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

Breaching Drug Disclosure on Tresiba been refused U.S. approval – Novo Nordisk A/S (NVO) Reported To Police

Reporter: Aviva Lev-Ari, PhD, RN

SOURCE

http://www.biospace.com/news_story.aspx?NewsEntityId=318189&type=email&source=GP_121013

Novo Nordisk A/S (NVO) Reported To Police For Breaching Drug Disclosure Rules

12/10/2013 7:32:19 AM

Novo Nordisk, the world’s largest insulin maker, is facing a Danish police probe after it was reported by the financial watchdog for not disclosing at once that its big new product hope Tresiba had been refused U.S. approval.

Although the probe is unlikely to have a serious financial impact on the company, the largest by market value in the Nordic region, it may tarnish its reputation and could leave it open to lawsuits from investors in the United States, where its shares also trade.

The Danish Financial Supervisory Authority (FSA) said on Tuesday Novo should have issued a statement about the U.S. decision not to approve Tresiba, its new long-acting insulin, on the evening of Friday, February 8 instead of waiting until Sunday, February 10.

 

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Saudi Human Genome Program, International Barcode of Life Project

Reporter: Aviva Lev-Ari, PhD, RN

Life Tech Becomes Partner in Saudi Human Genome Program, International Barcode of Life Project

December 09, 2013

NEW YORK, GenomeWeb − Life Technologies has become a partner in two research projects, the Saudi Human Genome Program and the International Barcode of Life (iBOL) project, the company said this week. The projects will employ the firm’s Ion Proton, capillary electrophoresis, and PGM sequencing technologies.

The goal of the Saudi Human Genome Project, led by Saudi Arabia’s national funding agency, the King Abdulaziz City for Science and Technology (KACST), is to study the genetic basis of disease in Saudi Arabia and the Middle East.

Over the next five years, the project aims to sequence 100,000 genomes from individuals from the region using Life Tech’s Ion Proton technology. Sequencing will be initially conducted at 10 genome centers across Saudi Arabia, with five additional centers to be created in the future.

Life Tech will design and equip the centers, and provide “end-to-end solutions” and services for operations and informatics. Integrated Gulf Biosystems, Life Tech’s distributor in the Middle East, said it played a “pivotal role” in bringing Life Tech’s technology to KACST.

Results from the project will be used to build a Saudi-specific database, providing the basis for future personalized medicine in the Kingdom. Specifically, the information is expected to help with premarital and prenatal screening for rare genetic diseases, as well as for population studies.

SOURCE

http://www.genomeweb.com//node/1321146?utm_source=SilverpopMailing&utm_medium=email&utm_campaign=Management%20Shakeup%20at%20Hologic;%20Life%20Tech%20Partners%20on%20Saudi%20Genome%20Project;%20Cancer%20Driver%20Gene%20Study%20-%2012/09/2013%2010:50:00%20AM

 

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Silencing Cancers with Synthetic siRNAs

Larry H. Bernstein, MD, FCAP, Reviewer and Curator

Article ID #91: Silencing Cancers with Synthetic siRNAs. Published on 12/9/2013

WordCloud Image Produced by Adam Tubman

http://pharmaceuticalinnovation.com/2012-12-09/larryhbern/Silencing Cancers with Synthetic siRNAs

The challenge of cancer drug development has been marker by less than a century of development of major insights into the know of biochemical pathways and the changes in those pathways in a dramatic shift in enrgy utilization and organ development, and the changes in those pathways with the development of malignant neoplasia.  The first notable change is the Warburg Effect (attributed to the 1860 obsevation by Pasteur that yeast cells use glycolysis under anaerobic conditions).  Warburg also referred to earlier work by Meyerhoff, in a ratio of CO2 release to O2 consumption, a Meyerhoff ratio.  Much more was elucidated after the discovery of the pyridine nucleotides, which gave understanding of glycolysis and lactate production with a key two enzyme separation at the forward LDH reaction and the back reentry to the TCA cycle.  But the TCA cycle could be used for oxidative energy utilization in the mitochondria by oxidative phosphorylation elucidated by Peter Mitchell, or it can alternatively be used for syntheses, like proteins and lipid membrane structures.

A brilliant student in Leloir’s laboratory in Brazil undertook a study of isoenzyme structure in 1971, at a time that I was working under Nathan O. Kaplan on the mechanism of inhibition of mitochondrial malate dehydrogenase. In his descripton, taking into account the effect of substrates upon protein stability (FEBS) could be, in a prebiotic system, the form required in order to select protein and RNA in parallel or in tandem in a way that generates the genetic code (3 bases for one amino acid). Later, other proteins like reverse transcriptase, could transcribe it into the more stable DNA. Leloir had just finished ( a few years before 1971 but, not published by these days yet) a somehow similar reasoning about metabolic regions rich in A or in C or .. G or T.  He later spent time in London to study the early events in the transition of growing cells linked to ion fluxes, which he was attracted to by the idea that life is so strongly associated with the K (potassium) and Na (sodium) asymmetry.   Moreover, he notes that while DNA is the same no matter the cell is dead or alive,  and therefore,  it is a huge mistake to call DNA the molecule of life. In all life forms, you will find K reach inside and Na rich outside its membrane. On his return to Brazil, he accepted a request to collaborate with the Surgery department in energetic metabolism of tissues submitted to ischemia and reperfusion. This led me back to Pasteur and Warburg effects and like in Leloir´s time, he worked with a dimorphic yeast/mold that was considered a morphogenetic presentation of the Pasteur Effect.  His findings were as follows. In absence of glucose, a condition that prevents the yeast like cell morphology, which led to the study of an enzyme “half reaction”. The reaction that on the half, “seen in our experimental conditions did not followed classical thermodynamics” (According to Collowick & Kaplan (of your personal knowledge) vol. I See Utter and Kurahashi in it). This somehow contributed to a way of seeing biochemistry with modesty. The second and more strongly related to the Pasteur Effect was the use an entirely designed and produced in our Medical School Coulometer spirometer that measures oxygen consumption in a condition of constant oxygen supply. At variance with Warburg apparatus and Clark´s electrode, this oxymeters uses decrease in partial oxygen pressure and decrease electrical signal of oxygen polarography to measure it (Leite, J.V.P. Research in Physiol. Kao, Koissumi, Vassali eds Aulo Gaggi Bologna, 673-80-1971). “With this, I was able to measure the same mycelium in low and high “cell density” inside the same culture media. The result shows, high density one stops mitochondrial function while low density continues to consume oxygen (the internal increase or decrease in glycogen levels shows which one does or does not do it). Translation for today: The same genome in the same chemical environment behave differently mostly likely by its interaction differences. This previous experience fits well with what  I have to read by that time of my work with surgeons.  Submitted to total ischemia tissues mitochondrial function is stopped when they already have enough oxyhemoglobin (1) Epstein, Balaban and Ross Am J Physiol.243, F356-63 (1982) 2) Bashford , C. L, Biological membranes a practical approach Oxford Was. P 219-239 (1987).”

Of course, the world of medical and pharmaceutical engagement with this problem, though changed in focus, has benefitted hugely from “The Human Genome Project”, and the events since the millenium, because of technology advances in instrumental analysis, and in bioinformatics and computational biology.  This has lead to recent advances in regenerative biology with stem cell “models”, to advances in resorbable matrices, and so on.  We proceed to an interesting work that applies synthetic work with nucleic acid signaling to pharmacotherapy of cancer.

Synthetic RNAs Designed to Fight Cancer

Fri, 12/06/2013 Biosci Technology
Xiaowei Wang and his colleagues have designed synthetic molecules that combine the advantages of two experimental RNA therapies against cancer. (Source: WUSTL/Robert J. Boston)In search of better cancer treatments, researchers at Washington University School of Medicine in St. Louis have designed synthetic molecules that combine the advantages of two experimental RNA therapies.  The study appears in the December issue of the journal RNA.
 RNAs play an important role in how genes are turned on and off in the body. Both siRNAs and microRNAs are snippets of RNA known to modulate a gene’s signal or shut it down entirely. Separately, siRNA and microRNA treatment strategies are in early clinical trials against cancer, but few groups have attempted to marry the two.   “These are preliminary findings, but we have shown that the concept is worth pursuing,” said Xiaowei Wang, assistant professor of radiation oncology at the School of Medicine and a member of the Siteman Cancer Center. “We are trying to merge two largely separate fields of RNA research and harness the advantages of both.”
 “We designed an artificial RNA that is a combination of siRNA and microRNA, The showed that the artificial RNA combines the functions of the two separate molecules, simultaneously inhibiting both cell migration and proliferation. They designed and assembled small interfering” RNAs, or siRNAs,  made to shut down– or interfere with– a single specific gene that drives cancer.  The siRNA molecules work extremely well at silencing a gene target because the siRNA sequence is made to perfectly complement the target sequence, thereby
  • silencing a gene’s expression.
Though siRNAs are great at turning off the gene target, they also have potentially dangerous side effects:
  • siRNAs inadvertently can shut down other genes that need to be expressed to carry out tasks that keep the body healthy.
 According to Wang and his colleagues, siRNAs interfere with off-target genes that closely complement their “seed region,” a short but important
  • section of the siRNA sequence that governs binding to a gene target.
 “We can never predict all of the toxic side effects that we might see with a particular siRNA,” said Wang. “In the past, we tried to block the seed region in an attempt to reduce the side effects. Until now,
  • we never tried to replace the seed region completely.”
 Wang and his colleagues asked whether
  • they could replace the siRNA’s seed region with the seed region from microRNA.
Unlike siRNA, microRNA is a natural part of the body’s gene expression. And it can also shut down genes. As such, the microRNA seed region (with its natural targets) might reduce
  • the toxic side effects caused by the artificial siRNA seed region. Plus,
  • the microRNA seed region would add a new tool to shut down other genes that also may be driving cancer.
 Wang’s group started with a bioinformatics approach, using a computer algorithm to design
  • siRNA sequences against a common driver of cancer,
  • a gene called AKT1 that encourages uncontrolled cell division.
They used the program to select siRNAs against AKT1 that also had a seed region highly similar to the seed region of a microRNA known to inhibit a cell’s ability to move, thus
  • potentially reducing the cancer’s ability to spread.
In theory, replacing the siRNA seed region with the microRNA seed region also would combine their functions
  • reducing cell division and
  • movement with a single RNA molecule.
 Of more than 1,000 siRNAs that can target AKT1,
  • they found only three that each had a seed region remarkably similar to the seed region of the microRNA that reduces cell movement.
 They then took the microRNA seed region and
  • used it to replace the seed region in the three siRNAs that target AKT1.
The close similarity between the two seed regions is required because
  • changing the original siRNA sequence too much would make it less effective at shutting down AKT1.
 They dubbed the resulting combination RNA molecule “artificial interfering” RNA, or aiRNA. Once they arrived at these three sequences using computer models,
  1. they assembled the aiRNAs and
  2. tested them in cancer cells.
 One of the three artificial RNAs that they built in the lab
  • combined the advantages of the original siRNA and the microRNA seed region that was transplanted into it.
This aiRNA greatly reduced both
  1. cell division (like the siRNA) and
  2. movement (like the microRNA).
And to further show proof-of-concept, they also did the reverse, designing an aiRNA that
  1. both resists chemotherapy and
  2. promotes movement of the cancer cells.
 “Obviously, we would not increase cell survival and movement for cancer therapy, but we wanted to show how flexible this technology can be, potentially expanding it to treat diseases other than cancer,” Wang said.
Source: WUSTL

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Larry H Bernstein, MD, FCAP, Reviewer and Curator

http://pharmaceuticalintelligence.com/2013-12-08/larryhbern/Developments-in-the-Genomics-and-Proteomics-of-Type-2-Diabetes-Mellitus-and-Treatment-Targets

Researchers Solve a Mystery about Type 2 Diabetes Drug

AB SCIEX TripleTOF® and QTRAP® technologies support breakthrough medical study.
Published: Friday, November 22, 2013
Researchers from St. Vincent’s Institute of Medical Research in Melbourne, Australia, in collaboration with researchers at McMaster University in Canada, are reportedly the first to discover how the type 2 diabetes drug metformin actually works, providing a molecular understanding that could lead to the development of more effective therapies. Mass spectrometry technologies from AB SCIEX played a critical role in the analysis that led to this breakthrough finding.  The research is published in this month’s issue of the journal Nature Medicine.
Doctors have known for decades that metformin helps treat type 2 diabetes.  However, questions had lingered for more than 50 years whether this drug, which is available as a generic drug,
  • worked to lower blood glucose in patients by directly working on the glucose.
People with type 2 diabetes have high blood sugar levels and have trouble converting sugar in their blood into energy because of low levels of insulin. For treating this condition, metformin is considered the most widely prescribed anti-diabetic drug in the world.
Until now, no one had been able to explain adequately how this drug lowers blood sugar. According to this new study, the drug works by reducing harmful fat in the liver. People who take metformin reportedly often have a fatty liver, which is frequently caused by obesity.
“Fat is likely a key trigger for pre-diabetes in humans,” said Professor Bruce Kemp, PhD, the Head of Protein Chemistry and Metabolism at St. Vincent’s Institute of Medical Research.  “Our study indicates that
  • metformin doesn’t directly reduce sugar metabolism, as previously suspected, but instead
  •  reduces fat in the liver, which in turn allows insulin to work effectively.”
The breakthrough in pinning down how the drug functions began with the researchers making
  • genetic mutations to the genes of two enzymes, ACC1 and ACC2,
in mice, so they could no longer be controlled.  What happened next surprised the researchers:
  • the mice didn’t get fat as expected,
but Associate Professor Gregory Steinberg, PhD at McMaster University noticed that
  • the mice had fatty livers and a pre-diabetic condition.
Then the researchers put the mice on
  • a high fat diet and they became fat, while metformin
  • did not lower the blood sugar levels of the mutant mice.
The findings are expected to help researchers better directly target the condition, which affects over 100 million people around the world, according to published reports. It is also believed that with the mystery of metformin solved, the application of the drug could go beyond just diabetes and potentially be used to treat other medical conditions.
“AB SCIEX mass spectrometry solutions help researchers explore big questions and conduct breakthrough studies, such as this remarkable type 2 diabetes study,” said Rainer Blair, President of AB SCIEX.   “In order to understand disease at the molecular level, researchers need the sensitive detection and reproducible quantitation provided by AB SCIEX tools. We enable the research community to solve biological mysteries and rethink the possibilities to transform health.
For the research conducted by the Australian and Canadian researchers, the analysis at the molecular level was optimized on AB SCIEX instrumentation, including the AB SCIEX TripleTOF® 5600 and the AB SCIEX QTRAP® 5500 system.
The TripleTOF system, with its high-speed, high-quality MS/MS capabilities,
  • was used for the discovery of key proteins and phosphopeptides.
The QTRAP system, with its high sensitivity MRM (multiple reaction monitoring) capabilities,
  • was used for quantitation of metabolites, including nucleotides and malonyl-CoA. 

Bardoxolone Methyl in Type 2 Diabetes and Stage 4 Chronic Kidney Disease

D de Zeeuw, T Akizawa, P Audhya, GL Bakris, M Chin, ….,and GM Chertow, for the BEACON Trial Investigators
Type 2 diabetes mellitus is the most important cause of progressive chronic kidney disease in the developed and developing worlds. Various therapeutic approaches to slow progression, including
  • restriction of dietary protein,
  • glycemic control, and
  • control of hypertension,
have yielded mixed results.1-3 Several randomized clinical trials have shown that
  • inhibitors of the renin–angiotensin–aldosterone system significantly reduce the risk of progression,4-6 although
  • the residual risk remains high.7
None of the new agents tested during the past decade have proved effective in late-stage clinical trials.8-12
Oxidative stress and impaired antioxidant capacity intensify 
  • with the progression of chronic kidney disease.13
In animals with chronic kidney disease,
  • oxidative stress and inflammation
  • are associated with impaired activity of the nuclear 1 factor (erythroid-derived 2)–related factor 2 (Nrf2) transcription factor.
The synthetic triterpenoid bardoxolone methyl and its analogues are the most potent known activators of the Nrf2 pathway. Studies involving humans,14 including persons with type 2 diabetes mellitus and stage 3b or 4 chronic kidney disease, have shown that
  • bardoxolone methyl can reduce the serum creatinine concentration for up to 52 weeks.15
We designed the Bardoxolone Methyl Evaluation in Patients with Chronic Kidney Disease and Type 2 Diabetes Mellitus: the Occurrence of Renal Events (BEACON) trial to test the hypothesis that
  • treatment with bardoxolone methyl reduces the risk of end-stage renal disease (ESRD) or death from cardiovascular causes
among patients with type 2 diabetes mellitus and stage 4 chronic kidney disease.

Methods

Study Design and Oversight

The BEACON trial was a phase 3, randomized, double-blind, parallel-group, international, multicenter trial of
  • once-daily administration of bardoxolone methyl (at a dose of 20 mg in an amorphous spray-dried dispersion formulation), as compared with placebo.
Participants were receiving background conventional therapy that included 
  • inhibitors of the renin–angiotensin–aldosterone system,
  • insulin or other hypoglycemic agents, and, when appropriate,
  • other cardiovascular medications.
The trial design and the characteristics of the trial participants at baseline have been described previously.16,17
Reata Pharmaceuticals sponsored the trial. The trial was jointly designed by employees of the sponsor and the academic investigators who were members of the steering committee. The steering committee, which was led by the academic investigators and included members who were employees of the sponsor, supervised the trial design and operation. An independent data and safety monitoring committee reviewed interim safety data every 90 days or on an ad hoc basis on request. The sponsor collected the trial data and transferred them to independent statisticians at Statistics Collaborative. The sponsor also contracted a second independent statistical group (Axio Research) to support the independent data and safety monitoring committee. The trial protocol was approved by the institutional review board at each participating study site. The protocol and amendments are available with the full text of this article at NEJM.org. The steering committee takes full responsibility for the integrity of the data and the interpretation of the trial results and for the fidelity of the study to the protocol. The first and last authors wrote the first draft of the manuscript. All the members of the steering committee made the decision to submit the manuscript for publication.

Study Population

Briefly, we included adults with 
  • type 2 diabetes mellitus and
  • an estimated glomerular filtration rate (GFR) of 15 to <30 ml per minute per 1.73 m2 BSA.
  1. Persons with poor glycemic control,
  2. uncontrolled hypertension, or
  3. a recent cardiovascular event (≤12 weeks before randomization) or
  4. New York Heart Association class III or IV heart failure were excluded.
Additional inclusion and exclusion criteria are listed in Table S1 in the Supplementary Appendix, available at NEJM.org. All the patients provided written informed consent.

