part of the decay process a list of β-emitting radionuclides used in radiotherapeutic nanoparticle preparation is given in table1 of this paper.) that are delivered using advanced image-guidance have significant potential to improve solid tumor therapy. The use of image-guidance in combination with nanoparticle carriers can improve the delivery of localized radiation to tumors. Nanoparticles labeled with certain beta-emitting radionuclides are intrinsically theranostic agents that can provide information regarding distribution and regional dosimetry within the tumor and the body. Image-guided thermal therapy results in increased uptake of intravenous nanoparticles within tumors, improving therapy. In addition, nanoparticles are ideal carriers for direct intratumoral infusion of beta-emitting radionuclides by convection enhanced delivery, permitting the delivery of localized therapeutic radiation without the requirement of the radionuclide exiting from the nanoparticle. With this approach, very high doses of radiation can be delivered to solid tumors while sparing normal organs. Recent technological developments in image-guidance, convection enhanced delivery and newly developed nanoparticles carrying beta-emitting radionuclides will be reviewed. Examples will be shown describing how this new approach has promise for the treatment of brain, head and neck, and other types of solid tumors.

The challenges this review discusses

  • intravenously administered drugs are inhibited in their intratumoral penetration by high interstitial pressures which prevent diffusion of drugs from the blood circulation into the tumor tissue [1–5].
  • relatively rapid clearance of intravenously administered drugs from the blood circulation by kidneys and liver.
  • drugs that do reach the solid tumor by diffusion are inhomogeneously distributed at the micro-scale – This cannot be overcome by simply administering larger systemic doses as toxicity to normal organs is generally the dose limiting factor.
  • even nanoparticulate drugs have poor penetration from the vascular compartment into the tumor and the nanoparticles that do penetrate are most often heterogeneously distributed

How imaging could mitigate the above mentioned challenges

  • The inclusion of an imaging probe during drug development can aid in determining the clearance kinetics and tissue distribution of the drug non-invasively. Such probe can also be used to determine the likelihood of the drug reaching the tumor and to what extent.

Note: Drugs that have increased accumulation within the targeted site are likely to be more effective as compared with others. In that respect, Nanoparticle-based drugs have an additional advantage over free drugs with their potential to be multifunctional carriers capable of carrying both therapeutic and diagnostic imaging probes (theranostic) in the same nanocarrier. These multifunctional nanoparticles can serve as theranostic agents and facilitate personalized treatment planning.

  • Imaging can also be used for localization of the tumor to improve the placement of a catheter or external device within tumors to cause cell death through thermal ablation or oxidative stress secondary to reactive oxygen species.

See the example of Vintfolide in The Role of Medical Imaging in Personalized Medicine

vinta

Note: Image guided thermal ablation methods include radiofrequency (RF) ablation, microwave ablation or high intensity focused ultrasound (HIFU). Photodynamic therapy methods using external light devices to activate photosensitizing agents can also be used to treat superficial tumors or deeper tumors when used with endoscopic catheters.

  • Quality control during and post treatment

For example: The use of high intensity focused ultrasound (HIFU) combined with nanoparticle therapeutics: HIFU is applied to improve drug delivery and to trigger drug release from nanoparticles. Gas-bubbles are playing the role of the drug’s nano-carrier. These are used both to increase the drug transport into the cell and as ultrasound-imaging contrast material. The ultrasound is also used for processes of drug-release and ablation.

 HIFU

Additional example; Multifunctional nanoparticles for tracking CED (convection enhanced delivery)  distribution within tumors: Nanoparticle that could serve as a carrier not only for the therapeutic radionuclides but simultaneously also for a therapeutic drug and 4 different types of imaging contrast agents including an MRI contrast agent, PET and SPECT nuclear diagnostic imaging agents and optical contrast agents as shown below. The ability to perform multiple types of imaging on the same nanoparticles will allow studies investigating the distribution and retention of nanoparticles initially in vivo using non-invasive imaging and later at the histological level using optical imaging.

