Rensselaer In The News: 7 Cool New Findings About the Brain PDF Print E-mail
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Tuesday, 14 January 2014 11:02

January 9, 2014 | via: Huffington Post - Peter Tessier of Rensselaer Polytechnic Institute is working to engineer antibodies that have precise properties. By placing DNA sequences from a target protein within antibodies, Tessier may design the antibodies to bind to select proteins, such as proteins linked with Alzheimer's called beta-amyloid plaques. Further research may lead to the development of antibodies that recognize and remove toxic particles before they do harm.

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Last Updated on Tuesday, 14 January 2014 11:14
Congenital Diaphragmatic Hernia Traced from Genetic Roots to Physical Defect PDF Print E-mail
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Tuesday, 14 January 2014 10:27

Rensselaer Researchers Contribute to Discovery of Gene Associated With Deadly Birth Defect


Troy, N.Y. – A team including researchers from Rensselaer Polytechnic Institute have discovered that a specific gene may play a major role in the development of a life-threatening birth defect called congenital diaphragmatic hernia, or CDH, which affects approximately one out of every 3,000 live births.


The hallmark of CDH is a rupture of the diaphragm that allows organs found in the lower abdomen, such as the liver, spleen, and intestines, to push their way into the chest cavity. The invading organs crowd the limited space and can lead to abnormal lung and heart development or poor heart and lung function, which, depending on the severity of the condition, can cause disability or death.


In a paper published recently in the Journal of Clinical Investigation, lead authors at the University of Georgia, along with colleagues from the Rensselaer and the University of California at San Diego, demonstrated for the first time that the gene NDST1 plays a significant role in the proper development of the diaphragm, and that abnormal expression of the gene could lead to CDH.


“We now have a really good picture of this abnormality in mice, and we suspect it is very similar in humans,” said Fuming Zhang, a research professor in the laboratory of Robert J. Linhardt, the Ann and John H. Broadbent Jr ’59 Senior Constellation Professor of Biocatalysis and Metabolic Engineering, and a member of the Center for Biotechnology and Interdisciplinary Studies at Rensselaer. “What this gives us is a total view, from the genetic level, to the molecular level, to the cellular or tissue level, to something that a physician would see — a hernia in a newborn.”


The discovery began with the observation that mice bred without the NDST1 gene, which produces the eponymous NDST1 enzyme, are more likely to develop CDH than ordinary mice. The enzyme NDST1 is one of four isoforms — a group of molecules that are chemically similar, but show subtle functional differences. In mice lacking the NDST1 gene, and therefore the NDST1 enzyme, nature substitutes with an NDST1 isoform (NDST2, NDST3, and NDST4), but the results — like substitutions in cooking — are noticeable.


In the absence of NDST1, blood vessels supplying the developing diaphragm muscles formed inconsistently, leading to weak points in the muscle tissues that make them prone to hernia. Researchers knew that the NDST1 enzyme is involved in the synthesis of heparan sulfate, so the group turned to the Linhardt’s research team at Rensselaer – experts in heparan sulfate and glycosaminoglycan analysis – to pinpoint the biochemical basis for the abnormality.


“There are two molecules in the interaction that leads to proper blood vessel formation in the diaphragm — NDST1 biosynthesized heparan sulfate and the protein SLIT3,” said Zhang. “In order for those interactions to be successful, and for blood vessels to form properly, everything must be accomplished within a specific time frame and having a specific structure. We were able to investigate the interactions between the two.”


Zhang used surface plasmon resonance spectroscopy to measure aspects of the interaction such as the rate at which the two molecules bound together, the strength of their interaction, and the molecular structure of heparan sulfate required for a successful interaction. The results of his measurements explain the inconsistent blood vessel growth and weak muscle tissue observed in the mice.


“The binding strength, the binding rate, and the length of the heparan sulfate required for binding to the SLIT3 protein are inadequate for the job in this defect,” said Zhang. “We were able to understand why, at a molecular level, this failure in development takes place.”


Linhardt said the findings allow researchers to think about “routes for intervention at all levels.” Gene therapy might supply the correct gene, drugs might deliver a substitute molecule, tissue engineering might enable the tissue to repair itself, or a surgeon might repair the damage after a hernia has occurred.


“We understand that the muscle is damaged because blood flow is damaged because the vascular system feeding the blood flow isn’t forming properly,” said Linhardt. “Because we now understand what is wrong, it allows us to think about the opportunity for therapy at all levels.”



Mary Martialay

Rensselaer Polytechnic Institute

(518) 276-2146

(518) 951-5650 (mobile) 

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Last Updated on Tuesday, 14 January 2014 10:51
RPI - ISMMS Seed Funding PDF Print E-mail
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Friday, 10 January 2014 10:29

We are pleased to announce the awardees of the inaugural Rensselaer-­‐Icahn School of Medicine at Mount Sinai seed funding program to advance collaborative science between the two institutions. These projects were selected from among 29 excellent applications. The remarkably enthusiastic response reflects a strong mutual interest in aligning the strengths of each institution to advance discovery and innovation in biomedical sciences and engineering. These projects underscore the value of cross-­‐disciplinary teams in translating our science into new technologies.

We congratulate the awardees and all the applicants for embracing this opportunity, and look forward to learning of the new advances the projects generate.