Randomization and Intervention

 Randomization was stratified according to study site with the use of variable-sized blocks. The steering committee, sponsor, investigators, and trial participants were unaware of the group assignments. After randomization,
  • patients received either bardoxolone methyl or placebo.
The prescription of all other medications was at the discretion of treating physicians, who were encouraged to adhere to published clinical-practice guidelines. Patients underwent event ascertainment and laboratory testing according to the study schema shown in Figure S1 in the Supplementary Appendix. Ambulatory blood-pressure monitoring was performed in a substudy that included 174 patients (8%).
The statistical analysis plan defined the study period as the number of days from randomization to a common study-termination date. In the case of patients who were still receiving the study drug on the termination date, data on vital events were collected for an additional 30 days.
Outcomes
 The primary composite outcome was ESRD or death from cardiovascular causes. We defined ESRD as
  • the need for maintenance dialysis for 12 weeks or more or kidney transplantation.
If a patient died before undergoing dialysis for 12 weeks, the independent events-adjudication committee adjudicated whether the need for dialysis represented ESRD or acute renal failure. Patients who declined dialysis and who subsequently died were categorized as having had ESRD. All ESRD events were adjudicated. Death from cardiovascular causes was defined as death due to either cardiovascular or unknown causes.
The trial had three prespecified secondary outcomes —
  1. first, the change in estimated GFR as calculated with the use of the four-variable Modification of Diet in Renal Disease study equation, with serum creatinine levels calibrated to an isotope-dilution standard for mass spectrometry;
  2. second, hospitalization for heart failure or death due to heart failure; and
  3. third, a composite outcome of nonfatal myocardial infarction, nonfatal stroke, hospitalization for heart failure, or death from cardiovascular causes.

The events-adjudication committee, whose members were unaware of the study assignments, evaluated whether

  • ESRD events,
  • cardiovascular events,
  • neurologic events, and
  • deaths
met the prespecified criteria for primary and secondary outcomes (described in detail in the Supplementary Appendix).
Statistical Analysis
We calculated that we needed to enroll 2000 patients on the basis of the following assumptions:

  • a two-sided type I error rate of 5%, an event rate of 24% for the primary composite outcome in the placebo group during the first 2 years of the study,
  • a hazard ratio of 0.68 (bardoxolone methyl vs. placebo) for the primary composite outcome,
  • discontinuation of the study drug by 13.5% of the patients in the bardoxolone methyl group each year, and
  • a 2.5% annual loss to follow-up in each group.

Under these assumptions, if 300 patients had a primary composite outcome, the statistical power would be 85%.

We collected and analyzed all outcome data in accordance with the intention-to-treat principle. We calculated Kaplan–Meier product-limit estimates of
  • the cumulative incidence of the primary composite outcome.
We computed hazard ratios and 95% confidence intervals with the use of Cox proportional-hazards regression models with adjustment for

  • the baseline estimated GFR and urinary albumin-to-creatinine ratio.

We performed analogous analyses for secondary time-to-event outcomes. Given the abundance of early adverse events, we also report discrete cumulative incidences at 4 weeks and 52 weeks.

For longitudinal analyses of estimated GFR, we performed mixed-effects regression analyses using

  1. study group,
  2. time,
  3. the interaction of study group with time,
  4. estimated GFR at baseline,
  5. the interaction of baseline estimated GFR with time, and
  6. urinary albumin-to-creatinine ratio as covariates, and
  7. we compared the means between the bardoxolone methyl group and the placebo group.
We adopted similar approaches when examining the effects of treatment on other continuous measures assessed at multiple visits. Since the between-group difference in the primary composite outcome was not significant,
secondary and other outcomes with P values of less than 0.05 were considered to be nominally significant.
Statistical analyses were performed with the use of SAS software, version 9.3 (SAS Institute). Additional details of the statistical analysis are provided in the Supplementary Appendix.

Results

Patients

From June 2011 through September 2012, a total of 2185 patients underwent randomization, including 1545 (71%) in the United States, 334 (15%) in the European Union, 133 (6%) in Australia, 87 (4%) in Canada, 46 (2%) in Israel, and 40 (2%) in Mexico. Figure S2 in the Supplementary Appendix shows the disposition of the study participants.
As shown in Table 1Table 1Baseline Characteristics of the Patients in the Intention-to-Treat Population., the patients were diverse with respect to age, sex, race or ethnic group, and region of origin;
  • diabetic retinopathy and neuropathy were common conditions among the patients,
  • as was overt cardiovascular disease.
See Table S2 in the Supplementary Appendix for a more detailed description of the characteristics of the patients at baseline; Figure S3 in the Supplementary Appendix shows the distribution of baseline estimated GFR and urinary albumin-to-creatinine ratio.
Drug Exposure
The median duration of exposure to the study drug was 7 months (interquartile range, 3 to 11) among patients randomly assigned to bardoxolone methyl and
  • 8 months (interquartile range, 5 to 11) among those randomly assigned to placebo.
Figure S4 in the Supplementary Appendix shows the time to discontinuation of the study drug. Table S3 in the Supplementary Appendix shows the reasons that patients discontinued the study drug and the reasons that patients discontinued the study.
  • The median duration of follow-up was 9 months in both groups.

Outcomes

Primary Composite Outcome
A total of 69 of 1088 patients (6%) randomly assigned to bardoxolone methyl and 69 of 1097 (6%) randomly assigned to placebo had a primary composite outcome (hazard ratio in the bardoxolone methyl group vs. the placebo group, 0.98; 95% confidence interval [CI], 0.70 to 1.37; P=0.92) (Figure 1AFigure 1Kaplan–Meier Plots of the Time to the First Event of the Primary Outcome and Its Components.).
  • Death from cardiovascular causes occurred in 27 patients randomly assigned to bardoxolone methyl and in 19 randomly assigned to placebo (hazard ratio, 1.44; 95% CI, 0.80 to 2.59; P=0.23) (Figure 1B).
  • ESRD developed in 43 patients randomly assigned to bardoxolone methyl and in 51 randomly assigned to placebo (hazard ratio, 0.82; 95% CI, 0.55 to 1.24; P=0.35) (Figure 1C).

One patient in each group died from cardiovascular causes after the development of ESRD. The mean (±SD) estimated GFR

  • before the development of ESRD was 18.1±8.3 ml per minute per 1.73 m^2 in the bardoxolone methyl group and
  • 14.9±4.0 ml per minute per 1.73 m2 in the placebo group.
Secondary Outcomes
During the study period, 96 patients in the bardoxolone methyl group had heart-failure events (93 patients with at least one hospitalization due to heart failure and 3 patients who died from heart failure without hospitalization),
  • as compared with 55 in the placebo group (55 patients with at least one hospitalization due to heart failure and
  • no patients who died from heart failure without hospitalization) (hazard ratio, 1.83; 95% CI, 1.32 to 2.55; P<0.001) (Figure 2AFigure 2Kaplan–Meier Plots of the Time to the First Event of the Discrete Secondary Outcomes.).
A total of 139 patients in the bardoxolone methyl group, as compared with 86 in the placebo group, had
  • a composite outcome event of nonfatal myocardial infarction, nonfatal stroke, hospitalization for heart failure, or death from cardiovascular causes (hazard ratio, 1.71; 95% CI, 1.31 to 2.24; P<0.001) (Figure 2B).
Incidences of Composite Outcomes and Rates of Death from Any Cause
The cumulative incidences of the primary composite outcome and of the two secondary composite outcomes at 4 weeks and at 52 weeks are shown in Table S4 in the Supplementary Appendix. The rates of death from any cause are shown in Figure S5 in the Supplementary Appendix. From the time of randomization to the end of follow-up, 75 patients died: 44 patients in the bardoxolone methyl group and 31 in the placebo group (hazard ratio, 1.47; 95% CI, 0.93 to 2.32; P=0.10). The causes of death are listed in Table S5 in the Supplementary Appendix.

Estimated GFR

Patients randomly assigned to placebo had a significant mean decline in the estimated GFR from the baseline value (−0.9 ml per minute per 1.73 m2; 95% CI, −1.2 to −0.5), whereas those randomly assigned to bardoxolone methyl had a significant mean increase from the baseline value (5.5 ml per minute per 1.73 m2; 95% CI, 5.2 to 5.9). The difference between the two groups was 6.4 ml per minute per 1.73 m2 (95% CI, 5.9 to 6.9; P<0.001) (Figure 3AFigure 3Estimated Glomerular Filtration Rate (GFR), Body Weight, and Urinary Albumin-to-Creatinine Ratio.).
Physiological Variables
Physiological variables are shown in Table S6 in the Supplementary Appendix. The mean body weight remained stable in the placebo group
  • but declined steadily and substantially in the bardoxolone methyl group (Figure 3B).
There was a significantly smaller decrease from baseline in mean systolic blood pressure in the bardoxolone methyl group than in the placebo group (between-group difference, 1.5 mm Hg [95% CI, 0.5 to 2.5]), and
  • the mean diastolic blood pressure increased from baseline in the bardoxolone methyl group whereas it decreased in the placebo group (between-group difference, 2.1 mm Hg [95% CI, 1.6 to 2.6]).
Blood-pressure results from the substudy in which ambulatory blood-pressure monitoring was performed were similar in direction but were more pronounced (between-group difference of 7.9 mm Hg [95% CI, 3.8 to 12.0] in systolic blood pressure and 3.2 mm Hg [95% CI, 1.3 to 5.2] in diastolic blood pressure).
  • Heart rate also increased significantly in the bardoxolone methyl group, as compared with the placebo group (between-group difference, 3.8 beats per minute; 95% CI, 3.2 to 4.4).
Other Laboratory Variables
Data on laboratory variables are shown in Table S7 in the Supplementary Appendix.
  • The urinary albumin-to-creatinine ratio increased significantly in the bardoxolone methyl group, as compared with the placebo group (Figure 3C).
  • Serum magnesium, albumin, hemoglobin, and glycated hemoglobin levels decreased significantly in the bardoxolone methyl group, as compared with the placebo group.
  • The level of B-type natriuretic peptide increased significantly by week 24 in the bardoxolone methyl group, as compared with the placebo group.
Adverse Events
The rates of serious adverse events are summarized in Table 2Table 2Most Commonly Reported Serious Adverse Events in the Intention-to-Treat Population. Serious adverse events occurred more frequently in the bardoxolone methyl group than in the placebo group (717 events in 363 patients vs. 557 events in 295 patients). There were 11 neoplastic events in the bardoxolone methyl group and 10 in placebo group. The most commonly reported adverse events are summarized in Table S8 in the Supplementary Appendix.

Discussion

The current trial was designed to determine whether bardoxolone methyl, an activator of the cytoprotective Nrf2 pathway, would reduce the risk of ESRD
  • among patients with type 2 diabetes mellitus and stage 4 chronic kidney disease
  • who were receiving guideline-based conventional therapy.
The trial was terminated early because of safety concerns, driven primarily by an increase in cardiovascular events in the bardoxolone methyl group. Bardoxolone methyl did not lower the risk of ESRD or of death from cardiovascular causes, although too few events occurred during the trial to reliably determine the true effect of the drug on the primary composite outcome.
Given the truncated duration of the trial and the number of adjudicated events (46% of the events planned), and assuming no change in any of the original assumptions, we estimated the conditional power of the trial to be less than 40%. Although patients treated with bardoxolone methyl had a significant increase in the estimated GFR, as compared with those who received placebo,
  • there was a significantly higher incidence of heart failure and of the composite outcome of nonfatal myocardial infarction, nonfatal stroke, hospitalization for heart failure, or death from cardiovascular causes in the bardoxolone methyl group.
  • There were numerically more deaths from any cause among patients treated with bardoxolone methyl than among those in the placebo group.
Bardoxolone methyl is among the first orally available antioxidant Nrf2 activators. A small previous study showed that bardoxolone methyl
  • reduced inflammation and oxidative stress13 and
  • induced a decline in the serum creatinine level.
In the 52-Week Bardoxolone Methyl Treatment: Renal Function in CKD/Type 2 Diabetes (BEAM) trial,15 227 patients with type 2 diabetes mellitus and an estimated GFR of 20 to 45 ml per minute per 1.73 m2
  • had a significant increase in the estimated GFR (mean change, 8.2 to 11.4 ml per minute per 1.73 m2, depending on the dose group)
  • that was sustained over the entire trial period.
Muscle spasms and hypomagnesemia were the most common adverse events;
  • there was no increase in the rate of heart failure or other cardiovascular events.
The current trial was designed to determine whether the change in estimated GFR that we anticipated on the basis of the results of the BEAM trial would translate into a slower progression toward ESRD. Although in the current trial ESRD developed in fewer patients in the bardoxolone methyl group than in the placebo group, the early termination of the trial precludes conclusion of the effect on ESRD events.
The mechanism linking bardoxolone methyl to heart failure is unknown. Since an excess in heart-failure events was unanticipated, echocardiography was not performed routinely before randomization. Although weight declined significantly in the bardoxolone methyl group, we were unable to determine whether there was loss of body fat, intracellular (skeletal muscle) water, or extracellular (interstitial) water.
The fall in serum albumin and hemoglobin levels may reflect hemodilution caused by fluid retention.
Bardoxolone methyl also increased blood pressure.
An increase in preload due to volume expansion and an increase in afterload (as reflected by increased blood pressure),
  • coupled with an increase in heart rate,
  • constitute a potentially potent combination of factors that are likely to precipitate heart failure in an at-risk population.
The rise in the level of B-type natriuretic peptide with bardoxolone methyl
  • is consistent with an increase in left ventricular wall stress owing to one or more of these mediators or to unrecognized factors such as
  • impaired diastolic filling of the left ventricle.
After recognizing the initial increase in heart-failure events, the independent data and safety monitoring committee tried to identify
  • clinical characteristics that were associated with patients who were at elevated risk for heart failure
  • after the initiation of bardoxolone methyl therapy (with the possibility of modifying eligibility criteria or otherwise altering the trial),
but the committee was unable to do so. Other, noncardiovascular adverse events were also observed more frequently among patients exposed to bardoxolone methyl than among those who received placebo. Whether the effects of Nrf2 activation, or one or more counterregulatory responses, rendered this particular population vulnerable, is unknown. Zoja et al.18 found an increase in albuminuria and blood pressure along with weight loss in Zucker diabetic fatty rats treated with an analogue of bardoxolone methyl; these effects were not observed in other studies in Zucker diabetic fatty rats or other rodent models or in 1-year toxicologic studies in monkeys.19-21
Why were these adverse effects identified in the current trial and not in the BEAM trial?
  1. First, the number of patient-months of drug exposure in the current trial was roughly 10 times that in the BEAM trial.
  2. Second, the population in the present trial had more severe chronic kidney disease than did the population in the BEAM trial.
Observational studies have shown significantly higher rates of death and cardiovascular events, including heart failure,
  • among patients with stage 4 chronic kidney disease than among patients with stage 3 chronic kidney disease.22
Finally, our trial used an amorphous spray-dried dispersion formulation of bardoxolone methyl at a fixed dose rather than at an adjusted dose. We chose the 20-mg dose and the specific formulation used in the BEACON trial
  1. on the basis of four phase 2 studies of chronic kidney disease (three studies used the crystalline formulation, and one used the amorphous formulation),
  2. a crossover pharmacokinetics study involving humans that used both formulations, and
  3. several studies in animals that used both formulations (Meyer C: personal communication),
to provide an activity and safety profile that was similar to that observed with 75 mg of the crystalline formulation, which was one of the dose levels tested in the BEAM trial.
In conclusion, among patients with type 2 diabetes mellitus and stage 4 chronic kidney disease, bardoxolone methyl did not reduce the risk of the primary composite outcome of ESRD or death from cardiovascular causes. Significantly increased risks of heart failure and of the composite cardiovascular outcome (nonfatal myocardial infarction, nonfatal stroke, hospitalization for heart failure, or death from cardiovascular causes) prompted termination of the trial.
Alto, CA 93034, or at gchertow@stanford.edu.
Investigators in the Bardoxolone Methyl Evaluation in Patients with Chronic Kidney Disease and Type 2 Diabetes Mellitus: the Occurrence of Renal Events (BEACON) trial are listed in the Supplementary Appendix, available at NEJM.org.
Table 1. Baseline Characteristics of the Patients in the Intention-to-Treat Population.

Fig 1. Kaplan–Meier Plots of the Time to the First Event of the Primary Outcome and Its Components.

nejmoa1303154_f1   Kaplan–Meier Plot of Cumulative Probabilities of the Primary and Secondary End Points and Death.