 multi

Conclusions

Image-guided radiotherapeutic nanoparticles have significant potential for solid tumor cancer therapy. The current success of this therapy in animals is most likely due to the improved accumulation, retention and dispersion of nanoparticles within solid tumor following image-guided therapies as well as the micro-field of the β-particle which reduces the requirement of perfectly homogeneous tumor coverage. It is also possible that the intratumoral distribution of nanoparticles may benefit from their uptake by intratumoral macrophages although more research is required to determine the importance of this aspect of intratumoral radionuclide nanoparticle therapy. This new approach to cancer therapy is a fertile ground for many new technological developments as well as for new understandings in the basic biology of cancer therapy. The clinical success of this approach will depend on progress in many areas of interdisciplinary research including imaging technology, nanoparticle technology, computer and robot assisted image-guided application of therapies, radiation physics and oncology. Close collaboration of a wide variety of scientists and physicians including chemists, nanotechnologists, drug delivery experts, radiation physicists, robotics and software experts, toxicologists, surgeons, imaging physicians, and oncologists will best facilitate the implementation of this novel approach to the treatment of cancer in the clinical environment. Image-guided nanoparticle therapies including those with β-emission radionuclide nanoparticles have excellent promise to significantly impact clinical cancer therapy and advance the field of drug delivery.

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Leaders in Pharmaceutical Business Intelligence Announced New Cardiovascular Series of e-Books at SACHS Associates 14th Annual Biotech In Europe Forum

Reporter: Aviva Lev-Ari, PhD, RN

 

 

Please see Further Titles at

http://pharmaceuticalintelligence.com/biomed-e-books/

Please see Further Information on the Sachs Associates 14th Annual Biotech in Europe Forum for Global Investing & Partnering at:

http://pharmaceuticalintelligence.com/2014/03/25/14th-annual-biotech-in-europe-forum-for-global-partnering-investment-930-1012014-%E2%80%A2-congress-center-basel-sachs-associates-london/

AND

http://www.sachsforum.com/basel14/index.html

why-is-twitter-s-logo-named-after-larry-bird--b8d70319daON TWITTER Follow at

@SachsAssociates

#Sachs14thBEF

@pharma_BI

@AVIVA1950 

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Larry H. Bernstein, MD, FCAP, Curator

Leaders in Pharmaceutical Intelligence

Early discharge using single cardiac troponin and copeptin testing in patients
with suspected 
acute coronary syndrome (ACS): a randomized, controlled
clinical process study
M Mockel, J Searle, Christian Hamm, A Slagman, S Blankenberg, et al.
EurHeartJ Apr 2014.  http://dx.doi.org:/10.1093/eurheartj/ehu178

This randomized controlled trial (RCT) evaluated whether a process with single
combined testing of copeptin and troponin at admission in patients with low-to-
intermediate risk and suspected acute coronary syndrome (ACS)  does not lead to a higher proportion of major adverse cardiac events (MACE) than
the current standard process (non-inferiority design). After clinical work-up and  single combined testing of troponin and copeptin to rule-out AMI,  early  discharge
of low- to intermediate risk patients with suspected ACS seems to be safe and has
the potential to shorten length of stay in the ED.

Diagnostic accuracy of combined cardiac troponin and copeptin
assessment for 
early rule-out of myocardial infarction: a systematic
review and meta-analysis
T Raskovalova, R Twerenbold, PO Collinson, T Keller, H Bouvaist, et al.
http://acc.sagepub.com/content/3/1/18
EurHeartJ: Acute Cardiovascular Care 2014; 3(1): 18-27.
http://dx.doi.org:/10.1177/2048872613514015

This systematic review aimed to investigate the diagnostic accuracy of combined
cardiac troponin (cTn) and  copeptin assessment in comparison to cTn alone for
early rule-out of acute myocardial infarction (AMI).  In 15  studies totalling 8740
patients (prevalence of   AMI 16%), adding copeptin improved the sensitivity
of cTn assays  (from 0.87 to 0.96, p=0.003) at the expense of lower specificity
(from 0.84 to 0.56, p<0.001).

In 12 studies providing for 6988 patients without ST-segment elevation,
the summary sensitivity and specificity  estimates were 0.95 (95% CI 0.89 to
0.98) and 0.57 (95% CI 0.49 to   0.65) for the combined assessment of cTn
and copeptin. When a high-sensitivity cTnT assay was used in combination
with copeptin,  the summary sensitivity  and specificity estimates were 0.98
(95% CI 0.96 to 1.00) and 0.50 (95% CI 0.42 to 0.58). The result indicates
that  copeptin significantly improves baseline cTn sensitivity.