Fig 2. Kaplan–Meier Plots of the Time to the First Event of the Discrete Secondary Outcomes

nejmoa1303154_f2  Kaplan–Meier Plot of Cumulative Probabilities of Acute Kidney Injury and Hyperkalemia
Fig 3.  Estimated Glomerular Filtration Rate (GFR), Body Weight, and Urinary Albumin-to-Creatinine Ratio
Table 2  Most Commonly Reported Serious Adverse Events in the Intention-to-Treat Population

References

    1  Klahr S, Levey AS, Beck GJ, et al. The effects of dietary protein restriction and blood-pressure control on the progression of chronic renal disease. N Engl J Med 1994;330:877-884
    2  The ADVANCE Collaborative Group. Intensive blood glucose control and vascular outcomes in patients with type 2 diabetes. N Engl J Med 2008;358:2560-2572
    3  Parving HH, Andersen AR, Smidt UM, Svendsen PA. Early aggressive antihypertensive treatment reduces rate of decline in kidney function in diabetic nephropathy. Lancet 1983;1:1175-1179
    4  Brenner BM, Cooper ME, de Zeeuw D, et al. Effects of losartan on renal and cardiovascular outcomes in patients with type 2 diabetes and nephropathy. N Engl J Med 2001;345:861-869
    5 Lewis EJ, Hunsicker LG, Clarke WR, et al. Renoprotective effect of the angiotensin-receptor antagonist irbesartan in patients with nephropathy due to type 2 diabetes. N Engl J Med 2001;345:851-860
   6  Parving HH, Lehnert H, Brochner-Mortensen J, Gomis R, Andersen S, Arner P. The effect of irbesartan on the development of diabetic nephropathy in patients with type 2 diabetes. N Engl J Med 2001;345:870-878
    7  Heerspink HJ, de Zeeuw D. The kidney in type 2 diabetes therapy. Rev Diabet Stud 2011;8:392-402
    8  Pfeffer MA, Burdmann EA, Chen CY, et al. A trial of darbepoetin alfa in type 2 diabetes and chronic kidney disease. N Engl J Med 2009;361:2019-2032
    9   Parving HH, Brenner BM, McMurray JJ, et al. Cardiorenal end points in a trial of aliskiren for type 2 diabetes. N Engl J Med 2012;367:2204-2213
    10   Packham DK, Wolfe R, Reutens AT, et al. Sulodexide fails to demonstrate renoprotection in overt type 2 diabetic nephropathy. J Am Soc Nephrol 2012;23:123-130
Combined Angiotensin Inhibition for the Treatment of Diabetic Nephropathy
Linda F. Fried, M.D., M.P.H., Nicholas Emanuele, M.D., Jane H. Zhang, Ph.D., Mary Brophy, M.D., Todd A. Conner, Pharm.D., William Duckworth, M.D., David J. Leehey, M.D., Peter A. McCullough, M.D., M.P.H., Theresa O’Connor, Ph.D., Paul M. Palevsky, M.D., Robert F. Reilly, M.D., Stephen L. Seliger, M.D., Stuart R. Warren, J.D., Pharm.D., Suzanne Watnick, M.D., Peter Peduzzi, Ph.D., and Peter Guarino, M.P.H., Ph.D. for the VA NEPHRON-D Investigators
N Engl J Med 2013; 369:1892-1903November 14, 2013DOI: 10.1056/NEJMoa1303154
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Background
Combination therapy with angiotensin-converting–enzyme (ACE) inhibitors and angiotensin-receptor blockers (ARBs) decreases proteinuria; however, its safety and effect on the progression of kidney disease are uncertain.
Methods
We provided losartan (at a dose of 100 mg per day) to patients with type 2 diabetes, a urinary albumin-to-creatinine ratio (with albumin measured in milligrams and creatinine measured in grams) of at least 300, and an estimated glomerular filtration rate (GFR) of 30.0 to 89.9 ml per minute per 1.73 m2 of body-surface area and then randomly assigned them to receive lisinopril (at a dose of 10 to 40 mg per day) or placebo. The primary end point was the first occurrence of a change in the estimated GFR (a decline of ≥30 ml per minute per 1.73 m2 if the initial estimated GFR was ≥60 ml per minute per 1.73 m2 or a decline of ≥50% if the initial estimated GFR was <60 ml per minute per 1.73 m2), end-stage renal disease (ESRD), or death. The secondary renal end point was the first occurrence of a decline in the estimated GFR or ESRD. Safety outcomes included mortality, hyperkalemia, and acute kidney injury.
Results
The study was stopped early owing to safety concerns. Among 1448 randomly assigned patients with a median follow-up of 2.2 years, there were 152 primary end-point events in the monotherapy group and 132 in the combination-therapy group (hazard ratio with combination therapy, 0.88; 95% confidence interval [CI], 0.70 to 1.12; P=0.30). A trend toward a benefit from combination therapy with respect to the secondary end point (hazard ratio, 0.78; 95% CI, 0.58 to 1.05; P=0.10) decreased with time (P=0.02 for nonproportionality). There was no benefit with respect to mortality (hazard ratio for death, 1.04; 95% CI, 0.73 to 1.49; P=0.75) or cardiovascular events. Combination therapy increased the risk of hyperkalemia (6.3 events per 100 person-years, vs. 2.6 events per 100 person-years with monotherapy; P<0.001) and acute kidney injury (12.2 vs. 6.7 events per 100 person-years, P<0.001).
Conclusions
Combination therapy with an ACE inhibitor and an ARB was associated with an increased risk of adverse events among patients with diabetic nephropathy. (Funded by the Cooperative Studies Program of the Department of Veterans Affairs Office of Research and Development; VA NEPHRON-D ClinicalTrials.gov number, NCT00555217.)
A complete list of investigators in the Veterans Affairs Nephropathy in Diabetes (VA NEPHRON-D) study is provided in the Supplementary Appendix, available at NEJM.org.
Figure 1  Kaplan–Meier Plot of Cumulative Probabilities of the Primary and Secondary End Points and Death.
Figure 2 Kaplan–Meier Plot of Cumulative Probabilities of Acute Kidney Injury and Hyperkalemia

The End of Dual Therapy with Renin–Angiotensin–Aldosterone System Blockade?

Nov 14, 2013       de Zeeuw D.  (Editorial)
 N Engl J Med 2013; 369:1960-1962
Treatment aimed at multiple risk factors and specific markers such as glucose level, blood pressure, body weight, cholesterol levels, and albuminuria has been the main focus to slow cardiovascular and renal risk among patients with diabetes. Among the agents used, those that interrupt the renin–angiotensin–aldosterone system (RAAS) have shown protection that extends beyond decreasing blood pressure. In part, these additional effects may be explained by a decrease in albuminuria.1 Therefore, angiotensin-converting–enzyme (ACE) inhibitors and angiotensin II–receptor blockers (ARBs) have become first-choice drugs in patients with diabetes. Despite some success, the residual cardiovascular and renal risk among patients with diabetes remains

Diabetes: Mouse Studies Point to Kinase as Treatment Target

Published: Nov 24, 2013
By Kristina Fiore, Staff Writer, MedPage Today

Targeting a pathway that plays a major role in both hepatic glucose production and insulin sensitivity may eventually help treat type 2 diabetes, researchers reported.
In a series of experiments in mice, researchers found that inhibition of the kinase CaMKII — or even some of its downstream components — lowered blood glucose and insulin levels, Ira Tabas, MD, PhD, of Columbia University Medical Center in New York City, and colleagues reported online in Cell Metabolism.
The pathway is activated by glucagon signaling in the liver, and appears to have roles in both insulin resistance as well as hepatic glucose production in the liver.
In an earlier study, Tabas and colleagues showed that inhibiting the CaMKII pathway lowered hepatic glucose production by suppressing p38-mediated FoxO1 nuclear localization.
In the current study, they found CaMKII inhibition suppresses levels of the pseudo-kinase TRB3 to improve Akt-phosphorylation, thereby improving insulin sensitivity.
Thus this single pathway targets “two cardinal features of type 2 diabetes — hyperglycemia and defective insulin signaling,” the researchers wrote.
“When we realized we had one common pathway that was responsible for these two disparate processes that, in essence, comprises all of type 2 diabetes, we though it would be an ideal target for new drug therapy,” Tabas told MedPage Today.
Tabas and colleagues conducted several experiments to evaluate the CaMKII pathway.
In one experiment in obese mice, they found that

  • no matter how CaMKII was knocked out, it led to lower blood glucose levels and lower fasting plasma insulin levels in response to a glucose challenge.

The improvements also occurred

  • when they knocked out downstream processes, including p38 and MAPK-activating protein kinase 2 (MK2).

“Thus liver p38 and MK2, like CaMKII, play an important role in the development of hyperglycemia and hyperinsulinemia in obese mice,” they wrote.
In further analyses, the researchers discovered

  • deleting or inhibiting any of these three elements ultimately improved insulin-induced Akt-phosphorylation in obese mice —
  • an important part of improving insulin sensitivity.

And unlike the effects on hepatic glucose production, these changes didn’t occur through effects on FoxO1.
Instead, inhibiting the CaMKII pathway suppressed levels of the pseudo-kinase TRB3, which likely occurred because of suppression of ATF4

  • all of which led to an increase in Akt-phosphorylation and insulin sensitivity.

Indeed, when mice were made to overexpress TRB3, the improvement in phosphorylation disappeared, “indicating that

  • the suppression of TRB3 by CaMKII deficiency is causally important in the improvement in insulin signaling,” they wrote.

As a result, there “appear to be two separate CaMKII pathways,

  • one involved in CaMKII-p38-FoxO1 dependent hepatic glucose production, and
  • the other involved in defective insulin-induced p-Akt,” they wrote.

The findings suggest the possibility of a drug that can target both hyperglycemia and insulin resistance in type 2 diabetes, they said.

Association Between a Genetic Variant Related to Glutamic Acid Metabolism and Coronary Heart Disease in Individuals With Type 2 Diabetes

Lu Qi; Qibin Qi; S Prudente; C Mendonca; F Andreozzi; et al.
JAMA. 2013;310(8):821-828.     http://dx.doi.org/10.1001/jama.2013.276305.

Importance

Diabetes is associated with an elevated risk of coronary heart disease (CHD). Previous studies have suggested that the genetic factors predisposing to excess cardiovascular risk may be different in diabetic and nondiabetic individuals.

Objective

To identify genetic determinants of CHD that are specific to patients with diabetes.

Design, Setting, and Participants

We studied 5 independent sets of CHD cases and CHD-negative controls from the Nurses’ Health Study (enrolled in 1976 and followed up through 2008), Health Professionals Follow-up Study (enrolled in 1986 and followed up through 2008), Joslin Heart Study (enrolled in 2001-2008), Gargano Heart Study (enrolled in 2001-2008), and Catanzaro Study (enrolled in 2004-2010). Included were a total of 1517 CHD cases and 2671 CHD-negative controls, all with type 2 diabetes. Results in diabetic patients were compared with those in 737 nondiabetic CHD cases and 1637 nondiabetic CHD-negative controls from the Nurses’ Health Study and Health Professionals Follow-up Study cohorts. Exposures included 2 543 016 common genetic variants occurring throughout the genome.

Main Outcomes and Measures

Coronary heart disease—defined as fatal or nonfatal myocardial infarction, coronary artery bypass grafting, percutaneous transluminal coronary angioplasty, or angiographic evidence of significant stenosis of the coronary arteries.

Results

A variant on chromosome 1q25 (rs10911021) was consistently associated with CHD risk among diabetic participants,

  • with risk allele frequencies of 0.733 in cases vs 0.679 in controls (odds ratio, 1.36 [95% CI, 1.22-1.51]; P = 2 × 10−8).

No association between this variant and CHD was detected among nondiabetic participants, with risk allele frequencies of 0.697 in cases vs 0.696 in controls (odds ratio, 0.99 [95% CI, 0.87-1.13]; P = .89),

  • consistent with a significant gene × diabetes interaction on CHD risk (P = 2 × 10−4).

Compared with protective allele homozygotes, rs10911021 risk allele

  • homozygotes were characterized by a 32% decrease in the expression of the neighboring glutamate-ammonia ligase (GLUL) gene in human endothelial cells (P = .0048).
  • A decreased ratio between plasma levels of γ-glutamyl cycle intermediates pyroglutamic and glutamic acid was also shown in risk allele homozygotes (P = .029).

Conclusion and Relevance

A single-nucleotide polymorphism (rs10911021) was identified that was significantly associated with CHD among persons with diabetes but not in those without diabetes and was functionally related to glutamic acid metabolism, suggesting a mechanistic link.

Adipocyte Heme Oxygenase-1 Induction Attenuates Metabolic Syndrome In Both Male And Female Obese Mice

Angela Burgess1,2, Ming Li2, Luca Vanella1, Dong Hyun Kim1, Rita Rezzani4, et al.

1Department of Physiology and Pharmacology, University of Toledo, Toledo, OH 43614
2Department of Pharmacology, New York Medical College, Valhalla, NY 10595
3Department of Medicine, New York Medical College, Valhalla, NY 10595
4Department of Biomedical Sciences and Biotechnology, University of Brescia, Brescia, Italy
5Department of Pediatrics and Center for Applied Genomics, Charles University, Prague, Czech Republic
6The Rockefeller University, New York, New York 10065

Hypertension. 2010 December ; 56(6): 1124–1130.    http://dx.doi.org/10.1161/HYPERTENSIONAHA.110.151423

Abstract

Increases in visceral fat are associated with
  • increased inflammation,
  • dyslipidemia,
  • insulin resistance,
  • glucose intolerance and
  • vascular dysfunction.
We examined the effect of the potent heme oxygenase (HO)-1 inducer, cobalt protoporphyrin (CoPP), on regulation of adiposity and glucose levels in both female and male obese mice. Both lean and obese mice were administered CoPP intraperitoneally, (3mg/kg/once a week) for 6 weeks. Serum levels of
  1. adiponectin,
  2. TNFα,
  3. IL-1β and
  4. IL-6, and
  5. HO-1,
  6. PPARγ,
  7. pAKT, and
  8. pMPK protein expression
were measured in adipocytes and vascular tissue . While female obese mice continued to gain weight at a rate similar to controls, induction of HO-1 slowed the rate of weight gain in male obese mice. HO-1 induction led to lowered blood pressure
levels in obese males and females mice similar to that of lean male and female mice.
HO-1 induction also produced a significant decrease in the plasma levels of IL-6, TNF-α, IL-1β and fasting glucose of obese females compared to untreated female obese mice. HO-1 induction
  • increased the number and
  • decreased the size of adipocytes of obese animals.
HO-1 induction increased adiponectin, pAKT, pAMPK, and PPARγ levels in adipocyte of obese animals. Induction of HO-1, in adipocytes was associated with
  • an increase in adiponectin and
  • a reduction in inflammatory cytokines.
These findings offer the possibility of treating not only hypertension, but also other detrimental metabolic consequences of obesity
  • including insulin resistance and dyslipidemia in obese populations
  • by induction of HO-1 in adipocytes.
Introduction
Moderate to severe obesity is associated with increased risk for cardiovascular complications and insulin resistance in humans1, 2 and animals3, 4. Cardiovascular risk is specifically associated with increased intra-abdominal fat. Women in their reproductive years have a higher BMI than males, which largely reflects increased overall subcutaneous adipose tissue or “gynoid” obesity, this is not associated with increased cardiovascular risk5. However, due to increases in visceral fat with aging, after the age of 60 the fat distribution in females more closely resembles that in males6. Increased androgen levels also often occur after the menopausal transition. These changes in visceral fat content and androgen levels correlate with both central obesity and insulin resistance and are an important determinant of cardiovascular risk7.
Heme oxygenase (HO) catalyzes the breakdown of heme, a potentially harmful pro-oxidant, into its products biliverdin and carbon monoxide, with a concomitant release of iron (reviewed in8). While HO-2 is expressed constitutively, HO-1 is inducible in response to oxidative stress and its induction has been reported to normalize vascular and renal function9–11. Further, induction of HO-1 slows weight gain, decreases levels of TNF-α and IL-6 and increases serum levels of adiponectin in obese rats and obese diabetic mice4, 9, 12.
The association observed between HO-1 and adiponectin has led to the proposal of the existence of a cytoprotective HO-1/adiponectin axis4, 13. Previously, L’Abbate et al,14 have shown that induction of HO-1 is associated with a parallel increase in the serum levels of adiponectin, which has well-documented
  1. insulin-sensitizing,
  2. antiapoptotic,
  3. antioxidative and
  4. anti-inflammatory properties.
Adiponectin is an abundant protein secreted from adipocytes. Once secreted, it mediates its actions by binding to a set of receptors, such as
  • adipoR1 and adipoR2, and also
  • through induction of AMPK signaling pathways15, 16.
In addition, increases in adiponectin play a protective role against TNF mediated endothelial activation17.
In this study, we evaluated the effect of CoPP, a potent inducer of HO-1,
  • on visceral and subcutaneous fat distribution in both female and male obese mice.
We show for the first time a resistance to weight reduction upon administration of CoPP in female obese mice but
  • a significant decrease in inflammatory cytokines.
Despite continued obesity,
  1. CoPP normalized blood pressure levels,
  2. decreased circulating cytokines, and
  3. increased insulin sensitivity in obese females.
CoPP treatment of obese mice
  • increased the number and
  • reduced the size of adipocytes.
CoPP treatment of both male and female obese mice reversed the reduction in adiponectin levels seen in obesity. This study suggests that in spite of continued obesity,
  • HO-1 induction in female obese mice serves a protective role against obesity associated metabolic consequences via expansion of healthy smaller insulin-sensitive adipocytes.

Results

Effect of induction of HO-1 on body weight, appearance, and fat content of female and male obese mice. Previously, we have shown CoPP treatment results in the prevention of weight gain in several male models of obesity including obese and db/db mice and Zucker fat rats4, 12. We extended our studies to examine the effect of CoPP on weight gain in female obese mice. CoPP-treatment prevented weight gain in male obese mice when compared to age-matched male controls (Figure S1). The revention of body weight gain was accompanied by a
reduction in visceral fat in male obese mice. However, female obese mice administered CoPP did not lose weight but continued to gain weight at the same rate as untreated female obese mice (Figure S1). This was in spite of food intake being comparable between the two
groups. CoPP administration decreased subcutaneous fat content in both obese males and females (p<0.05; p<0.05, respectively). CoPP produced a decrease (p<0.05) in visceral fat in male but not in female obese mice when compared to untreated obese mice (Figure S1D).
We examined adipocyte size by haematoxilin-eosin staining in both lean, obese and CoPP treated obese female mice (Figure 1A, upper panel). CoPP treatment resulted in a decrease in adipocyte size (p<0.05) compared to untreated obese animals (Figure 1A, lower left panel). We then examined the number of adipocytes in lean, obese and CoPP-treated obese female mice. The number of adipocytes (mean±SE) in lean, obese and CoPP-treated obese animals was 40.83±3.50, 18.33±1.80 and 32.00±1.67 respectively indicating that CoPP treatment of obese mice increased the number of adipocytes to levels similar to those in lean animals (Figure 1A, lower right panel). Similar results were seen in male animals.
The induction of HO-1 was associated with a reduction in blood pressure (BP). Systolic blood pressure in obese female mice was 142 ± 6.5 mm Hg compared to obese-CoPP treated, 109 ± 8.1 mm Hg, p<0.05. The value in obese female mice treated with CoPP is similar to the blood pressure seen in lean female mice (110 ± 9.6 mm Hg). The systolic blood pressure in obese male mice was 144± 4.5 mm Hg compared to obese-CoPP treated, 104 ± 3.6 mm Hg, p<0.05.
We further examined whether CoPP affects HO-1 expression in adipocyte using immunohistochemistry and western blot analysis. Immunostaining showed increased levels of HO-1 (green staining), located on the surface of adipocytes, after CoPP treatment (p<0.05), compared with female obese mice, Figure 1B. As seen in Figure 1C, HO-1 and

HO-2 levels in adipocyte isolated from lean, untreated female obese mice or female obese mice treated with CoPP. Densitometry analysis showed that HO-1 was increased
significantly in female obese mice treated with CoPP, compared to non-treated female obese mice, p<0.05, which is in agreement with immunohistochemistry results. This pattern of HO expression in obesity occurs in other tissues, including aortas, kidneys and hearts of male obese mice4, 13.
Effect of CoPP on HO-1 expression and HO activity in female and male obese mice
HO-1 protein levels were increased by CoPP treatments in liver and renal tissues similar to that seen in adipocytes. Western blot analysis showed significant differences  (p<0.05) in the ratio of HO-1 to actin in renal of male and female obese and lean mice (Figure S 2A). Obesity decreasd HO-1 levels in both sexes when compared to age matched lean animals.
In addition, HO-1 levels were significantly (p<0.05) lower in obese females compared to obese males (Figure S 2A). This reflects a less active HO system in both male and female
obese animals compared to age matched lean controls. Next, we compared the effect of CoPP on male and female HO-1 gene expression in adipocytes. CoPP increased HO-1
expression in both male and female obese animals compared to untreated obese animals (Figure S 2B, p<0.001 and p<0.001, respectively). Similar results of HO-1 expression were seen in liver tissues (Result not shown).
Effect of CoPP on cytokine levels in female and male obese mice
CoPP administration resulted in a significnt increase in the levels of plasma adiponectin in both female (p<0.001) and male obese (p<0.001) mice (Figure 2A). Untreated female obese animals exhibited a significant (p<0.05) increase in plasma IL-6 levels when compared to age-matched male obese mice (Figure 2B). CoPP decreased plasma IL-6 levels in both female and male obese mice (p<0.05A )p<0.01, respectively) when compared to untreated obese miec. Similar results were observed with plasma TNF-α and IL-1β levels (Figure 2C and 2D). These results indicate that though female obese mice exhibited elevated serum levels of inflammatory cytokines compared to male obese mice, CoPP acts with equal efficacy in both female and male obese animals in reducing inflammation while simultaneously increasing serum adiponectin levels (Figure 2). 