Diagnostic accuracy of copeptin sensitivity and specificity in patients with
suspected non-ST-elevation myocardial infarction with troponin I below
the 
99th centile at presentation
J Duchenne, S Mestres, N Dublanchet, N Combaret, G Marceau, et al.
BMJ Open 2014;4:e004449.
http://dx.doi.org:/10.1136/bmjopen-2013-004449

To our knowledge, our prospective multicentric study is the only one that includes
only patients with suspected non-ST-segment elevation myocardial infarction and
high-sensitive cardiac troponin I below  the 99th centile  at presentation to the
emergency department, to limit spectrum bias. Our study included only patients
with negative ultrasensitive troponin at admission. However, this is the only group
of patients for which a multimarker rule-out strategy could add diagnostic value.
Serial clinical, electrographical and biochemical investigations were performed at
admission and after 2, 4, 6 and 12 h. Hs-cTnT was measured using an assay with
Dimension VISTA, Siemens. Copeptin was measured by the BRAHMS copeptin-us
assay on the KRYPTOR Compact Plus system. The follow-up period was 90 days.

The final diagnosis was adjudicated blinded to copeptin result. During 12 months,
102 patients were analysed. Final diagnosis was NSTEMI for 7.8% (n=8), unstable
angina for 3.9% (n=4), cardiac but non coronary artery disease for 8.8% (n=9),
non-cardiac chest pain for 52% (n=53) and unknown for 27.5% (n=28).

There was no statistical difference for copeptin values between patients with
NSTEMI and others (respectively 5.5 pmol/L IQR (3.1–7.9) and 6.5 pmol/L IQR
(3.9–12.1), p=0.49). Only one patient with NSTEMI had a copeptin value
above the cut-off
 of 95th centile at admission.

In this study, copeptin does not add a diagnostic value at admission to ED for patients
with suspected acute coronary syndrome without ST-
segment elevation and with hs-cTnT below the 99th centile.

Can a Second Measurement of Copeptin Improve Acute Myocardial
Infarction Rule Out?

N Marston, K Shah, C Mueller, Sean-Xavier Neath, R Christenson, J McCord, et al.
J Am Coll Cardiol. 2014;63(12_S):A202.  Presentation Number: 1226-242
http://dx.doi.org:/10.1016/S0735-1097(14)60202-3

Of the 494 patients analyzed, 378 (76.5%) had a persistently elevated copeptin at 2
hours and 116 patients (23.5%) had a copeptin that fell below the cutoff of 14 pmol/l.
The AMI rate was 6.1% when the second copeptin was elevated compared to 0%
when the second copeptin was not (p=.006), yielding a sensitivity of 100%. This
strategy identified 23.5% of patients with an intermediate risk who could be ruled
out for AMI while still in the ED. In contrast, a second troponin measurement had a
sensitivity of 74%. A negative second copeptin drawn 2 hours after presentation
demonstrated 100% sensitivity for AMI, allowing for effective rule out in this
intermediate risk cohort. This strategy identified nearly 25% of intermediate risk
patients who could be considered for discharge.

 The role of copeptin as a diagnostic and prognostic biomarker for risk
stratification in the emergency department.
Nickel CH, Bingisser R and Morgenthaler NG
BMC Medicine 2012, 10:7
http://www.biomedcentral.com/1741-7015/10/7

Copeptin, the C-terminal part of the arginine vasopressin precursor peptide,
is a sensitive and stable surrogate marker for arginine vasopressin release.
Measurement of copeptin levels has been shown to be useful in a variety of
clinical scenarios, particularly as a prognostic marker in patients with acute
diseases such as lower respiratory tract infection, heart disease and stroke.

Read Full Post »

Larry H Bernstein, MD, Curator

Leaders in Pharmaceutical Intelligence

 

Natriuretic Peptides (BNP and Amino-terminal proBNP)

Author: Larry Bernstein, M.D.,
(see Reviewers/Authors page)
Revised: 12 December 2010, last major update December 2010
Copyright: (c) 2003-2010, PathologyOutlines.com, Inc.
http://dx.doi.org:/PathologyOutlines.com/cardiac

General
=========================================================================

  • Brain natriuretic peptide (BNP), now known as B-type natriuretic peptide (also BNP),
    is a 32 amino acid polypeptide secreted by the cardiac ventricles in response to
    excessive stretching of cardiomyocytes (Wikipedia)
  • BNP was originally identified in extracts of porcine brain, although in humans
    it is produced mainly in the cardiac ventricles
  • BNP is co-secreted with a 76 amino acid N-terminal fragment (NT-proBNP),
    which is biologically inactive Indications

=========================================================================

  • Evaluation of dyspneic patient with suspected congestive heart failure,
    regardless of renal function (J Am Coll Cardiol 2006;47:91)
  • B-type natriuretic peptide levels are higher in patients with congestive heart
    failure than in dyspnea from other causes (J Am Coll Cardiol 2002;39:202,
    N Engl J Med 2004;350:647)
  • NT-proBNP measurement is a valuable addition to standard clinical
    assessment for the identification and exclusion of acute CHF in the
    emergency department setting (Am J Cardiol 2005;95:9480)