Effect of CoPP on blood glucose and LDL levels in female and male obese mice 

Fasting glucose levels were determined after the development of insulin resistance. CoPP produced a decrease in glucose levels in both fasting female (p<0.05) and male (p<0.001) obese mice when compared to untreated obese control animals (Figure 3A). CoPP reduced LDL levels in both male (p<0.01) and female (p<0.05) obese mice when compared to untreated obese controls (Figure 3B). Treatment with SnMP, increased LDL levels. In separate experiments two weeks apart, glucose levels and insulin sensitivity were determined after development of insulin resistance (Fig. 4A and B). Blood glucose levels in female obese mice were elevated (p<0.01) 30 min after glucose administration and remained elevated. In CoPP-treated female obese mice produced a decrease in glucose but not in the vehicle-treated female obese mice (p<0.01).

Effect of Obesity on Protein Expression Levels of pAKT, pAMPK, and PPARγ levels in female and male obese mice

Western blot analysis of adipocytes harvested from fat tissues,showed significant  differences in basal protein expression levels of pAKT and pAMPK in untreated female obese mice compared to untreated obese male mice. pAMPK levels were higher in obese females compared to obese males (Figure 5A, p< 0.05). This was also the case for pAKT protein levels, where increased levels of pAKT were seen in obese females compared to obese males (Figure 5B, p<0.05). CoPP treatment increased pAMPK and pAKT levels in bothe obese females and obese males. In addition, CoPP administration increased PPARγ levels, in both male (p<0.001) and female (p<0.05) obese mice (Figures 5C).

Discussion

In the current study, we show for the first time that induction of HO-1 regulates adiposity in both male and female animals via an increase in adipocyte HO-1 protein levels. A second novel finding is that induction of HO-1 was associated not only with a decrease in adipocyte cell size but with an increase in adipocyte cell number. Further, induction of HO-1 affects visceral and subcutaneous fat distribution and metabolic function in male obese mice differently than in female obese mice. Despite continued obesity, upregulation of HO-1 induced major improvements in the metabolic profile of female obese mice exhibiting symptoms of Type 2 diabetes including: high plasma levels of proinflammatory cytokines, hyperglycemia, dyslipidemia, and low adiponectin levels. CoPP treatment resulted in increased serum adiponectin levels and decreased blood pressure. Adiponectin is exclusively secreted from adipose tissue, and its expression is higher in subcutaneous rather than invisceral adipose tissue. Increased adiponectin levels reduce adipocyte size and increase adipocyte number12, resulting in smaller, more insulin sensitive adipocytes. Adiponectin has recently attracted much attention because it has insulin-sensitizing properties that enhance fatty acid oxidation, liver insulin action, and glucose uptake and positively affect serum trglyceride levels18–21. Levels of circulating adiponectin are inversely correlated with plasma levels of oxidized LDL in patients with Type 2 diabetes and coronary artery disease, which suggests that low adiponectin levels are associated with an increased oxidative state in the arterial wall22. Thus, increases in adiponectin mediated by upregulation of HO-1 may account for improved insulin sensitivity and reduced levels of LDL and inflammatory cytokines (TNF-α, IL-1β, and IL-6 levels) in both male and female mice.

 Females continued to gain weight in spite of the metabolic improvements. One plausible explanation for this anomaly is the direct effects of HO-1 on adiponectin mediating clonal expansion of pre-adipocytes. This supports the concept that expansion of adipogenesis leads to an increased number of adipocytes of smaller cell size; smaller adipocytes are considered to be healthy, insulin sensitive adipocyte cells that are capable of producing adiponectin23. This hypothesis is supported by the increase in the number of smaller adipocytes seen in
CoPP-treated female obese animals without affecting weight gain when compared to female obese animals. Similar results for the presence were seen in males indicating that this effect is not sex specific.
Upregulation of HO-1 was also associated with increased levels of adipocyte pAKT, and pAMPK and PPARγ levels. Previous studies have indicated that insulin resistance and  impaired PI3K/pAKT signaling can lead to the of endothelial dysfunction24. In the current study, increased HO-1 expression was associated with increases in both AKT and AMPK phosphorylation; these actions may protect renal arterioles from insulin mediated endothelial damage. By this mechanism, increased levels of HO-1 limit oxidative stress and facilitate activation of an adiponectin-pAMPK-pAKT pathway and increased insulin sensitivity. Induction of adiponectin and activation of the pAMPK-AKT pathway has been shown to provide vascular protection25, 26. A reduction in AMPK and AKT levels may also explain why inhibition of HO activity in CoPP-treated obese mice  increased inflammatory cytokine levels while decreasing adiponectin. The action of CoPP in increasing pAKT, pAMPK and PPARγ is associated with improved glucose tolerance and decreased insulin resistant.

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Larry, H. Bernstein, MD, FCAP, Author and Curator
Http://pharmaceuticalintelligence.com/2013-12-4/larryhbern/Vitamin_D_-_Binding_Protein_and_Vitamin_D_Status

Vitamin D–Binding Protein and Vitamin D Status of Black Americans and White Americans

CE Powe, MK Evans, J Wenger, AB Zonderman, AH Berg, M Nalls, H Tamez, et al.
N Engl J Med 21 Nov,2013; 369:1991-2000
http://dx.doi.org/10.1056/NEJMoa1306357

Summary

BACKGROUND

Low levels of total 25-hydroxyvitamin D are common among black Americans. Vitamin D–binding protein has not been considered in the assessment of vitamin D deficiency.

METHODS

In the Healthy Aging in Neighborhoods of Diversity across the Life Span cohort of blacks and whites (2085 participants), we measured
  • levels of total 25-hydroxyvitamin D,
  • vitamin D–binding protein, and
  • parathyroid hormone as well as
  • bone mineral density (BMD).

We genotyped study participants for two common polymorphisms in the vitamin D–binding protein gene (rs7041 and rs4588). We estimated levels of bioavailable 25-hydroxyvitamin D in homozygous participants. 

RESULTS

Mean (±SE) levels of both total 25-hydroxyvitamin D and vitamin D–binding protein were lower in blacks than in whites (total 25-hydroxyvitamin D, 15.6±0.2 ng per milliliter vs. 25.8±0.4 ng per milliliter, P<0.001; vitamin D–binding protein, 168±3 μg per milliliter vs. 337±5 μg per milliliter, P<0.001).
  • Genetic polymorphisms independently appeared to explain 79.4% and 9.9% of the variation in levels of vitamin D–binding protein and total 25-hydroxyvitamin D, respectively.
  • BMD was higher in blacks than in whites (1.05±0.01 g per square centimeter vs. 0.94±0.01 g per square centimeter, P<0.001).
  • Levels of parathyroid hormone increased with decreasing levels of total or bioavailable 25-hydroxyvitamin D (P<0.001 for both relationships),
    • yet within each quintile of parathyroid hormone concentration, blacks had significantly lower levels of total 25-hydroxyvitamin D than whites.

Among homozygous participants, blacks and whites had similar levels of bioavailable 25-hydroxyvitamin D overall (2.9±0.1 ng per milliliter and 3.1±0.1 ng per milliliter, respectively; P=0.71) and

  • within quintiles of parathyroid hormone concentration.

CONCLUSIONS

Community-dwelling black Americans, as compared with whites, had low levels of total 25-hydroxyvitamin D and vitamin D–binding protein,
  • resulting in similar concentrations of estimated bioavailable 25-hydroxyvitamin D.

Racial differences in the prevalence of common genetic polymorphisms provide a likely explanation for this observation. (Funded by the National Institute on Aging and others.)

 

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Hyperhomocysteinemia interaction with Protein C and Increased Thrombotic Risk

Reporter and Curator: Larry H Bernstein, MD, FCAP

 

This document explores the relationship between thromboembolic risk related to hyperhomocysteinemia related to the HHcy interaction with and blocking the protective effect of APC.

Previous Venous Thromboembolism Relationships With Plasma Homocysteine Levels

Marco Cattaneo, Franca Franchi, Maddalena L. Zighetti, Ida Martinelli, Daniela Asti, P. Mannuccio Mannucci
Arterioscler Thromb Vasc Biol. 1998;18:1371-1375.
Received January 28, 1998; revision accepted March 16, 1998. From the Angelo Bianchi Bonomi Hemophilia and Thrombosis Center, Institute of Internal Medicine, IRCCS Ospedale Maggiore, University of Milano, Italy.
Correspondence to Marco Cattaneo, MD, Hemophilia and Thrombosis Center, Via Pace 9, 20122 Milano, Italy. E-mail marco.cattaneo@unimi.it © 1998 American Heart Association, Inc. 1371 Original Contributions

Abstract—

The proteolytic enzyme activated protein C (APC) is a normal plasma component, indicating that protein C (PC) is continuously activated in vivo. High concentrations of homocysteine (Hcy) inhibit the activation of PC in vitro;

  • this effect may account for the high risk for thrombosis in patients with hyperhomocysteinemia (HyperHcy).

We measured the plasma levels of APC in 128 patients with previous venous thromboembolism (VTE) and in 98 age- and sex-matched healthy controls and

  • correlated them with the plasma levels of total Hcy (tHcy) measured before and after an oral methionine loading (PML).

Forty- eight patients had HyperHcy and 80 had normal levels of tHcy. No subject was known to have any of the congenital or acquired thrombophilic states at the time of the study.  Because the plasma levels of APC and PC were correlated in healthy controls,  the APC/PC ratios were also analyzed.

Plasma APC levels and APC/PC ratios were significantly higher in VTE patients than in controls (P < 0.03 and 0.0004, respectively).

  • Most of the increase in APC levels and APC/PC ratios were attributable to patients with HyperHcy.

Patients with normal tHcy had intermediate values, which did not differ significantly from those of healthy controls.

  • There was no correlation between the plasma levels of tHcy or its PML increments and APC or APC/PC ratios in controls.
  • The fasting plasma levels of APC and APC/PC ratios of 10 controls did not increase 4 hours PML, despite a 2-fold increase in tHcy.

This study indicates that

  • APC plasma levels are sensitive markers of activation of the hemostatic system in vivo and
  • that Hcy does not interfere with the activation of PC in vivo.

Key Words: homocysteine, protein C, thromboembolism, activated protein C, hypercoagulability,  T mechanism.

The zymogen protein C is converted to the active protease, activated protein C (APC),

  • through proteolytic cleavage by thrombin bound to its endothelial membrane receptor thrombomodulin.1

The demonstration that APC is a normal plasma component,2,3whose enzymatic activity can be detected with specific and sensitive methods,4,5indicates that

  • the protein C anticoagulant pathway is continuously activated in vivo.

Measurement of APC plasma levels might therefore be helpful in determining the in vivo integrity of the protein C anticoagulant pathway. More generally,

  • APC levels might mirror the in vivo activation of the coagulation system and
  • serve as a marker of thrombin activity in the circulation.4

The mechanism(s) by which a moderate elevation of plasma levels of homocysteine (Hcy) increases the risk for arterial and venous thrombotic disease is still unclear.6,7 In vitro studies showed that

  • Hcy inhibits the thrombomodulin- dependent protein C activation to APC and
  • interferes with the expression of thrombomodulin on human umbilical vein endothelial cells.8–10

These findings may be relevant to unravel the thrombogenic mechanism of Hcy, because

the protein C anticoagulant system is of major physiological importance in the regulation of the hemostatic  congenital or acquired disorders

  • characterized by impaired production or function of APC are associated with a high risk for venous thromboembolism (VTE).11

It must be noted, how ever, that these in vitro findings have been obtained by using very high concentrations of Hcy,

  • at least 1 order of magnitude higher than the plasma concentrations found in patients with homozygous homocystinuria.12,13

Their clinical relevance is therefore uncertain and awaits confirmation from ex vivo and/or in vivo studies in humans. In this study, we compared the plasma levels of APC with those of the prothrombin fragment F1,2, a marker of thrombin generation,14in healthy subjects and patients with previous episodes of VTE and

  • tested whether the levels are affected by plasma Hcy concentrations.

Methods

Materials

L-Methionine, tri-n-butylphosphine, 7-fluoro-2,1,3-benzoxadiazole- 4-sulfonamide (ABDF), L-cystine, Tween 20, Tween 80, benzamidine, and HEPES were from Sigma. (4-Amidinophenyl)-methanesulfonylfluoride (APMSF) was from Boehringer, BSA from Calbiochem, and the chromogenic substrate L-homocystine, ovalbumin, S-2366 from Chromogenics. The monoclonal antibody directed against the light chain of protein C (C3-Mab) was a kind gift of Dr H.P. Schwarz (Immuno, Vienna, Austria). All other chemicals were of reagent grade. Subjects We studied 128 patients with previous VTE and 98 healthy controls. All diagnoses of thrombotic episodes, excluding those of superficial veins, had been confirmed by objective methods: compression ultrasonography or venography for deep vein thrombosis; and ventilation/perfusion scintigraphy for pulmonary embolism. The contemporary presence of deep vein thrombosis in patients with superficial vein thrombosis had not been excluded by objective methods. Table 1 shows the characteristics of the patients studied.

They belonged to a cohort of 315 patients who had been screened for thrombophilic states at our Center between December 1993 and July 1995 and were selected on the basis of the following characteristics:
(1) absence of congenital or acquired thrombophilic states except hyperhomocysteinemia (HyperHcy) (see below);
(2) oral anticoagu- lant therapy discontinued at least 1 month before screening;
(3) at least 4 months elapsed since the last thrombotic episode; and
(4) willingness to participate in the study.

The screening for thrombophilia included the following tests:

  • prothrombin time;
  • activated partial thromboplastin time;
  • thrombin time;
  • plasma levels of fibrinogen,
  • protein C,
  • protein S, and
  • antithrombin;
  • APC resistance; and
  • screening for antiphospholipid syndrome15 and
  • plasma levels of total homocysteine (tHcy)

before and 4 hours after an oral methionine load. Patients with abnormal APC resistance were also screened for factor V Leiden.16

The study was designed and completed before the demonstration that the mutation G20210A of the prothrombin gene is a risk factor for deep vein thrombosis.17 This mutation therefore was looked for retrospectively only in those subjects whose DNA was still available for analysis (all controls and 50 patients): 5 patients (10%) and 2 controls (2.1%) were heterozygous for the mutation. Of the 128 patients enrolled in the study,

  • 48 had hyperhomocysteinemia (VTE-HyperHcy) according to the diagnostic criteria outlined below, and
  • 80 had normal Hcy levels (VTE-NormoHcy).
    • The healthy controls, who were age and sex matched with the patients (male/female, 50/45; median age, 40 years [range, 20 to 73 years]), had been chosen from the same geographical area and with the same socioeconomic background as the patients.
  1. Previous episodes of thrombosis had been ruled out by a validated structured questionnaire.18
  2. No subject had abnormal liver or renal function, or overt autoimmune or neoplastic disease.
  3. Informed consent to participate in the study was obtained from all subjects.
  4. The study was approved by the ethics committee of the University of Milano.

Study Protocol

After an overnight fast, blood samples were drawn between 8:30 and 9:30 AM in K3-EDTA for measurement of total Hcy (tHcy), in 0.013 mol/L trisodium citrate for measurement of F1?2 and protein C, and in citrate plus 0.03 mol/L benzamidine (a reversible inhibitor of APC) for measurement of APC. L-Methionine (3.8 g/m2body surface area) was then administered orally in approximately 200 mL of orange juice. Four hours later, a second blood sample was collected in EDTA for tHcy measurement from all subjects and in citrate plus benzamidine for measurement of APC plasma levels from 10 controls. All subjects remained in the fasting state until the second blood sample had been taken. Plasma Hcy Assay Blood samples in K3-EDTA were immediately placed on ice and centrifuged at 2000xG, 4°C, for 15 minutes. The supernatant was stored in aliquots at < 70°C until assay.
The plasma levels of tHcy (free and protein bound) were determined by high-performance liquid chromatography (Waters Millipore 6000A pump, Millipore) and fluorescence detection (Waters 474) by the method of Ubbink et al,19with slight modifications.20 Briefly, 100 uL of plasma was incubated with 10 uL of 10% tri-n-butylphosphine in dimethylfor- mamide at 4°C for 30 minutes to reduce homocystine and mixed disulfide and deconjugate Hcy from plasma proteins. Then, 100 uL of 10% trichloroacetic acid was added, and the mixture was centrifuged in an Eppendorf microcentrifuge at 13 000 rpm for 10 minutes.
After centrifugation, the mixture was incubated with 1 mg/mL ABDF in borate buffer to derivatize the thiols. The mobile phase, pumped at 1 mL/min, consisted of 0.1 mol/L potassium dihydrogenophosphate, 0.06 mmol/L EDTA, and 12% acetonitrile (pH = 2.1).