Clinical features
=========================================================================

  • Reduces misdiagnosis of congestive heart failure, which occurs
    50% to 75% of the time
  • NT-proBNP is superior to BNP for predicting mortality and morbidity for heart
    failure (Clin Chem 2006;52:1528), and coexisting renal disease and heart failure
    (Clin Chem 2007;53:1511)

Reference ranges
=========================================================================

  • BNP levels below 100 pg/mL indicate no heart failure

Limitations
=========================================================================

  • Determination of endogenous BNP with the AxSYM assay using frozen
    plasma samples may not be valid after 1 day, but NT-proBNP as
    measured by the Elecsys assay may be stored at -20 degrees C for
    at least four months without a relevant loss of the immunoreactive
    analyte (Clin Chem Lab Med 2004;42:942)

Additional references
=========================================================================

  • Clin Chem 2007;53:1928, Am J Kidney Dis 2005;46:610,
    Hypertension 2005;46:118, Hypertension 2006;47:874,
    Eur J Heart Fail 2004;6:269

Natriuretic peptides for risk stratification of patients with acute
coronary
 syndromes  
M Galvani,  D Ferrini, F Ottani. Eur J Heart Fail 2004;  6: 327–333.
http://eurjhf.oxfordjournals.org

Both BNP and NT-proBNP possess several characteristics of the ideal biomarker,
showing independent and incremental prognostic value above traditional clinical,
electrocardiographic, and biochemical (particularly troponin) risk indicators. Specifically,
in ACS patients, BNP and NT-proBNP have powerful prognostic value both in patients
without a history of previous heart failure or without clinical or instrumental signs of
left ventricular dysfunction on admission or during hospital stay.

Our results show that the prognostic value of natriuretic peptides is similar:
(1) both at short- and long-term;
(2) when natriuretic peptides are measured at first patient contact or during hospital stay;
(3) for BNP or NT-proBNP; and
(4) in patients with ST elevation myocardial infarction or no ST elevation ACS.

 

Steady-State Levels of Troponin and Brain Natriuretic Peptide for Prediction
of Long-Term
 Outcome after Acute Heart Failure with or without Stage 3 to 4
Chronic Kidney Disease

Y Endo, S Kohsaka, T Nagai, K Koide, M Takahashi, et al.
Br J Med Med Res 2012; 2(4): 490-500.
http://dx.doi.org:/10.9734/BJMMR/2012/1384

The population was predominantly male (69.3%), and the mean age was 66.6±15.3 years.
Patients with higher BNP levels or detectable TnT had a worse prognosis (BNP45.0% vs.
18.8%, p<0.001; TnT 43.8% vs. 25.1%, p=0.002, respectively). The primary event rate
was additively worse among patients with both increased BNP levels and detectable TnT
compared to those with increased levels of BNP or detectable TnT alone (log-rank p<0.001).
A similar trend was observed in the subgroup of patients with CKD stage III–V (n=172).

The Effect of Correction of Mild Anemia in Severe, Resistant Congestive
Heart Failure
 Using Subcutaneous Erythropoietin and Intravenous Iron:
A Randomized Controlled Study

DS. Silverberg, D Wexler, D Sheps, M Blum, G Keren, et al.  JACC 2001; 37(7).
PII S0735-1097(01)01248-7  http://www.ncbi.nlm.nih.gov/pubmed/11401110

When anemia in CHF is treated with EPO and IV iron, a marked improvement in
cardiac and patient function is seen, associated with less hospitalization and renal
impairment and less need for diuretics. (J Am Coll Cardiol 2001;37:1775– 80)

 

 

 

Hemoglobin on NT proBNP

Hemoglobin on NT proBNP

 

 

 

 

What is the best approximation of reference normal for NT-proBNP?
Clinical levels for enhanced assessment
 of NT-proBNP (CLEAN) 

Larry H. Bernstein1*, Michael Y. Zions1,4, Mohammed E. Alam1,5, Salman A. Haq1,
John F. Heitner1, Stuart Zarich2, Bette Seamonds3 and Stanley Berger3
1New York Methodist Hospital, Brooklyn, NY; 2Bridgeport Hospital, Bridgeport, CT;
3Mercy Catholic Medical Center, Darby, Phila, PA;  4Touro College, &  5Medgar
Evers College, Brooklyn, NY
Journal of Medical Laboratory and Diagnosis 04/2011; 2:16-21.
http://www.academicjournals.org/jmld

The natriuretic peptides, B-type natriuretic peptide (BNP) and NT-proBNP that
have emerged as tools for diagnosing congestive heart failure (CHF) are affected
by age and renal insufficiency (RI).  NTproBNP is used in rejecting CHF and as a
marker of risk for patients with acute coronary syndromes. This observational study
was undertaken to evaluate the reference value for interpreting NT-proBNP
concentrations. The hypothesis is that increasing concentrations of NT-proBNP
are associated with the effects of multiple co-morbidities, not merely CHF,
resulting in altered volume status or myocardial filling pressures.

NT-proBNP was measured in a population with normal trans-thoracic echocardiograms
(TTE) and free of anemia or renal impairment. Exclusion conditions were the following
co-morbidities:

  • anemia as defined by WHO,
  • atrial fibrillation (AF),
  • elevated troponin T exceeding 0.070 mg/dl,
  • systolic or diastolic blood pressure exceeding 140 and 90 respectively,
  • ejection fraction less than 45%,
  • left ventricular hypertrophy (LVH),
  • left ventricular wall relaxation impairment, and
  • renal insufficiency (RI) defined by creatinine clearance < 60ml/min using
    the MDRD formula .

Study participants were seen in acute care for symptoms of shortness of breath
suspicious for CHF requiring evaluation with cardiac NTproBNP assay. The median
NT-proBNP for patients under 50 years is 60.5 pg/ml with an upper limit of 462 pg/ml,
and for patients over 50 years the median was 272.8 pg/ml with an upper limit of
998.2 pg/ml.
We suggest that NT-proBNP levels can be more accurately interpreted only after
removal of the major co-morbidities that affect an increase in this  peptide in serum.
The PRIDE study guidelines should be applied until presence or absence of
comorbidities is diagnosed. With no comorbidities, the reference range for normal
over 50 years of age remains steady at ~1000 pg/ml. The effect shown in previous
papers likely is due to increasing concurrent comorbidity with age.

NT-proBNP profile of combined population taken from 3 sites and donors.

Age    Under 50 years 50-69 years 70 and over
NT-proBNP

Mean   
95% CI of Mean
Median   
95% CI of median
2.5-97.5 percentile   
25-75 percentile
209
35.9
29.8-43.3
27.6
24.8-33.6
5.0-1364
14.9-55.8
126
182.4
132.1-251.9
142.3
92.3-219.0
10.8-11604
42.1-565
82
611.7
425.2-880.1
564.2
419.7-1007.7
28.8-14242
210.2-2062

 

We observe the following changes with respect to NTproBNP and age:

(i) Sharp increase in NT-proBNP at over age 50

(ii) Increase in NT-proBNP at 7% per decade over 50

(iii) Decrease in eGFR at 4% per decade over 50

(iv) Slope of NT-proBNP increase with age is related to proportion of patients with
eGFR less than 90

(v) NT-proBNP increase can be delayed or accelerated based on disease
comorbidities

NT-proBNP sensitivity and specificity with RI prevalence

NT-proBNP sensitivity and specificity with RI prevalence

Figure 1. Plot of NT-proBNP sensitivity and specificity with RI prevalence.
GFRe scale: 0, > 120; 1, 90- 119; 2, 60-89; 3, 40-59; 4, 15-39; 5, under 15 ml/min.

NKF staging by GFRe interval and NT-proBNP (CHF removed).

NKF staging by GFRe interval and NT-proBNP (CHF removed).

 

Figure 2  plots the mean and 95% CI of NTproBNP (CHF removed) by the National Kidney Foundation
staging for eGFR interval (eGFR scale: 0, > 120; 1, 90 to 119;2, 60 to 89; 3, 40 to 59; 4, 15 to 39; 5,
under 15 ml/min). We created a new variable to minimize the effects of age and eGFR variability by
correcting these large effects in the whole sample population.

Adjustment of the NT-proBNP for eGFR and for age over 50 differences. We have
carried out a normalization to adjust for both eGFR and for age over 50:

(i) Take Log of NT-proBNP and multiply by 1000

(ii) Divide the result by eGFR (using MDRD9 or Cockroft Gault10)

(iii) Compare results for age under 50, 50-70, and over 70 years

(iv) Adjust to age under 50 years by multiplying by 0.66 and 0.56.

The equation does not require weight because the results are reported normalized
to 1.73 m2 body surface area, which is an accepted average adult surface area.