Criteria for Diagnosis of HyperHcy  HyperHcy was diagnosed when
  1. fasting plasma levels of tHcy or its postmethionine load absolute increments above fasting levels exceeded the 95th percentiles of distribution of values obtained in 388 healthy controls.
Measurement of Plasma APC  Plasma APC levels were measured with < enzyme capture assay, essentially as described by Gruber and Griffin.4 Blood samples were

TABLE 1.
Patients With Previous VTE-NormoHcy

Demographic Characteristics of Patients With Previous VTE-HyperHcy
VTE-HyperHcyVTE-NormoHcy                                                                                                        4880
No. Males/females                                                                                                                                                23/25
Median age, y (range)                                                                                                                                     36 (19–69)
Median age at the first thrombotic episode, y (range)                                                                     32 (17–62)
Time elapsed since last episode, mo (range)                                                                                        14 (4–70)
Time elapsed since discontinuation of oral anticoagulant therapy, mo (range)                   11 (1–64)Type of first thrombotic episode
Deep vein thrombosis                                                                                                                                       31/49
Pulmonary embolism                                                                                                                                    36 (14–62)
Superficial vein thrombosis                                                                                                                       31 (13–60)
Venous thrombosis of other sites                                                                                                           14 (4–90)                                                                                                                                                                          
With 1 or more episodes                                                                                                                              11 (1–70)
2233                                                                                                                                                                    26 (54.2%)
With circumstantial risk factors* at first episode                                                                             44 (55%)
*The following circumstantial risk factors were considered: surgery (26), trauma (50), immobilization (47), pregnancy/puerperium (16,21), and oral contraceptives (22).

1372

Activated Protein C, Thrombosis, and Homocysteine

centrifuged within 60 minutes from collection at 1200xG, 4°C, for 30 minutes to obtain platelet-poor plasma, which was frozen in aliquots at < 70°C. A plasma pool from 30 healthy individuals (15 men, 15 women) was obtained in the same way and used to prepare the standards.
(removed)…  The chromogenic substrate for APC S-2366 (0.46 mmol/L in Tris-buffered saline, pH 7.4) was then added to the wells. After incubation of the sealed plates at 4°C in wet chambers for 3 weeks, hydrolysis of the substrate was monitored at a dual wavelength setting of 405/655 nm.
The concentration of APC in the unknown samples was calculated from the absorbance of each sample with the standard curve as a reference. Results were expressed as percentage of pooled normal plasma. Measurement of Plasma F1?2 F1?2 was assayed by a commercial ELISA (Behringwerke), as previously described.21

Statistical Analysis

The two-tailed t test was used to compare VTE patients and healthy controls. ANOVA was used to compare VTE-HyperHcy, VTE controls, and healthy controls, followed by the Dunnett’s test for internal contrasts. The Pearson r value was calculated for correla- tions between the variables studied.

Results

The results obtained in all VTE patients and controls are presented, including those with the heterozygous G20210A mutation of the prothrombin gene. A subanalysis of the results obtained in the 40 patients and 98 controls, in whom the mutation was looked for, revealed that

  • exclusion of the subjects heterozygous for the mutation did not significantly affect the results.

Plasma tHcy Levels

The mean (SD) fasting levels of plasma tHcy were significantly higher in VTE-HyperHcy (28.8?19.5 ?mol/L) than in VTE-NormoHcy (12.0+5.2, P<0.001) and healthy con- trols (11.0+5.3, P<0.001). The mean postmethionine load increments of tHcy above fasting levels were also higher in VTE-HyperHcy (32.9+13.5 umol/L) than in VTE- NormoHcy (19.8+7.5, P<0.001) and healthy controls (16.1+7.6, P<0.001). Differences between VTE-NormoHcy and healthy controls were not statistically significant. Six healthy controls (6.3%) had HyperHcy, according to the diagnostic criteria previously outlined. Plasma Levels of APC Healthy Controls The mean plasma level of APC in healthy controls was 116(20%). There was a statistically significant correlation between the plasma levels of APC and those of protein C (r?0.48, P?0.001) (Figure 1). Therefore, because APC levels are influenced by the concentration of their zymogen, both the absolute APC levels and the activated protein C/protein C (APC/PC) ratios were used for subsequent analysis. The mean value of the APC/PC ratio in healthy controls was 1.01?0.2.

There was no correlation between the plasma levels of APC (not shown) or the APC/PC ratios and the fasting plasma levels of tHcy (Figure 2) or its postmethionine load increments above fasting levels (not shown). The mean APC plasma levels and APC/PC ratios were similar in healthy controls whose tHcy plasma levels fell within the first (115 and 1.0), second (118 and 0.96), or third (115 and 1.01) tertiles of distribution. The mean fasting plasma levels of APC and the APC/PC ratios of 10 healthy controls

– did not significantly differ from those measured in the same subjects 4 hours after an oral methionine load,
– which increased the concentration of tHcy by more than 2-fold (Table 2).

VTE Patients

The mean plasma levels of APC and APC/PC ratios were higher in VTE patients than in healthy controls (124?32 versus 116?20, P?0.03 and 1.12?0.32 versus 0.99?0.19, P?0.0004). This difference was mostly due to VTE- HyperHcy patients whose plasma APC levels and APC/PC ratios were significantly higher than those of healthy controls (Table 3). In contrast, differences between VTE-NormoHcy and healthy controls and between VTE-HyperHcy and VTE- NormoHcy did not reach statistical significance (Table 3). Results did not change substantially when we excluded patients with thrombosis of the superficial veins (APC levels, 124+26 in VTE-HyperHcy and 121?31 in VTE-NormoHcy; APC/PC ratio, 1.17?0.25 in VTE-HyperHcy and 1.09?0.3 Figure 1. Correlation between the plasma levels of protein C and APC in 98 healthy volunteers. Values are expressed as per- centage of the concentrations measured in pooled normal plasma from 30 healthy blood donors. Figure 2. Correlation between the fasting plasma levels of tHcy and APC/PC ratios of 98 healthy volunteers. Cattaneo et al September 1998 1373 in VTE-NormoHcy) or women taking oral contraceptives (APC levels, 115?19 in controls, 130?29 in VTE- HyperHcy, and 121+33 in VTE-NormoHcy; APC/PC ratio, 0.98?0.23 in controls, 1.13?0.4 in VTE-HyperHcy, and 1.08?0.3 in VTE-NormoHcy). The prevalence of high APC/PC ratios was significantly higher in VTE patients than in controls, independent of the tHcy levels in their plasma (Table 4),

-whereas that of high plasma APC levels was significantly increased in VTE- HyperHcy patients only (Table 4).

Plasma Levels of F1?2

The mean plasma level of F1?2 in VTE patients (1.6?0.5 nmol/L) did not significantly differ from that measured in healthy controls (1.5?0.6 nmol/L). There was no statistically significant difference between plasma levels of F1?2 in VTE-HyperHcy (1.6?0.6 nmol/L), VTE-NormoHcy (1.6?0.6 nmol/L), and healthy controls. The mean F1?2 plasma levels were similar in healthy controls whose plasma levels of tHcy fell within the first, second, or third tertiles of distribution (not shown). F1?2 levels and APC/PC ratios were significantly correlated in controls (r?0.28, P?0.005) but not in VTE-HyperHcy (r? ?0.03, P?0.05) or VTE- NormoHcy (r?0.08, P?0.05).

Discussion

This study shows that

–  patients with previous episodes of VTE have higher circulating plasma levels of APC than healthy controls, particularly if they have HyperHcy.

The patients studied had none of the known congenital or acquired thrombophilic states, in which

–  the circulating levels of markers of activation of the coagulation system may be increased.21–24Even
– though the recently described G20210A mutation of the prothrombin gene17could be looked for retrospectively in only approximately one third of the pa- tients, also those patients in whom the prothrombin mutation was ruled out had high APC levels,
– excluding that they were mainly due to the presence of the mutation.

APC is generated from its plasma precursor, protein C, on activation by thrombin-thrombomodulin complex on the endothelial cell surface, probably acting in concert with the endothelial cell protein C receptor.1Subcoagulant amounts of thrombin in the circulation may increase the plasma levels of endogenous APC, which can therefore be considered markers of a hypercoagulable state.4Accordingly, the high APC plasma levels that we measured in patients with previous episodes of VTE may be interpreted as an index of ongoing thrombin formation,
despite the fact that at least 4 months (and a median of 14 months) elapsed since their last thrombotic episode. However,

–  the plasma concentrations of F1?2, a marker of thrombin generation, were not increased signifi cantly in the same VTE patients and were not correlated with APC levels or APC/PC ratios.

In contrast to VTE patients, a statistically significant correlation between APC and F1?2 plasma levels was found in healthy controls. On the basis of these data, we hypothesize that

–  the increased plasma levels of APC found in patients with previous episodes of VTE are not caused by heightened thrombin generation but by alternative mechanisms. Although we did not measure markers of activation of the fibrinolytic system,

– the possibility that high plasma levels of plasmin could be responsible for protein C activation25in these patients should be considered.

The greatest increase of APC plasma levels in VTE patients was observed in subjects with fasting and/or postmethionine-loading HyperHcy. VTE patients with nor mal plasma levels of tHcy had lower concentrations of APC than patients with HyperHcy, but this

–  difference could be due to chance alone, because it was not statistically significant. These results contrast with the alleged inhibitory effect of Hcy on protein C activation that was shown in in vitro studies.8–10

Our data obtained in healthy individuals

– support the view that Hcy does not affect protein C activation in vivo, because the
– mean plasma levels of APC of subjects in the highest tertile of distribution of tHcy levels were not different from those of subjects in the lowest tertile. Moreover,
– the rapid increase in plasma tHcy brought about by an oral methionine load did not affect the concentration of circulating APC

TABLE 2. Healthy Controls Before and 4 Hours After Methionine Loading (PML) Plasma Levels tHcy, APC, and APC/PC Ratios in 10 tHcy, ?mol/LAPC, %APC/PC Ratio Baseline 4 h PML* P† 10.5?3.8 29.5?7.6 0.0001 118?43 113?32 0.57 0.98?0.2 0.95?0.1 0.7 Data are mean?SD. *Methionine was given orally at a dose of 3.8 g/m2body surface area. †t test for paired samples. TABLE 4. APC/PC Ratios in Healthy Controls, Patients With Previous VTE-HyperHcy, and Patients With Previous VTE-NormoHcy Prevalences of High Plasma Levels of APC and Subjectsn With High APC LevelsWith High APC/PC Ratio n (%)OR (95% CI) n (%)OR (95% CI) Healthy controls 98 10 (10.2) 1.0 (reference) 10 (10.2) 1.0 (reference) VTE-HyperHcy48 12 (25.0) 2.9 (1.1–8.3) VTE-NormoHcy80 16 (20.0) 2.2 (0.9–5.7) 16 (33.3) 4.4 (1.7–11.4) 22 (27.5) 3.3 (1.4–8.1) CI indicates confidence interval. The cutoff points, which corresponded to the 90th percentiles of distribution among healthy controls, were 143.1% for APC levels and 1.22 for APC/PC ratios.

TABLE 3. Controls, Patients With Previous VTE-HyperHcy, and Patients With Previous VTE-NormoHcy

Plasma Levels of APC and APC/PC Ratios in Healthy Subjects nAPC,* %APC/PC Ratio† Healthy controls VTE-HyperHcy VTE-NormoHcy P (ANOVA) 98 48 80 116?20 128?29 121?33 0.03 0.99?0.19 1.15?0.33 1.10?0.31 0.002 Data are mean?SD. *VTE-HyperHcy versus VTE-NormoHcy (Dunnett’s test), P?NS; VTE- HyperHcy versus healthy controls, P?0.01; VTE-NormoHcy versus healthy controls, P?NS. †VTE-HyperHcy versus VTE-NormoHcy (Dunnett’s test), P?NS; VTE- yperHcy versus healthy controls, P?0.001; VTE-NormoHcy versus healthy controls, P?0.01. 1374

Activated Protein C, Thrombosis, and Homocysteine

Therefore, the results of our study suggest that Hcy does not negatively influence the plasma APC levels and argue against the hypothesis that

– it inhibits the activation of protein C in vivo by interfering with the activity of thrombomodulin.

Recently, Lentz et al,26in an experimental study of mon- keys with diet-induced moderate HyperHcy, showed that

– the thrombin-stimulated endothelium of aortas from hyperhomocysteinemic animals activated protein C in vitro less effectively than that of control animals.

This study, which supports the hypothesis that Hcy interferes with protein C activation, is in apparent contradiction with our results. At least two possible explanations for their different results can be proposed.

First, Hcy would not affect protein C activation that is ongoing in vivo under physiological conditions, whereas it would interfere with its activation at sites at which athero- genic or thrombogenic stimuli injured the endothelium and increased the local concentration of thrombin.
Second, due to the different relative densities of endothelial cell protein C receptor and thrombomodulin on the endothelium of large vessels and capillaries,1the regulation of protein C activation may differ in the two vascular districts. Although Lentz et al26 measured protein C activation by the endothelium of the aorta, we measured circulating APC, which mostly reflects protein C activation occurring in the microcirculation.

On the basis of the considerations above, we speculate that
– Hcy does not interfere with protein C activation ongoing in the micro- circulation under physiological conditions, whereas
– it could inhibit protein C activation on large, injured vessels.

In conclusion, our study shows that APC plasma levels are high in patients with previous episodes of VTE in whom the plasma levels of F1?2 are normal. Therefore, APC plasma levels represent a sensitive marker of activation of the hemostatic system. In addition, the study showed that high Hcy levels are not associated with heightened thrombin generation and do not interfere with the activation of protein C under physiological conditions in vivo. Further studies are needed to unravel the mechanism(s) by which HyperHcy increases the risks for atherosclerosis and thrombosis.

References

1. Esmon CT, Ding W, Yasuhiro K, Gu J-M, Ferrel G, Regan LM, Stearns- Kurosawa DJ, Kurosawa S, Mather T, Laszik Z, Esmon NL. The protein C pathway: new insights. Thromb Haemost. 1997;78:70–74.
2. Bauer KA, Kass BL, Beeler DL, Rosenberg RD. Detection of protein C activation in humans. J Clin Invest. 1984;74:2033–2041.
3. Heeb MJ, Mosher D, Griffin JH. Inhibition and complexation of activated protein C by two major inhibitors in plasma. Blood. 1989;73:446–454.
4. Gruber A, Griffin JH. Direct detection of activated protein C in blood from human subjects. Blood. 1992;79:2340–2348.
5. Espan ˜a F, Zuazu I, Vicente V, Estelle ´s A, Marco P, Aznar J. Quantifi- cation of circulating activated protein C in human plasma by immuno- assays: enzyme levels are proportional to total protein C levels. Thromb Haemost. 1996;75:56–61.
6. Cattaneo M. Hyperhomocysteinemia: a risk factor for arterial and venous thrombotic disease. Int J Clin Lab Res. 1997;27:139–144.
7. Harpel PC, Zhang X, Borth W. Homocysteine and hemostasis: patho- genetic mechanisms predisposing to thrombosis. J Nutr. 1996;126: 1285S–1289S.
8. Rodgers GM, Conn MT. Homocysteine, an atherogenic stimulus, reduces protein C activation by arterial and venous endothelial cells. Blood. 1990;75:895–901.
9. Lentz SR, Sadler JE. Inhibition of thrombomodulin surface expression and protein C activation by the thrombogenic agent homocysteine. J Clin Invest. 1991;88:1906–1914.
10. Hayashi T, Honda G, Suzuki K. An atherogenic stimulus homocysteine inhibits cofactor activity of thrombomodulin and enhances thrombo- modulin expression in human umbilical vein endothelial cells. Blood. 1992;79:2930–2936.
saee original manuscript for further referencesz  and for figures (not shown)

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Stabilizers that prevent Transthyretin-mediated Cardiomyocyte Amyloidotic Toxicity

Reporter and curator: Larry H. Bernstein, MD, FCAP

http://pharmaceuticalintelligence.com/12-2-2013/larryhbern/Stabilizers that prevent transthyretin-mediated cardiomyocyte amyloidotic toxicity

Transthyretin is a small protein with a half-life of < 48 hours, synthesized by the liver, and a major transport protein for thyroxin.  There are 80 variants known, and some variants that occur in the Portuguese, a small section of Japan, Sweden, and Brazil, are associated will primary amyloidosis, the only cure for which is liver transplantation.  It causes fibrillary inclusions in the heart, but also affects the autonomic nervous system.  Some of the major work on this has been done for many years in the laboratory of   Jeffery W. Kelly, at the Skaggs Institute for Chemical Biology, the Scripps Research Institute.  A recent publication is of considerable interest.

Potent Kinetic Stabilizers that Prevent Transthyretin-mediated Cardiomyocyte Proteotoxicity

 Mamoun M. Alhamadsheh1,6,7, Stephen Connelly2,7, Ahryon Cho1, Natàlia Reixach3, Evan T. Powers3,4,5, Dorothy W. Pan1, Ian A. Wilson2,5, Jeffery W. Kelly3,4,5, and Isabella A. Graef1,*
Sci Transl Med. Author manuscript; available in PMC 2012 August 24.
1Department of Pathology, Stanford University Medical School, Stanford, California, USA
2Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, USA
3Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California, USA
4Department of Chemistry, The Scripps Research Institute, La Jolla, California, USA
5The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA
6Department of Pharmaceutics & Medicinal Chemistry, University of the Pacific, Stockton, California, USA

Abstract

The V122I mutation that alters the stability of transthyretin (TTR) affects 3–4% of African Americans and leads to amyloidogenesis and development of cardiomyopathy. In addition, 10–15% of individuals over the age of 65 develop senile systemic amyloidosis (SSA) and cardiac
TTR deposits due to wild-type TTR amyloidogenesis. As no approved therapies for TTR amyloid cardiomyopathy are available, the development of drugs that prevent amyloid-mediated cardiotoxicity is desired. To this aim, we developed a fluorescence polarization-based HTS screen,
which identified several new chemical scaffolds targeting TTR. These novel compounds were potent kinetic stabilizers of TTR and
  • prevented tetramer dissociation,
  • unfolding and aggregation of both wild type and the most common cardiomyopathy-associated TTR mutant, V122I-TTR.
High-resolution co-crystal structures and characterization of the binding energetics revealed how these diverse structures bound to tetrameric TTR. Our study also showed that these compounds effectively inhibited the proteotoxicity of V122I-TTR towards human cardiomyocytes.
Several of these ligands stabilized TTR in human serum more effectively than diflunisal, which is one of the best known inhibitors of TTR aggregation, and may be promising leads for the treatment and/or prevention of TTR-mediated cardiomyopathy.