 

fn.log-NT-proBNP vs age

fn.log-NT-proBNP vs age

Figure 3.  Plot of 1000*log (NT-proBNP)/GFR vs age at  eGFR over 90  and 60 ml/min

scatterplot and regression line with centroid and confidence interval for fn.logNTproBNP vs age

scatterplot and regression line with centroid and confidence interval for fn.logNTproBNP vs age

Figure 4. Superimposed scatterplot and regression line with centroid and
confidence interval for 1000*log(NT-proBNP)/eGFR vs age (anemia removed)
at eGFR over 40 and 90 ml/min. (Black: eGFR > 90, Blue:  eGFR > 40)  

 

Ref Range NTpro NKLogNTpro

Ref Range NTpro NKLogNTpro

 

Reference range for NT-proBNP before and after adjusting

 

Amino-Terminal Pro-Brain Natriuretic Peptide, Renal Function, and
Outcomes in Acute Heart Failure
RRJ. van Kimmenade,  JL. Januzzi, JR,  AL. Baggish, et al. JACC 2006; 48(8).: 1621-7.

We sought to study the individual and integrative role of amino-terminal pro-brain natriuretic
peptide (NT-proBNP) and parameters of renal function for prognosis in heart failure. The
combination of NT-proBNP with measures of renal function better predicts short-term outcome
in acute heart failure than either parameter alone. Among heart failure patients, the objective
parameter of NT-proBNP seems more useful to delineate the “cardiorenal syndrome” than the
previous criteria of a clinical diagnosis of heart failure.

 

NT-proBNP testing for diagnosis and short-term prognosis in acute destabilized
heart failure: an international pooled analysis of 1256 patients The International
Collaborative of NT-proBNP Study
Januzzi, R van Kimmenade, J Lainchbury, A Bayes-Genis, J Ordonez-Llanos, et al.
Eur Heart J 2006; 27, 330–337. http://dx.doi.org:/10.1093/eurheartj/ehi631

Differences in NT-proBNP levels among 1256 patients with and without acute HF and the relationship
between NT-proBNPlevels and HF symptomswere examined.Optimal cut-points for diagnosis and
prognosis were identified and verified using bootstrapping and multi-variable logistic regression techniques.

Seven hundred and twenty subjects (57.3%) had acute HF, whose median NT-proBNP was considerably
higher than those without (4639 vs. 108 pg/mL, P < 0.001), and levels of NT-proBNP correlated with HF
symptom severity (P < 0.008). An optimal strategy to identify acute HF was to use age-related cut-points
of 450, 900, and 1800 pg/mL for ages < 50, 50–75, and  > 75, which yielded 90% sensitivity and 84% specificity
for acute HF. An age-independent cut-point of 300 pg/mL had 98% negative predictive value to exclude acute
HF. Among those with acute HF, a presenting NT-proBNP concentration > 5180 pg/mL was strongly predictive
of death by 76 days [odds ratio = 5.2, 95% confidence interval (CI) =2.2 – 8.1, P < 0.001].

Effect of B-type natriuretic peptide-guided treatment of chronic heart failure on total mortality
and hospitalization: an individual patient meta-analysis
RW. Troughton, CM. Frampton, HP Brunner-La Rocca, M Pfisterer, LW.M. Eurlings, et al.
Eur Heart J Mar 2014; 35, 1559–1567.
http://dx.doi.org:/10.1093/eurheartj/ehu090

We sought to perform an individual patient data meta-analysis to evaluate the effect of NP-guided treatment
of heart failure on all-cause mortality.  The survival benefit from NP-guided therapy was seen in younger (< 75
years) patients [0.62 (0.45–0.85); P = 0.004] but not older (≥75 years) patients [0.98 (0.75–1.27); P = 0.96].
Hospitalization due to heart failure [0.80 (0.67–0.94); P = 0.009] or cardiovascular disease [0.82 (0.67–0.99);
P = 0.048] was significantly lower in NP-guided patients with no heterogeneity between studies and no interaction
with age or LVEF.