Author Contributions:

M.M.A. designed and performed most experiments, S.C. performed crystallographic structure determination, A.C peformed the serum TTR stabilization. N.R. performed the cell-based assays.   E.T.P. analyzed the ITC data. D.W.P. helped with probe synthesis. I.A.W. supervised the crystallographic work. J.W.K. supervised the work, S.C., N.R., I.A.W. and J.W.K. edited the paper. I.A.G supervised the work, M.M.A. and I.A.G prepared the manuscript.

 INTRODUCTION

The misassembly of soluble proteins into toxic amyloid aggregates underlies a large number of human degenerative diseases (1–3). TTR is one of more than 30 human amyloidogenic proteins whose misassembly can cause
  • a variety of degenerative gain-of-toxic-function diseases.
TTR is a tetrameric protein (54 kDa), secreted from the liver into the blood where, using orthogonal sites,
  • it transports thyroxine (T4) and
  • holo-retinol binding protein (4).
However, 99% of the TTR T4 binding sites remain unoccupied in humans
  • owing to the presence of two other T4 transport proteins in blood (3).
Familial TTR amyloid diseases, which are associated with one of more than 80 mutations in the TTR gene, include
  • the systemic neuropathies (familial amyloid polyneuropathy [FAP]),
  • cardiomyopathies (familial amyloid cardiomyopathy [FAC]), and
  • central nervous system amyloidoses (CNSA) (5–8).
Cardiac amyloidosis is most commonly caused by
  • deposition of immunoglobulin light chains or
  • TTR in the cardiac interstitium and conducting system.
It is a chronic and progressive condition, which can lead to arrhythmias, biventricular heart failure, and death (8–10). Two types of TTR-associated amyloid cardiomyopathies are clinically important.
  1. Wild-type (WT) TTR aggregation underlies the development of senile systemic amyloidosis (SSA). Cardiac TTR deposits can be found in 10 to 15% of the population over the age of 65 at autopsy (10,11). Many of these patients are asymptomatic, but there is little doubt that SSA is an underdiagnosed disease.
  2. In addition, a number of TTR mutations, including V122I, lead to amyloidogenesis and familial amyloid cardiomyopathy (FAC) (12–15). Population studies show that the V122I mutation is found in 3–4% of African Americans (~1.3 million people) and contributes to the increased prevalence of heart failure among this population segment (14,15).

The mutant TTR allele behaves as an autosomal dominant allele with age-dependent penetrance and

  • the frequency of cardiac amyloidosis from TTR in African-American individuals above age 60 is four times that seen in Caucasian-Americans of comparable age.
All of the TTR mutations associated with familial amyloidosis decrease tetramer stability, and
  • some decrease the kinetic barrier for tetramer dissociation (3, 16).
  • The latter is important because tetramer dissociation is the rate-limiting step in the TTR amyloidogenesis cascade (3).

Kinetic stabilization of the native, tetrameric structure of TTR by

  • interallelic trans suppression (incorporation of mutant subunits that raise the dissociative transition state energy) prevents
    1. post-secretory dissociation and aggregation, as well as the related disease 
    2. familial amyloid polyneuropathy (FAP), by slowing TTR tetramer dissociation (17).
Occupancy of the TTR T4 binding sites with rationally designed small molecules is known to stabilize the native tetrameric state of TTR over the dissociative transition state,
  • raising the kinetic barrier,
  • imposing kinetic stabilization on the tetramer and
  • preventing amyloidogenesis (3, 16, 18).
Previous studies have focused on rational ligand design and as a result
  • most of the TTR stabilizers reported to date are halogenated biaryl analogues of T4,
  • many resembling non-steroidal anti-inflammatory drugs (NSAIDs).
Some of these compounds, such as the NSAID diflunisal, which is currently tested in clinical trials in FAP patients for its efficacy to ameliorate
  • peripheral neuropathy resulting from TTR deposition, (19) have anti-inflammatory activity (20, 21).
The pharmacological effects of NSAIDs are due to inhibition of cyclo-oxygenase (COX) enzymes (22). Inhibition of COX-1 can produce side effects such as
  • gastrointestinal irritation, leading to ulcers and bleeding (23).
Inhibition of COX-2 has been associated with an
  • increased risk of severe cardiovascular events, including heart failure,
  • particularly in patients with preexisting cardiorenal dysfunction (20, 21, 24, 25).
Therefore, heart and kidney impairment are exclusion criteria for participation of patients in the diflunisal clinical trials to treat TTR-mediated FAP (19). Genomic variations can
  • increase the sensitivity of individuals to adverse side effects of NSAIDs.
Serum concentrations of NSAIDs depend on CYP2C9 and/or CYP2C8 activity. CYP2C9 polymorphism might play a significant role in the profile of adverse side effects of NSAID and alleles that affect the activity of CYP2C9 are found at different frequency in subjects of Caucasian, African or Asian descent (26, 27). Hence, the long-term therapy with drugs that have inhibitory effect on COX activity to prevent TTR aggregation is especially problematic in patients who suffer from TTR-mediated cardiomyopathy. The design and development of drugs to treat/prevent FAC or SSA thus presents the challenge
  1. not only to find compounds with a greater variety of chemical scaffolds that accomplish stabilization, but
  2. do so without the adverse side effects due to inhibition of COX activity.
 For these reasons, the development of a rapid and robust screen for compounds that bind to and stabilize TTR could be useful. To date, no high-throughput screening (HTS) methodology is available for the discovery of TTR ligands (28,29). Therefore, we developed a versatile
  • fluorescence polarization (FP) based HTS assay that can detect
  • binding of small molecules to the T4 binding pocket of TTR under physiological conditions.

RESULTS

Design and synthesis of the TTR FP probe

FP is used to study molecular interactions by monitoring changes in the apparent size of a fluorescently labeled molecule. Binding is measured by an increase in the FP signal, which is proportional to the decrease in the rate of tumbling of a fluorescent ligand upon association with macromolecules such as proteins (Fig. 1A). To synthesize a fluorescent TTR ligand 1, we initially started with the NSAID diflunisal analogue 2 (Fig. 1B) (30). The product of attaching a linker to 2, compound 3, had very low binding affinity to TTR (Kd1 >3290 nM, fig. S1A and fig. S1B).
The crystal structure of the diclofenac analog 4 showed that
  • the phenolic hydroxyl flanked by the two chlorine atoms is oriented out of the binding pocket into the solvent (31).
  • We reasoned that attaching a PEG amine linker to the phenol group of 4 would generate compound 5 which would bind to TTR (Fig. 1B and fig. S1C)

5 was coupled to fluorescein isothiocyanate (FITC) to produce the FITC-coupled TTR FP probe (1, Fig. 1B). The binding characteristics of the probe (Kd1 = 13 nM and Kd2 = 100 nM) were assessed with ITC (Fig. 2A).

Evaluation of the FP assay

The binding of 1 to TTR was evaluated to test its suitability for the FP assay with a standard saturation binding experiment. A fixed concentration of probe 1 (0.1 μM) was incubated with increasing concentrations of TTR (0.005 μM to 10 μM) and the formation of 1•TTR complex was quantified by the increase in FP signal (excitation λ 485 nm, emission λ 525 nm) relative to the concentration of TTR (Fig. 2B). The fluorescence polarization increased with the concentration of TTR until saturation was reached. A large dynamic range (70 – 330 mP) was measured for the assay. To validate the FP assay, we tested known TTR binders in a displacement assay (for detailed information see Supplemental Material). Compound 2 (Kapp = 231 nM, R2 = 0.997), Thyroxine (T4) (Kapp = 186 nM, R2 = 0.998) and diclofenac (Kapp = 4660 nM, R2 = 0.999) decreased the FP signal in a dose- dependent  manner  (Fig. 2C,  fig. S2B and S2C). The FP assay is a competitive displacement assay and therefore it provides apparent binding constants (Kapp). However, these apparent binding constants correlate well with the data obtained by ITC which measures direct interactions in solution and gives an actual (Kd) value.

 Adaptation of the FP assay for HTS

Next, we optimized the FP assay for HTS and screened a ~130,000 small molecule library for compounds that displaced probe 1 from the T4 binding sites of TTR. The FP assay was performed in 384-well plates with low concentrations of probe 1 (1.5 nM) and TTR (50 nM) in a 10  μL assay volume.  Detergent (0.01% Triton X-100) was added to the assay buffer to avoid false positive hits from aggregation of the small molecules. The assay demonstrated robust performance, with a, large dynamic range (~70–230 mP) and a Z′ factor (32, 33) in the range of 0.57–0.78 (fig. S3A and S3B).

Hits were defined as compounds, which resulted in at least 50% decrease in FP and demonstrated relative fluorescence between 70 and 130%. Many fluorescence quenchers and enhancers, which have less than 70% and greater than 130% total fluorescence relative to a control (compound without TTR), were excluded from the hit list. The excluded compounds have native fluorescence that is similar to fluorescein, which would interfere with the FP measurements and result in false positive hits. Two hundred compounds were designated as positive hits (0.167% hit rate). The top 33 compounds (compounds with lowest FP IC50) were assayed in a 10-point duplicate dose-response FP assay and displayed an IC50 (concentration that resulted in 50% decrease in the FP signal) between 0.277 and 10.957 μM (table S2).

Validation of the HTS hits

The top 33 compounds were retested with the FP assay (table S2) and with surface plasmon resonance (SPR) as another independent biophysical method. Solutions of the 33 hits were passed over immobilized, biotinylated TTR on a streptavidin coated chip. The binding of a small molecule to TTR on the sensor chip produces a SPR response signal (RU). The RU signal after addition of the top 33 compounds was measured and compared to a negative, solvent only, control. All compounds identified by the screen as hits were confirmed as TTR binders using SPR (fig. S4). We also found known TTR binders, such as NSAIDs (diclofenac, meclofenamic acid, and niflumic acid) and isoflavones (apigenin) in our screen (3, 34) (table S2). Among the best ligands (Fig. 2D) were the NSAID, niflumic acid, two catechol-O-methyl-tranferase (COMT) inhibitors, 3,5-dintrocatechol and Ro 41-0960 (35) and a number  of compounds   not previously known to bind to TTR. The chemical structures of these ligands were confirmed by 1H NMR and high-resolution mass spectrometry(HRMS) and the chemical purity was determined to be >95% (fig. S5).

Inhibition of TTR amyloidogenesis by the HTS hits

To test whether the new TTR ligands (7.2 μM) could function as kinetic stabilizers, we measured their ability to inhibit TTR (3.6 μM) amyloidogenesis at 72 hrs at pH 4.4 (fig. S6) (29). All 33 compounds inhibited TTR aggregation (<50% fibril formation, table S2). Of these, 23 were very good (<20% fibril formation) and 11 were excellent (<2% fibril formation) TTR kinetic stabilizers (Fig. 3A). All of the potent TTR stabilizers, except niflumic acid, and the two COMT inhibitors 3,5-dintrocatechol and Ro 41-0960, were chemical entities with no previously reported biological activity. Since occupancy of only
one T4 binding site within TTR is sufficient for kinetic stabilization of the tetramer (3), we tested the most potent ligands at substoichiometric concentrations (2.4 fold molar excess of TTR relative to ligand) in a kinetic aggregation assay monitored over 5 days (Fig. 3B). Under these conditions ligands 7, 14, 15 and Ro 41-0960 dramatically slowed fibril formation and outperformed the known TTR stabilizer, diclofenac, which blocked only ~55% of TTR aggregation.

Evaluating the TTR ligands for COX-1 enzymatic inhibition and binding to thyroid hormone receptor

A successful clinical candidate against TTR amyloid cardiomyopathy should have minimal off-target toxicity due to the potential need for life-long use of these drugs. Specifically, the TTR ligands should exhibit minimal binding to COX and the nuclear thyroid hormone receptor (THR). Inhibition of COX is contraindicated for treating FAC patients, since COX inhibition can not only lead to renal dysfunction and blood pressure elevation, but may precipitate heart failure in vulnerable individuals (20, 21, 24, 25). Therefore, the most potent TTR ligands were evaluated for their ability to inhibit COX-1 activity, as well as, for binding to THR, in comparison with the NSAID niflumic acid. Although niflumic acid exhibited substantial (94%) COX-1 inhibition, three of the 12 new compounds evaluated (7, 6 and 10) displayed less than 1% inhibition of COX-1. Only one ligand (compound 8) showed significant (58%) and two compounds (6 and 10) minor (5%) binding to THR (Fig. 3C).

Characterization of the binding energetics to TTR

Many reported TTR ligands, including T4, bind TTR with negative cooperativity, which appears to arise from subtle conformational changes in TTR upon ligand binding to the first T4 site (3, 16, 36). We used ITC to determine the binding constants and to evaluate cooperativity between the two TTR T4 sites (Fig. 2A, Fig. 4A, Fig. 4B and fig. S1 and fig. S7). The ITC data for compounds 1, 7, 14, and Ro 41-0906 binding to TTR were fit to a two-site binding model and show that these potent ligands bind TTR with low nanomolar affinity. The dissociation constants for these ligands indicated that they bound TTR with negative cooperativity (table S3). Analysis of the free energies associated with ligand binding to TTR indicates that binding was driven both by burial of the hydrophobic ligand in the TTR binding site (which leads to the favorable binding entropies) and specific ligand-TTR interactions (which leads to the favorable binding enthalpies) (Fig. 2A, Fig. 4A, Fig.4B, and fig. S7B) (37). The binding of compounds 7 (Kd1 = 58 nM and Kd2 = 500 nM) and 14 (Kd1 = 26 nM and Kd2 = 1800 nM) to TTR did not cause major conformational changes to the TTR tetramer structure (Fig. 5).
Remainder of document is found at publication site, including Figures.
SOURCE

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Cardiology, Genomics and Individualized Heart Care: Framingham Heart Study (65 y-o study) & Jackson Heart Study (15 y-o study)

Cardiology, Genomics and Individualized Heart Care

Curator: Aviva Lev-Ari, PhD, RN

Article ID #90: Cardiology, Genomics and Individualized Heart Care: Framingham Heart Study (65 y-o study) & Jackson Heart Study (15 y-o study). Published on 12/1/2014

WordCloud Image Produced by Adam Tubman

 

The topic of Cardiology, Genomics and Individualized Heart Care is been developed in the following forthcoming e-Book on a related subject matter:

Curators: Larry H Bernstein, MD, FCAP and Aviva Lev-Ari, PhD, RN

This e-Book has the following Parts:

PART 1
Genomics and Medicine

Introduction to Volume Three
1.1: Genomics and Medicine: The Physician’s View
1.2: Ribozymes and RNA Machines – Work of Jennifer A. Doudn
1.3: Genomics and Medicine: The Geneticist’s View
1.4: Genomics in Medicine – Establishing a Patient-Centric View of Genomic Data

PART 2
Epigenetics- Modifiable Factors Causing Cardiovascular Diseases

2.1 Diseases Etiology

2.1.1 Environmental Contributors Implicated as Causing Cardiovascular Diseases
2.1.2 Diet: Solids and Fluid Intake
2.1.3 Physical Activity and Prevention of Cardiovascular Diseases
2.1.4 Psychological Stress and Mental Health: Risk for Cardiovascular Diseases
2.1.5 Correlation between Cancer and Cardiovascular Diseases
2.1.6 Medical Etiologies for Cardiovascular Diseases: Evidence-based Medicine – Leading DIAGNOSES of Cardiovascular Diseases, Risk Biomarkers and Therapies
2.1.7 Signaling Pathways
2.1.8 Proteomics and Metabolomics

2.2 Assessing Cardiovascular Disease with Biomarkers

2.2.1 Issues in Genomics of Cardiovascular Diseases
2.2.2 Endothelium, Angiogenesis, and Disordered Coagulation
2.2.3 Hypertension BioMarkers
2.2.4 Inflammatory, Atherosclerotic and Heart Failure Markers
2.2.5 Myocardial Markers

2.3  Therapeutic Implications: Focus on Ca(2+) signaling, platelets, endothelium

2.3.1 The Centrality of Ca(2+) Signaling and Cytoskeleton Involving Calmodulin Kinases and Ryanodine Receptors

2.3.2 Platelets in Translational Research ­ 2

2.3.3 The Final Considerations of the Role of Platelets and Platelet Endothelial Reactions in Atherosclerosis

2.3.4 Nitric Oxide Synthase Inhibitors (NOS-I)

2.3.5 Resistance to Receptor of Tyrosine Kinase

2.3.6 Oxidized Calcium Calmodulin Kinase and Atrial Fibrillation

2.3.7 Advanced Topics in Sepsis and the Cardiovascular System at its End Stage

2.4 Comorbidity of Diabetes and Aging

PART 3
Determinants of Cardiovascular Diseases
Genetics, Heredity and Genomics Discoveries

Introduction
3.1 Why cancer cells contain abnormal numbers of chromosomes (Aneuploidy)
3.2 Functional Characterization of Cardiovascular Genomics: Disease Case Studies @ 2013 ASHG
3.3 Leading DIAGNOSES of Cardiovascular Diseases covered in Circulation: Cardiovascular Genetics, 3/2010 – 3/2013
3.4  Commentary on Biomarkers for Genetics and Genomics of Cardiovascular Disease

PART 4
Individualized Medicine Guided by Genetics and Genomics Discoveries

4.1 Preventive Medicine: Cardiovascular Diseases
4.2 Gene-Therapy for Cardiovascular Diseases
4.3 Congenital Heart Disease/Defects
4.4 Pharmacogenomics for Cardiovascular Diseases

SOURCE

http://pharmaceuticalintelligence.com/biomed-e-books/series-a-e-books-on-cardiovascular-diseases/volume-three-etiologies-of-cardiovascular-diseases-epigenetics-genetics-genomics/

The Next Frontier in Heart Care

Research Aims to Personalize Treatment With Genetics

Nov. 25, 2013 7:18 p.m. ET

VIEW VIDEO

http://online.wsj.com/news/articles/SB10001424052702304281004579220373600912930#!

Two influential heart studies are joining forces to bring the power of genetics and other 21st century tools to battle against heart disease and stroke. Ron Winslow and study co-director Dr. Vasan Ramachandran explain. Photo: Shubhangi Ganeshrao Kene/Corbis.

Scientists from two landmark heart-disease studies are joining forces to wield the power of genetics in battling the leading cause of death in the U.S.

Cardiologists have struggled in recent years to score major advances against heart disease and stroke. Although death rates have been dropping steadily since the 1960s, progress combating the twin diseases has plateaued by other measures.