 

Diagnostic and prognostic evaluation of left ventricular systolic heart failure by plasma N-terminal
pro-brain natriuretic peptide concentrations in a large sample of the general population

BA Groenning, I Raymond, PR Hildebrandt, JC Nilsson, M Baumann, F Pedersen.
Heart 2004; 90:297–303.  http://dx.doi.org:/10.1136/hrt.2003.026021

Value of NT-proBNP in evaluating patients with symptoms of heart failure and impaired left ventricular (LV) systolic
function; prognostic value of NT-proBNP for mortality and hospital admissions. In 38 (5.6%) participants LV ejection
fraction (LVEF) was ( 40%. NT-proBNP identified patients with symptoms of heart failure and LVEF ( 40% with a
sensitivity of 0.92, a specificity of 0.86, AUC of 0.94.  NT-proBNP was the strongest independent predictor of mortality
(hazard ratio (HR) = 5.70, p , 0.0001), hospital admissions for heart failure (HR = 13.83, p , 0.0001), and other cardiac
admissions (HR = 3.69, p , 0.0001). Mortality (26 v 6, p = 0.0003), heart failure admissions (18 v 2, p = 0.0002), and
admissions for other cardiac causes (44 v 13, p , 0.0001) were significantly higher in patients with NTproBNP above the
study median (32.5 pmol/l).

 

Testing for BNP and NT-proBNP in the Diagnosis and Prognosis of Heart Failure
Evidence Report/Technology Assessment – Number 142. Agency for Healthcare Research and Quality.
Prepared by: McMaster University Evidence-based Practice Center, Hamilton, ON, Canada
C Balion, PL. Santaguida, S Hill, A Worster, M McQueen, et al.
http://archive.ahrq.gov/downloads/pub/evidence/pdf/bnp/bnp.pdf

Question 1: What are the determinants of both BNP and NT-proBNP?
Question 2a: What are the clinical performance characteristics of both BNP and NTproBNP
measurement in patients with symptoms suggestive of HF or with known HF?
Question 2b: Does measurement of BNP or NT-proBNP add independent diagnostic information
to the traditional diagnostic measures of HF in patients with suggestive HF?
Question 3a: Do BNP or NT-proBNP levels predict cardiac events in populations at risk of CAD,
with diagnosed CAD and HF?
Question 3b: What are the screening performance characteristics of BNP or NT-proBNP in
general asymptomatic populations?
Question 4: Can BNP or NT-proBNP measurement be used to monitor response to therapy?        

Diagnosis: In all settings both BNP and NT-proBNP show good diagnostic properties as a rule out test for HF.
Prognosis: BNP and NT-proBNP are consistent independent predictors of mortality and other cardiac composite
endpoints for populations with risk of CAD, diagnosed CAD, and diagnosed HF. There is insufficient evidence to
determine the value of B-type natriuretic peptides for screening of HF.
Monitoring Treatment: There is insufficient evidence to demonstrate that BNP and NT-proBNP levels
show change in response to therapies to manage stable chronic HF patients.

Guide-IT Trial

Biomarker-Guided HF Therapy: Is It Cost-Effective
www.medscape.org/viewarticle/764686_transcript

Jan 29, 2013 – Uploaded by DCLRI
Michael Felker, MD, MHS
Associate Professor in the Division of Cardiology
Duke University Medical Center
www.youtube.com/watch?v=AW0480EE2kw

GUIDE-IT will last five years and involve approximately 45 trial sites in the United States. The first group of
patients will be enrolled by the end of 2012.

The trial tests NT-proBNP guided therapy with a COMPANION diagnostic biomarker used to optimize already
available and effective therapies for heart failure. It may identify  patients who will benefit from intensified therapy,
and  who would not have been known using only signs and symptoms of heart failure as it is currently the practice.
The NT-proBNP biomarker would enable doctors to create personalized treatment plans for patients to substantially
reduce mortality and morbidity

 Risk stratification in acute heart failure: Rationale and design of the
STRATIFY and DECIDE studies 

SP. Collins, CJ. Lindsell, CA. Jenkins, FE. Harrell, et al.
Am Heart J 2012;164:825-34.
http://dx.doi.org/10.1016/j.ahj.2012.07.033

Two studies (STRATIFY and DECIDE) have been funded by the National Heart Lung and Blood Institute with
the goal of developing prediction rules to facilitate early decision making in AHF. Using prospectively gathered
evaluation and treatment data from the acute setting (STRATIFY) and early inpatient stay (DECIDE), rules will
be generated to predict risk for death and serious complications.
A rigorous analysis plan has been developed to construct the prediction rules that will maximally extract both the
statistical and clinical properties of every data element. Upon completion of this study we will subsequently externally
test the prediction rules in a heterogeneous patient cohort.

N-terminal pro-B-type natriuretic peptide and the prediction of primary cardiovascular
events: results from 15-year follow-up of WOSCOPS

P Welsh, O Doolin, P Willeit, C Packard, P Macfarlane, S Cobbe, et al.
Eur Heart J Aug  2012.
http://dx.doi.org:/10.1093/eurheartj/ehs239

To test whether N-terminal pro-B-type natriuretic peptide (NT-proBNP) was independently associated with, and
improved the prediction of, cardiovascular disease (CVD) in a primary prevention cohort. N-terminal pro-B-type
natriuretic peptide predicts CVD events in men without clinical evidence of CHD, angina, or history of stroke,
and appears related more strongly to the risk for fatal events.
NT-proBNP was associated with an increased risk of all CVD [HR: 1.17 (95% CI: 1.11–1.23) per standard deviation
increase in log NT-proBNP] after adjustment for classical and clinical cardiovascular risk factors plus C-reactive protein.
N-terminal pro-B-type natriuretic peptide was more strongly related to the rsk of fatal [HR: 1.34 (95% CI: 1.19–1.52)]
than non-fatal CVD [HR: 1.17 (95% CI: 1.10–1.24)] (P = 0.022). The addition of NT-proBNP to traditional risk factors
improved the C-index (+0.013; P = 0.001). The continuous net reclassification index improved with the addition of NT-
proBNP by 19.8% (95% CI: 13.6–25.9%) compared with 9.8% (95% CI: 4.2–15.6%) with the addition of C-reactive protein.

 

Utility of B-Natriuretic Peptide in Detecting Diastolic Dysfunction: Comparison With
Doppler Velocity Recordings
E Lubien, A DeMaria, P Krishnaswamy, P Clopton, J Koon…A Maisel.
http://circ.ahajournals.org/content/105/5/595
Circulation. 2002;105:595-601
http://dx.doi.org:/10.1161/hc0502.103010

Although Doppler echocardiography has been used to identify abnormal left ventricular (LV) diastolic filling dynamics,
inherent limitations suggest the need for additional measures of diastolic dysfunction. Because data suggest that B-natriuretic
peptide (BNP) partially reflects ventricular pressure, we hypothesized that BNP levels could predict diastolic abnormalities
in patients with normal systolic function. A rapid assay for BNP can reliably detect the presence of diastolic abnormalities
on echocardiography. In  patients with normal systolic function, elevated BNP levels and diastolic filling abnormalities might
help to reinforce the diagnosis diastolic dysfunction

Association of common variants in NPPA and NPPB with circulating natriuretic
peptides and blood pressure.
C Newton-Cheh, MG Larson, RS Vasan, D Levy, KD Bloch, et al.
Nat Genet. 2009 Mar; 41(3): 348–353.
http://dx.doi.org:/10.1038/ng.328

We examined the association of common variants at the NPPA-NPPB locus with circulating concentrations of the
natriuretic peptides, which have blood pressure–lowering properties. In 29,717 individuals, the alleles of rs5068
and rs198358 that showed association with increased circulating natriuretic peptide concentrations were also found
to be associated with lower systolic (P = 2 ×10−6 and 6 × 10−5, respectively) and diastolic blood pressure (P = 1 × 10−6
and 5 × 10−5), as well as reduced odds of hypertension (OR = 0.85, 95% CI = 0.79–0.92, P = 4 × 10−5; OR = 0.90, 95%
CI = 0.85–0.95, P = 2 × 10−4, respectively).

2013 ACC/AHA Guideline on the Assessment of Cardiovascular Risk
DC. Goff, Jr, DM. Lloyd-Jones, G Bennett, S Coady, RB. D’Agostino, Sr, et al.
Circulation. 2013;  http://circ.ahajournals.org/content/early/2013/11/11/01.cir.0000437741.48606.98.citation
http://dx.doi.org:/10.1161/01.cir.0000437741.48606.98

The ACC and AHA have collaborated with the National Heart, Lung, and Blood Institute (NHLBI) and stakeholder
and professional organizations to develop clinical practice guidelines for assessment of CV risk, lifestyle modifications
to reduce CV risk, and management of blood cholesterol, overweight and obesity in adults.
Although the Task Force led the final development of these prevention guidelines, they differ from other ACC/AHA
guidelines. First, as opposed to an extensive compendium of clinical information, these documents are significantly
more limited in scope and focus on selected CQs in each topic, based on the highest quality evidence available.
Recommendations were derived from randomized trials, meta-analyses, and observational studies evaluated for quality,
and were not formulated when sufficient evidence was not available. Second, the text accompanying each recommendation
is succinct, summarizing the evidence for each question. Third, the format of the recommendations differs from other
ACC/AHA guidelines. Each recommendation has been mapped from the NHLBI grading format to the ACC/AHA Class
of Recommendation/Level of Evidence (COR/LOE) construct (Table 1) and is expressed in both formats.

 

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