Genetics has had a profound impact on cancer treatment in recent years. Now, heart-disease specialists hope genetics will reveal fresh insight into the interaction between a

  • person’s biology,
  • living habits and
  • medications

that can better predict who is at risk of a heart attack or stroke.

“There’s a promise of new treatments with this research,” said Daniel Jones, chancellor of the University of Mississippi and former principal investigator of the 15-year-old Jackson Heart Study, a co-collaborator in the new genetics initiative.

Scienc e Source /Photo Researchers Inc. (hearts); below, l-r: Boston University; Robert Jordan/Univ. of Miss.; Jay Ferchaud/Univ. of Miss Medical Center

Prevention efforts also could improve with the help of genetics research, Dr. Jones said. For example, an estimated 75 million Americans currently have high blood pressure, or hypertension, but only about half of those are able to control it with medication. It can take months of trial-and-error for a doctor to get the right dose or combination of pills for a patient. Researchers hope genetic and other information might enable doctors to identify subgroups of hypertension that respond to specific treatments and target patients with an appropriate therapy.

Also collaborating on the genetics project is the 65-year-old Framingham Heart Study. Its breakthrough findings decades ago linked heart disease to such factors as smoking, high blood pressure and high cholesterol. Framingham findings have been a foundation of cardiovascular disease prevention policy for a half-century.

More than 15,000 people have participated in the Framingham study. The Jackson study, with more than 5,000 participants, was launched in 1998 to better understand risk factors in African-Americans, who were underrepresented in Framingham and who bear a higher burden of cardiovascular disease than the rest of the population. Both studies are funded by the National Heart, Lung, and Blood Institute, part of the National Institutes of Health.

Exactly how the collaboration, announced last week, will proceed hasn’t been determined. One promising area is the “biobank,” the collection of more than one million blood and other biological samples gathered during biennial checkups of Framingham study participants going back more than a half century.

The samples are stored in freezers in an underground earthquake-proof facility in Massachusetts, said Vasan Ramachandran, a Boston University scientist who takes over at the beginning of next year as principal investigator of the Framingham Heart Study. Another 40,000 samples from the Jackson study are kept in freezers in Vermont. By subjecting samples to DNA sequencing and other tests, researchers say they may be able to identify variations linked to progression of cardiovascular disease—or protection from it.

Each study is likely to enroll new participants as part of the collaboration to allow tracking of risk factors and diet and exercise habits, for instance, in real time instead of only during infrequent checkups.

Heart disease is linked to about 800,000 deaths a year in the U.S. In 2010, some 200,000 of those deaths could have been avoided, including more than 112,300 deaths among people younger than 65, according to a recent analysis by the Centers for Disease Control and Prevention. But those avoidable deaths reflected a 3.8% per year decline in mortality rates during the previous 10 years.

Now, widespread prevalence of obesity and diabetes threatens to undermine such gains. And a large gap remains between how white patients and minorities—especially African-Americans—benefit from effective strategies.

There have been few new transformative cardiovascular treatments since the mid-1980s to early 1990s, when a stream of large-scale trials of new agents ranging from clot-busters to treat heart attacks to the mega class of statins electrified the cardiology field with evidence of significant improvements in survival from the disease. One reason: Some of those remedies have proven tough to beat with new treatments.

What’s more, use of the current menu of medicines for reducing heart risk remains an imprecise art. Besides

  • blood pressure drugs,
  • cholesterol-lowering statins

also are widely prescribed. Drug-trial statistics show that to prevent a single first heart attack in otherwise healthy patients can require prescribing a statin to scores of patients, but no one knows for sure who actually benefits and who doesn’t.

“It would be great if we could make some more paradigm-shifting discoveries,” said Michael Lauer, director of cardiovascular sciences at the NHLBI, which is a part of the National Institutes of Health.

Finding new treatments isn’t the only aim of the new project. “You could use existing therapies smarter,” said Joseph Loscalzo, chairman of medicine at Brigham and Women’s Hospital in Boston.

The American Heart Association launched the initiative and has committed $30 million to it over the next five years. The AHA sees the project as critical to its goal to achieve a 20% improvement in cardiovascular health in the U.S. while also reducing deaths from heart disease and stroke by 20% for the decade ending in 2020, said Nancy Brown, the nonprofit organization’s chief executive.

The Jackson study has already identified characteristics of cardiovascular risk among African-American patients “that may have promise for new insights” in a collaborative effort, said Adolfo Correa, professor of medicine and pediatrics at University of Mississippi Medical Center and interim director of the Jackson study.

For instance, there is a higher prevalence of obesity among Jackson participants than seen in the Framingham cohorts. Obesity is associated with high blood pressure, diabetes and cardiovascular risk. Diabetes is also more prevalent among blacks than whites.

But African-Americans of normal weight appear to have higher rates of hypertension and diabetes than whites of normal weight. “The question is, should [measures] for defining diabetes be different or the same for the [different] populations and are they associated with the same risk of cardiovascular disease?” said Dr. Correa. The collaboration, he said, may provide better comparisons.

Researchers, who plan to use tools other than genetics, think more might be learned about blood pressure and heart and stroke risk by monitoring patients in real time using mobile devices rather than taking readings only in periodic office visits. For example, high blood pressure during sleep or spikes during exercise could indicate risks that don’t show up in a routine measurement in the doctors’ office.

A big challenge is making sense of the huge amounts of data involved in sequencing DNA and linking it to

  • medical records,
  • diet and
  • exercise habits and other variables that influence risk.

“The analytical methods for sorting out these complex relationships are still in evolution,” said Dr. Loscalzo, of Brigham and Women’s Hospital. “The cost of sequencing is getting cheaper and cheaper. The hard part is analyzing the data.”

Write to Ron Winslow at ron.winslow@wsj.com

SOURCE

http://online.wsj.com/news/articles/SB10001424052702304281004579220373600912930#!

The e-Reader is advised to to review tightly related articles in

http://pharmaceuticalintelligence.com/biomed-e-books/series-a-e-books-on-cardiovascular-diseases/volume-three-etiologies-of-cardiovascular-diseases-epigenetics-genetics-genomics/

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Liver Toxicity halts Clinical Trial of IAP Antagonist for Advanced Solid Tumors

Curator: Stephen J. Williams, Ph.D.

UPDATED 8/12/2022

Athough not related to IAP Antagonists this update does report 2 deaths from IDILI or idiosynchratic drug induced liver injury from a gene therapy trial using an AAV (adeno associated virus) targeting the disease spinal muscular atrophy.  Please see below after reading about IDILI.

 

A recent press release on FierceBiotech reported the FDA had put a halt on a phase 1 study for advanced refractory solid tumors and lymphomas of Curis Inc. oral inhibitor of apoptosis (IAP) antagonist CUDC-427.  The FDA placed the trial on partial clinical hold following reports of a death of a patient from severe liver failure.  The single-agent, dose escalation Phase 1 study was designed to determine the maximum tolerated dose and recommended doses for a Phase 2 trial. The press release can be found at:

http://www.fiercebiotech.com/press-releases/curis-reports-third-quarter-2013-financial-results-and-provides-cudc-427-de.

According to the report one patient with breast cancer that had metastasized to liver, lungs, bone, and ovaries developed severe hepatotoxicity as evidenced by elevated serum transaminase activities (AST and ALT) and hyper-billirubinemia.  Serum liver enzyme activities did not attenuate upon discontinuation of CUDC-427.  This was unlike prior experience to the CUDC-427 drug, in which decreased hepatic function was reversed upon drug discontinuation.  The patient died from liver failure one month after discontinuation of CUDC-427.

It was noted that no other patient had experienced such a serious, irreversible liver dysfunction.

Although any incidence of hepatotoxicity can be cause for concern, the incidence of IDIOSYNCRATIC IRREVERSIBLE HEPATOTOXICITY warrants a higher scrutiny.

Four general concepts can explain toxicity profiles and divergences between individuals:

  1. Toxicogenomics: Small differences in the genetic makeup between individuals (such as polymorphisms (SNP) could result in differences in toxicity profile for a drug.  This ais a serious possibility as only one patient presented with such irreversible liver damage
  2. Toxicodynamics:  The toxicologic effect is an extension of the pharmacologic mechanism of action (or  lack thereof: could there have been alternate signaling pathways activated in this patient or noncanonical mechanism)
  3. Toxicokinetic:  The differences in toxicological response due to differences in absorption, distribution, metabolism, excretion etc. (kinetic parameters)
  4. Idiosyncratic: etiology is unknown; usually a minority of adverse effects

 

Since there is not enough information to investigate toxicogenomic or toxicokinetic mechanisms for this compound, the rest of this post will investigate the possible mechanisms of hepatotoxicity due to IAP antagonists and clues from other clinical trials which might shed light on a mechanism of toxicity (toxicodynamic) or idiosyncratic events.

Therefore this post curates the current understanding of drug-induced liver injury (DILI), especially focusing on a type of liver injury referred to as idiosyncratic drug-induced liver injury (IDILI) in the context of:

  1. Targeted and newer chemotherapies such as IAP antagonists
  2. Current concepts of mechanisms of IDILI including:

i)        Inflammatory responses provoked by presence of disease

ii)      Cellular stresses, provoked by disease, uncovering NONCANONICAL toxicity pathways

iii)    Pharmacogenomics risk factors of IDILI

Eventually this post aims to stimulate the discussion: 

  • Given inflammation, genetic risk factors, and cellular stresses (seen in clinical setting) have been implicated in idiosyncratic drug-induced liver injury from targeted therapies, should preclinical hepatotoxicity studies also be conducted in the presence of the metastatic disease?
  • Does inflammation and cellular stress from clinical disease unmask NONCANONICAL pharmacologic and/or toxicological mechanisms of action?

Classification of types of Cellular Liver injury:  A listing of types of cellular injury is given for review

I.     Hepatic damage after Acute Exposure

A. Cytotoxic (Necrotic):  irreversible cell death characterized by loss of cell membrane integrity, intracellular swelling, nuclear shrinkage (pyknosis) and eventual cytoplasmic breakdown of nuclear DNA (either by a process known as karyolysis or karyorhexus) localized inflammation as a result of release of cellular constituents.  Intracellular ATP levels are commonly seen in necrotic death.  Necrosis, unlike apoptosis, does not require a source of ATP.  A nice review by Yoshihide Tsujimoto describing and showing (by microscopy) the  differences between apoptosis and necrosis can be found here.

B. Cholestatic:  hepatobiliary dysfunction with bile stasis and accumulation of bile salts.  Cholestatic injury can result in lipid (particularly cholesterol) accumulation in cannicular membranes resulting in decreased permeability of the membrane, hyperbillirubinemia and is generally thought to result in metabolic defects.

C. Lipid Peroxidation: free radical generation producing peroxide of cellular lipids, generally resulting in a cytotoxic cell death

II.     Hepatic damage after Chronic Exposure

A. Chirrotic: Chronic morphologic alteration of the liver characterized by the presence of septae of collagen distributed throughout the major portion of the liver; Forms fibrous sheaths altering hepatic blood flow, resulting in a necrotic process with scar tissue; Alteration of hepatic metabolic systems.

B. Carcinogenesis

III. Idiosyncratic Drug Induced Liver Injury

The aforementioned mechanisms of hepatotoxicity are commonly referred to as the “intrinsic” (or end target-organ) toxicity mechanisms.  Idiosyncratic drug-induced liver injury (IDILI) is not well understood but can be separated into allergic and nonallergic reactions.  Although the risk of acute liver failure associated with idiosyncratic hepatotoxins is low (about 1 in ten thousand patients) there are more than 1,000 drugs and herbal products associated with this type of toxic reaction. Idiosyncratic drug induced liver failure usually gets a black box warning from the FDA. Idiosyncratic drug-induced liver injury differs from “intrinsic” toxicity in that IDILI:

  • Happens in a minority of patients (susceptible patients)
  • Not reproducible in animal models
  • Not dose-dependent
  • Variable time of onset
  • Variable liver pathology (not distinctive lesions)
  • Not related to drug’s pharmacologic mechanism of action (trovafloxacin IDILI vs. levofloxacin)

A great review in Perspectives in Pharmacology written by Robert Roth and Patricia Ganey at Michigan State University explains these differences between intrinsic and idiosyncratic drug-induced hepatotoxicity[1] (however authors do note that there are many similarities between the two mechanisms).    It is felt that drug sensitivity (allergic) and inflammatory responses (nonallergic) may contribute to the occurrence of IDILI.  For instance lipopolysaccharide (LPS) form bacteria can potentiate acetaminophen toxicity.  In fact animal models of IDILI have been somewhat successful:

  • co-treatment of rats and mice with nontoxic doses of trovafloxacin (casues IDILI in humans) and LPS resulted in marked hepatotoxicity while no hepatotoxicity seen with levofloxacin plus LPS[2]
  • correlates well with incidence of human IDILI (adapted from a review Inflammatory Stress and Idiosyncratic Hepatotoxicity: Hints from Animal Models (in Pharmacology Reviews)[3].  Idiosyncratic injury damage has been reported for diclofenac, halothane, and sulinac.  These drugs also show hepatotoxicity in the LPS model for IDILI.
  • Roth and Ganey suggest the reason why idiosyncratic hepatotoxicity is not seen  in most acute animal toxicity studies is that, in absence of stress/inflammation  IDILI occurrence is masked by lethality but stress/inflammation shifts increases sensitivity to liver injury at a point before lethality is seen

IDILdosestressrossmantheory

Figure.  Idiosyncratic toxic responses of the liver.    In the absence of stress and/or genetic factors, drug exposure may result in an idiosyncratic liver injury (IDILI) at a point (or dose) beyond the therapeutic range and lethal exposure for that drug.  Preclinical studies, usually conducted at sublethal doses, would not detect DILI .  Stress and/or genetic factors sensitize the liver to toxic effects of the drug (synergism) and DILI is detected at exposure levels closer to therapeutic range.  Note IDILI is not necessarily dose-dependent but cellular stress (like ROS or inflammation) may expose NONCANONICAL mechanisms of drug action or toxicity which result in IDILI. Model adapted from Roth and Ganey.

What Stress factors contribute to IDILI?

Various stresses including inflammation from bacterial, viral infections ,inflammatory cytokines  and stress from reactive oxygen (ROS) have been suggested as mechanisms for IDILI.

  1. Inflammation/Cytokines (also discussed in other sections of this post):  Inflammation has long been associated with human cases of DILI.    Many cytokines and inflammatory mediators have been implicated including TNFα, IL7, TGFβ, and IFNϒ (viral infection) leading some to conclude that serum measurement of cytokines could be a potential biomarker for DILI[4].  In addition, ROS (see below) is generated from inflammation and also considered a risk factor for DILI[5].
  2. Reactive Oxygen (ROS)/Reactive Metabolites: Oxidative stress, either generated from reactive drug metabolites or from mitochondrial sources, has been shown to be involved in apoptotic and necrotic cell death.  Both alterations in the enzymes involved in the generation of and protection from ROS have been implicated in increased risk to DILI including (as discussed further) alterations in mitochondrial superoxide dismutase 2 (SOD2) and glutathione S-transferases.  Both ROS and inflammatory cytokines can promote JNK signaling, which has been implicated in DILI[6].

Dr. Neil Kaplowitz suggested that we:

“develop a unifying hypothesis that involves underlying genetic or acquired mitochondrial abnormalities as a major determinant of susceptibility for a number of drugs that target mitochondria and cause DILI. The mitochondrial hypothesis, implying gradually accumulating and initially silent mitochondrial injury in heteroplasmic cells which reaches a critical threshold and abruptly triggers liver injury, is consistent with the findings that typically idiosyncratic DILI is delayed (by weeks or months), that increasing age and female gender are risk factors and that these drugs are targeted to the liver and clearly exhibit a mitochondrial hazard in vitro and in vivo. New animal models (e.g., the Sod2(+/-) mouse) provide supporting evidence for this concept. However, genetic analyses of DILI patient samples are needed to ultimately provide the proof-of-concept”[7].

Clin Infect Dis. 2004 Mar 38(Supplement 2) S44-8, Figure 1

Clin Infect Dis. 2004 Mar 38(Supplement 2) S44-8, Figure 3

Figures. Mechanisms of Drug-Induced Liver Injury and Factors related to the occurrence of  DILI (used with permission from Oxford Press; reference [7])

To this end, Dr. Brett Howell and other colleagues at the Hamner-UNC Institute for Drug Safety Sciences (IDSS) developed an in-silico model of DILI ( the DILISym™ model)which is based on  depletion of cellular ATP and reactive metabolite formation as indices of DILI.

Have there been Genetic Risk Factors identified for DILI?

Candidate-gene-associated studies (CGAS) have been able to identify several genetic risk factors for DILI including:

  1. Uridine Diphosphate Glucuronosyltransferase 2B7 (UGT2B7): variant increased susceptibility to diclofenac-induced DILI
  2. Adenosine triphosphate-binding cassette C2 (ABCC2) variant ABCC-24CT increased susceptibility to diclofenac-induced DILI
  3. Glutathione S-transferase (GSTT1): patients with a double GSTT1-GSTM1 null genotype had a significant 2.7 fold increased risk of DILI from nonsteroidal anti-inlammatory agents, troglitazone and tacrine.  GSTs are involved in the detoxification of phase 1 metabolites and also protect against cellular ROS.

Although these CGAS confirmed these genetic risk factors,  Stefan Russman suggests a priori genome-wide association studies (GWAS) might provide a more complete picture of genetic risk factors for DILI as CGAS is limited due to

  1. Candidate genes are selected based on current mechanisms and knowledge of DILI so genetic variants with no known knowledge of or mechanistic information would not be detected
  2. Many CGAS rely on analysis of a limited number of SNP and did not consider intronic regions which may control gene expression

A priori GWAS have the advantage of being hypothesis-free, and although they may produce a high number of false-positives, new studies of genetic risk factors of ximelagatran, flucioxaciliin and diclofenac-induced liver injury are using a hybrid approach which combines the whole genome and unbiased benefits of GWAS with the confirmatory and rational design of CGAS[8-10].

Even though idiosyncratic DILI is rare, the severity, unpredictable onset, and unknown etiology and risk factors have prompted investigators such as Stefan Russmann from University Hospital Zurich and Ignazio Grattagliano from University of Bari to suggest:

Identification of risk factors for rare idiosyncratic hepatotoxicity requires special networks that contribute to data collection and subsequent identification of environmental as well as genetic risk factors for clinical cases of idiosyncratic DILI[11].

Therefore, a DILI network project (DILIN) had been developed to collect samples and detailed genetic and clinical data on IDILI cases from multiple medical centers.  The project aims to identify the upstream and downstream genetic risk factors for IDILI[12].  Please see a SlideShare presentation here of the goals of the DILI network project.

Drs Colin Spraggs and Christine Hunt had reviewed possible genetic risk factors of DILI seen with various tyrosine kinase inhibitors (TKIs) including Lapatinib (Tykerb/Tyverb©, a dual inhibitor of  HER2/EGFR heterodimer) and paopanib (Votrient©; a TKI that targets VEGFR1,2,3 and PDGFRs)[13].

From a compilation of studies:

  • Elevation in serum bilirubin during treatment with lapatinib and pazopanib are associated with UGT1A1 polymorphism related to Gilbert’s syndrome (a clinically benign syndrome)
  • Anecdotal evidence shows that polymorphisms of lapatinib and pazopanib metabolizing enzymes may contribute to differences seen in onset of DILI
  • Pazopanib-induced elevations of ALT correlate with HFE variants, suggesting alterations in iron transport may predispose to DILI
  • Strong correlations between lapatinib-induced DILI and class II HLA locus suggest inflammatory stress response important in DILI

Note that these clinical findings were not evident from the preclinical tox studies. According to the European Medicines Agency assessment report for Tykerb states: “the major findings in repeat dose toxicity studies were attributed to lapatinib pharmacology (epithelial effect in skin and GI system.  The toxic events occurred at exposures close to the human exposure at the recommended dose.  Repeat-dose toxicity studies did not reveal important safety concerns than what would be expected from the mode of action”.

However, it should be noted that in high dose repeat studies in mice and rats, severe lethality was seen with hematologic, gastrointestinal toxicities in combination with altered blood chemistry parameters and yellowing of internal organs.

IAP Antagonists, Mechanism of Action, and Clinical Trials:

A few IAP antagonists which are in early stage development include:

  • Norvatis IAP Inhibitor LCL161: at 2012 San Antonia Breast Cancer Symposium, a phase 1 trial in triple negative breast cancer showed promising results when given in combination with paclitaxel.
  • Ascenta Therapeutics IAP inhibitor AT-406 in phase 1 in collaboration with Debiopharm S.A. showed antitumor efficacy in xenograft models of breast, pancreatic, prostate and lung cancer. The development of this compound is described in a paper by Cai et. al.

National Cancer Institute sponsored trials using antagonists of IAPs include

  • Phase II Study of Birinapant for Advanced Ovarian, Fallopian Tube, and Peritoneal Cancer (NCI-12-C-0191). Principle Investigator: Dr. Christina Annunziata. See the protocol summary. More open trials for this drug are located here.  Closed trials including safety studies can be found here.
  • A Phase 1 non-randomized dose escalation study to determine maximum tolerated dose (MTD) and characterize the safety for the TetraLogic compound TL32711 had just been completed. Results have not been published yet.
  • Closed Clinical trials with the IAP antagonist HGS1029 in advanced solid tumors determined that weekly i.v. administration of HGS1029 reported a safety issue for primary outcome measures

A great review on IAP proteins and their role as regulators of apoptosis and potential targets for cancer therapy [14] can be found as a part of a Special Issue in Experimental Oncology “Apoptosis: Four Decades Later”.  Human IAPs (inhibitors of apoptosis) consist of eight proteins involved in cell death, immunity, inflammation, cell cycle, and migration including:

In general, IAP proteins are directly involved in inhibiting apoptosis by binding and directly inhibiting the effector cysteine protease caspases (caspase 3/7) ultimately responsible for the apoptotic process [15].  IAPs were actually first identified in baculoviral genomes because of their ability to suppress host-cell death responses during viral infection [16]. IAP proteins are often overexpressed in cancers [17].

Apoptosis is separated into two pathways, defined by the initial stress or death signal and the caspases involved:

  1. Extrinsic pathway: initiated by TNFα and death ligand FasLigand;  involves caspase-8; process inhibited by IAP1/2
  2. Intrinsic pathway: initiated by DNA damage, irradiation, chemotherapeutics; mitochondrial pathway involving caspase 9 and cytochrome c release from mitochondria; mitochondria also releases SMAC/DIABLO, which binds and inhibits XIAP (XIAP inhibits the Intrinsic apoptotic pathway.

 intrinsicextrinsicapoptosiswikidot

 

Intrinsic and Extrinsic pathways of apoptosis. Figure photocredit (wikidot.com)

The Curis IAP antagonist (and others) is a SMAC small molecule mimetic. It is interesting to note [18, 19] that IAP antagonists can result in death by

  • Apoptosis: an IAP antagonist in presence of competent TNFα signaling
  • Necrosis: seen with IAP inhibitors in cells with altered TNFα signaling or with presence of caspase inhibitors

IAPs are also involved in the regulation of signaling pathways such as:

NF-ΚB signaling pathway

NF-ΚB is a “rapid-acting” transcription factor which has been found to be overexpressed in various cancers.  Under most circumstances NF-ΚB translocation to the nucleus results in transcription of genes related to cell proliferation and survival.  NF-ΚB signaling is broken down in two pathways

  1. Canonical:  Canonical pathway can be initiated (for example in inflammation) when TNF-α binds its receptors activating  death domains (TRADD)
  2. Noncanonical: since requires new protein synthesis takes longer than canonical signaling.  Can be initiated by other TNF like ligands like CD40

IAP1/2 is a negative regulator of the noncanonical NF-ΚB signaling pathway by promoting proteosomal degradation of the TRAF signaling complex. A wonderfully annotated list of NF-ΚB target genes can be found on the Thomas Gilmore lab site at Boston University at http://www.bu.edu/nf-kb/gene-resources/target-genes/ .

NF-ΚB has been considered a possible target for chemotherapeutic development however Drs. Veronique Baud and Michael Karin have pondered the utility of IAP antagonists as a good target in their review: Is NF-ΚB a good target for cancer therapy?: Hopes and pitfalls [20].  The authors discuss issues such that IAP antagonism induced both the classical and noncanonical NF-ΚB pathway thru NIK stabilization, resulting in stabilization of NF-ΚB signaling and thereby undoing any chemotherapeutic effect which would be desired.

AKT signaling

IAPs have been shown to interact with other proteins including a report that SIAP regulates AKT activity and caspase-3-dependent cleavage during cisplatin-induced apoptosis in human ovarian cancer cells and could be another mechanism involved in cisplatin resistance[21].   In addition there have been reports that IAPs can regulate JNK and MAPK signaling.

Therefore, IAPs are involved in CANONICAL and NONCANONICAL pathways.

IAPs can Regulate Pro-Inflammatory Cytokines

A recent 2013 JBC paper [22]showed that IAPs and their antagonists can regulate spontaneous and TNF-induced proinflammatory cytokine and chemokine production and release

  • IAP required for production of multiple TNF-induced proinflammatory mediators
  • IAP antagonism decreased TNF-mediated production of chemokines and cytokines
  • But increased spontaneous release of chemokines

In addition Rume Damgaard and Mads Gynd-Hansen have suggested that IAP antagonists may be useful in treating inflammatory diseases like Crohn’s disease as IAPs regulate innate and acquired immune responses[23].

Toxicity profiles of IAP antagonists

NOTE: In a paper in Toxicological Science from 2012[24], Rebecca Ida Erickson form Genentech reported on the toxicity profile of the IAP antagonist GDC-0152 from a study performed in dogs and rats. A dose-dependent toxicity profile from i.v. administration was consistent with TNFα-mediated toxicity with

  • Elevated plasma cytokines and an inflammatory leukogram
  • Increased serum transaminases
  • Inflammatory infiltrate and apoptosis/necrosis in multiple tissues

In a related note, a similar type of fatal idiosyncratic hepatotoxicity was reported in a 62 year-old man treated with the Raf kinase inhibitor sorafenib for renal cell carcinoma[25]: Fatal case of sorafenib-associated idiosyncratic hepatotoxicity in the adjuvant treatment of a patient with renal cell carcinoma; Case Report  in BMC Cancer.

At week four after initiation of sorafenib treatment, the patient noticed increasing fatigue, malaise, gastrointestinal discomfort and abdominal rash.  Although treatment was discontinued, jaundice developed and blood test revealed an acute hepatitis with

  • Elevated serum ALT
  • Elevated serum alkaline phosphatase
  • Increased prothrombin time
  • Increased LDH

…elevated levels seen in the case with the aforementioned IAP antagonist.  Autopsy revealed

  • Lobular hepatitis
  • Mononuclear cell infiltrate
  • Hepatocyte necrosis

These findings are in line with a drug-induced inflammation and IDILI. In addition to hepatotoxicity, renal insufficiency developed in this patient. The authors had suggested the death was probably due to “an idiosyncratic allergic reaction to sorafenib manifesting as hepatotoxicity with associated renal impairment”.  The authors also noted that genome wide association studies of idiosyncratic drug-induced liver injury support involvement of major histocompatibility complex (MHC) polymorphisms[26].  MHC involvement has also been associated with lapatanib and pazopanib hepatotoxicity [27, 28].

Curis has been involved in another novel oncology therapeutic, a first in class.

Last year Roche and Genentech had won approval for a Hedgehog pathway inhibitor vismodegib for treatment of advanced basal cell carcinoma (reported at FierceBiotech©). Vismodegib was initially developed in collaboration with Curis, Inc.  The hedgehog signaling pathway, which controls the function of Gli factors (involved in stem cell differentiation), is overactive in advanced basal cell carcinoma as well as other cancer types.

As an additional reference, the FDA National Center for Toxicological Research has developed THE LIVER TOXICITY KNOWLEDGE BASE (LTKB).

“The LTKB is a project designed to study drug-induced liver injury (DILI). Liver toxicity is the most common cause for the discontinuation of clinical trials on a drug, as well as the most common reason for an approved drug’s withdrawal from the marketplace. Because of this, DILI has been identified by the FDA’s Critical Path Initiatives as a key area of focus in a concerted effort to broaden the agency’s knowledge for better evaluation tools and safety biomarkers.”

A nice SlideShow of Toxicity of Targeted Therapies can be found here: http://www.slideshare.net/RashaHaggag/toxicities-of-targeted-therapies

Also please note that ALL GENES in this article are linked to their GENECARD 

UPDATED 8/12/2022

 

Zolgensma Gene Therapy Linked to 2 Deaths in SMA Patients, Novartis Reports

The 2 deaths, due to acute liver failure, occurred in patients treated in Kazakhstan and Russia.

Two children with spinal muscular atrophy (SMA) have died after being treated with onasemnogene abeparvovec (Zolgensma; Novartis) from acute liver failure, a known safety risk of the therapy.1

Novartis has updated the FDA and other regulatory agencies in countries that Zolgensma is approved in, including Russia and Kazakhstan, where the deaths occurred. The company will also update the labeling of Zolgensma to include the deaths.

“While this is important safety information, it is not a new safety signal and we firmly believe in the overall favorable risk/benefit profile of Zolgensma, which to date has been used to treat more than 2300 patients worldwide across clinical trials, managed access programs, and in the commercial setting,” Novartis said in an emailed statement to BioPharma Dive.2

Zolgensma’s labeling includes the risk of liver injury and instructs clinicians to assess liver function before treatment and to manage liver enzyme counts with steroid treatment. The 2 deaths occurred 5 to 6 weeks after the one-time infusion and 1 to 10 days after corticosteroid treatment was tapered, according to an initial report from Stat News.1

READ MORE: Zolgensma Shows Efficacy in SMA With 3 SMN2 Copies

An FDA advisory committee meeting that took place last fall identified risks of adeno associated virus (AAV) gene therapies including, specifically, Zolgensma.2 The committee recommended caution, but nothing that would hinder gene therapy development.

Zolgensma, which was approved in the US in May 2019, just recently demonstrated further positive data from SPR1NT (NCT03505099), a phase 3 multicenter, single-arm trial on its effect in presymptomatic children with SMA in 2 articles published in Nature Medicine.3,4

All children in both the type 1 and type 2 cohorts achieved the ability to independently sit and most achieved other age-appropriate milestones including standing and walking. None of the children in the study required respiratory support or nutritional support, and there were no serious treatment-related adverse events observed.

“The robust data from both the 2- and 3-copy SPR1NT cohorts are being published together for the first time, further supporting the significant and clinically meaningful benefit of Zolgensma in presymptomatic babies with SMA,” Shephard Mpofu, MD, SVP, chief medical officer, Novartis Gene Therapies, said in a previous statement.5 “When treated with Zolgensma prior to the onset of symptoms, not only did all 29 patients enrolled in SPR1NT survive, but were thriving—breathing and eating on their own, with most even sitting, standing, and walking without assistance.”

REFERENCE

1. Silverman E. Novartis reports two children died from acute liver failure after treatment with Zolgensma gene therapy. STAT. August 11, 2022. https://www.statnews.com/pharmalot/2022/08/11/novartis-zolgensma-liver-failure-gene-therapy-death/

2. Pagliarulo N. Novartis reports deaths of two patients treated with Zolgensma gene therapy. BioPharma Dive. August 12, 2022. https://www.biopharmadive.com/news/novartis-zolgensma-patient-death-liver-injury/629542/

3. Strauss KA, Farrar MA, Muntoni F, et al. Onasemnogeneabeparvovec for presymptomatic infants with two copies of SMN2 at risk for spinal muscular atrophy type 1: the Phase III SPR1NT trial. Nat Med. Published online June 17, 2022. doi:10.1038/s41591-022-01866-42

4. Strauss KA, Farrar MA, Muntoni F, et al. Onasemnogeneabeparvovec for presymptomatic infants with three copies of SMN2 at risk for spinal muscular atrophy: the Phase III SPR1NT trial. Nat Med. Published online June 17, 2022.doi: 10.1038/s41591-022-01867-3

5. Novartis announces Nature Medicine publication of Zolgensma data demonstrating age-appropriate milestones when treating children with SMA presymptomatically. News release. Novartis. June 17, 2022. https://firstwordpharma.com/story/5597735

 

REFERENCES

1.            Roth RA, Ganey PE: Intrinsic versus idiosyncratic drug-induced hepatotoxicity–two villains or one? The Journal of pharmacology and experimental therapeutics 2010, 332(3):692-697.

2.            Waring JF, Liguori MJ, Luyendyk JP, Maddox JF, Ganey PE, Stachlewitz RF, North C, Blomme EA, Roth RA: Microarray analysis of lipopolysaccharide potentiation of trovafloxacin-induced liver injury in rats suggests a role for proinflammatory chemokines and neutrophils. The Journal of pharmacology and experimental therapeutics 2006, 316(3):1080-1087.

3.            Deng X, Luyendyk JP, Ganey PE, Roth RA: Inflammatory stress and idiosyncratic hepatotoxicity: hints from animal models. Pharmacological reviews 2009, 61(3):262-282.

4.            Laverty HG, Antoine DJ, Benson C, Chaponda M, Williams D, Kevin Park B: The potential of cytokines as safety biomarkers for drug-induced liver injury. European journal of clinical pharmacology 2010, 66(10):961-976.

5.            Schwabe RF, Brenner DA: Mechanisms of Liver Injury. I. TNF-alpha-induced liver injury: role of IKK, JNK, and ROS pathways. American journal of physiology Gastrointestinal and liver physiology 2006, 290(4):G583-589.

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Effect of Dietary Magnesium Intake on Insulin Resistance

Reporter: Larry H. Bernstein, MD, FCAP

Dietary Magnesium Intake Improves Insulin Resistance among Non-Diabetic Individuals with Metabolic Syndrome Participating in a Dietary Trial

J Wang1,2,†, G Persuitte3,†, BC Olendzki2, NM Wedick2, …, and Yunsheng Ma 2,*
1 Department of Preventive Medicine, Medical School of Yangzhou University, Yangzhou 225001, China
2 Division of Preventive and Behavioral Medicine, Department of Medicine, University of Massachusetts Medical School, Worcester, MA 01655, USA
3 Division of Biostatistics and Health Services Research, Department of Quantitative Health Science, University of Massachusetts Medical School, Worcester, MA 01655, USA †

Nutrients 27 Sep 2013; 5(10):3910-3919; http://dx.doi.org/10.3390/nu5103910

Many cross-sectional studies show

  1. an inverse association between dietary magnesium and insulin resistance, but
  2. few longitudinal studies examine the ability to meet the Recommended Dietary Allowance (RDA)
  • for magnesium intake through food and
  • its effect on insulin resistance among participants with metabolic syndrome (MetS).

The dietary intervention study examined this question in 234 individuals with MetS. Magnesium intake was assessed using 24-h dietary recalls at baseline, 6, and 12 months.

  1. Fasting glucose and insulin levels were collected at each time point; and
  2. insulin resistance was estimated by the homeostasis model assessment (HOMA-IR).

The relation between magnesium intake and HOMA-IR was assessed using linear mixed models adjusted for covariates.

  • Baseline magnesium intake was 287 ± 93 mg/day (mean ± standard deviation), and
  • HOMA-IR, fasting glucose and fasting insulin were 3.7 ± 3.5, 99 ± 13 mg/dL, and 15 ± 13 μU/mL, respectively.

At baseline, 6-, and 12-months, 23.5%, 30.4%, and 27.7% met the RDA for magnesium. After multivariate adjustment,

    • magnesium intake was inversely associated with metabolic biomarkers of insulin resistance (P < 0.01).

Further, the likelihood of elevated HOMA-IR (>3.6) over time was 71% lower [odds ratio (OR): 0.29; 95% confidence interval (CI): 0.12, 0.72] in participants

  • in the highest quartile of magnesium intake than those in the lowest quartile.

For individuals meeting the RDA for magnesium,

  • the multivariate-adjusted OR for high HOMA-IR over time was 0.37 (95% CI: 0.18, 0.77).

These findings indicate that dietary magnesium intake is inadequate among non-diabetic individuals with MetS and suggest that

    • increasing dietary magnesium to meet the RDA has a protective effect on insulin resistance.

Keywords: magnesium; insulin resistance; metabolic syndrome; epidemiology

Cite This Article

Wang J, Persuitte G, Olendzki BC, Wedick NM, Zhang Z, Merriam PA, Fang H, Carmody J, Olendzki G-F, Ma Y. Dietary Magnesium Intake Improves Insulin Resistance among Non-Diabetic Individuals with Metabolic Syndrome Participating in a Dietary Trial. Nutrients. 2013; 5(10):3910-3919.

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