Awardees (Rensselaer PI listed first):

1. Effects of Retrotransposons on genome stability and consequence for the biology of aging and cancer (P. Maxwell & M. O’Connor)
2. In situ generation of tissue-­‐engineered vascular conduits using PDGFRα+ vascular progenitor cells (M. Hahn & J. Kovacic)
3. Inhibiting hepatitis C virus with high affinity single-­‐domain antibodies (P. Tessier & M. Evans)
4. Proteoglycan metabolism and painful intervertebral disc degeneration (R. Linhardt & J. Iatridis)
5. Toward a Universal Influenza Virus Vaccine: Development of Nanoscale Constructs that Elicit Broadly Neutralizing Antibodies (R. Kane & P. Palese)
6. Continuous Monitoring of Compartmental Pressures for Objective Diagnosis of Compartment Syndrome (E. Ledet, K. Connor & D. Forsh, J. Gladstone)
7. Inducing Targeted Mutations in Cells in the Brain In Vivo (can Dopamine Transporter be modified to resist drug abuse) (S. Kotha & E. Nestler)
8. ReDrugS: Repurposing Drugs using Semantics (D. McGuinness & J. Dudley)

The Rensselaer-­‐Icahn School of Medicine at Mount Sinai Joint Steering Committee
Rensselaer: Jonathan Dordick, Wolf van Maltzahn, Deepak Vashishth
Mount Sinai: Geoffrey Smith, John Morrison, Scott Friedman


Last Updated on Friday, 10 January 2014 10:33
Researchers at Rensselaer Polytechnic Institute Uncover Mechanism of Genetic Mutations Known To Cause Familial Alzheimer’s Disease PDF Print E-mail
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Friday, 10 January 2014 08:57
Researchers at Rensselaer Polytechnic Institute Uncover Mechanism of Genetic Mutations Known To Cause Familial Alzheimer’s Disease
Thu, 2014-01-09 15:37 -- katzme

New Study Pinpoints Structural Effects of V44M and V44A Mutations

January 9, 2014

New research, led by Rensselaer Polytechnic Institute researcher Chunyu Wang, has solved one mystery in the development of Familial Alzheimer’s Disease (FAD), a genetic variant of the disease that affects a small fraction of the Alzheimer’s population. In a paper published January 6 in the journal Nature Communications, Wang and his team follow the trail of two genetic mutations – V44M and V44A – known to cause FAD, and show how the mutations lead to biochemical changes long linked to the disease.

The hallmark of FAD is the accumulation of the Amyloid Beta 42 peptide (a short chain of amino acids) in unusually high concentrations within the brain. In a healthy brain, Amyloid Beta-42 (Aβ42) and a similar peptide, Amyloid Beta-40 (Aβ40), are found in a ratio of about 1 to 9. In a brain affected by FAD, this ratio is much higher. The two peptides are nearly identical:  Aβ40 is a chain of 40 amino acids in length; Aβ42 is 42 amino acids in length. However, Aβ42 is much more toxic to neurons and plays a critical role in memory failure.

“The mutations that cause FAD lead to an increased ratio of Aβ42 over Aβ40,” said Wang, an associate professor of biological sciences within the School of Science, director of the biochemistry and biophysics graduate program, and member of the Rensselaer Center for Biotechnology and Interdisciplinary Studies, who co-wrote the paper with Wen Chan, a graduate student at Rensselaer. “That’s the biochemistry, and that has been observed by many people. But the question we asked is: how? How do the mutations lead to this increased ratio?”

There are hundreds of known genetic mutations linked to FAD, but they are all related to the processing of a large protein, the amyloid precursor protein (APP), which starts its life partially embedded in the cell membrane of brain cells, and is later cut into several pieces, one of which becomes either Aβ42 or Aβ40.

In a multi-step process, enzymes make several cuts to APP, and the location of the cuts dictates whether a resulting snippet of APP becomes Aβ42 or Aβ40. If an enzyme, γ-secretase, makes an initial cut at an amino acid within APP called Threonine 48 (T48), the remaining cuts result in Aβ42, whereas if the first cut is made at amino acid Leucine 49, the process will result in Aβ40.

Wang’s team used solution nuclear magnetic resonance spectroscopy to study the three-dimensional structure and dynamics of the transmembrane portion of APP affected by the two genetic mutations, and they discovered that the mutations cause a critical change to the T48 amino acid. That change makes it more likely that γ-secretase will prefer a cut at T48, leading to production of Aβ42, and increased concentrations of Aβ42 found in the brains of patients with FAD.

“The basic idea is that – in the mutated versions – this site, T48, becomes more open, more accessible to γ-secretase,” said Wang. “What we found is that the FAD mutation basically opens up the T-48 site, which makes it more likely for γ-secretase to produce Aβ42 peptide.”

The paper, titled “Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of Ɛ-cleavage site,” is available online at:

Last Updated on Monday, 13 January 2014 08:35
Rensselaer Polytechnic Institute Partners with Icahn School of Medicine at Mount Sinai to Train Tomorrow’s Health Care and Technology Leaders PDF Print E-mail
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Thursday, 05 December 2013 11:24

New $5 Million Research and Technology Hub at Mount Sinai is Critical Part of New $100 Million Public-Private Partnership to Boost New York City’s Biotechnology and Entrepreneurship Sectors

December 4, 2013

Rensselaer Polytechnic Institute will strengthen its strategic partnership with the Icahn School of Medicine at Mount Sinai on the launch of the new Mount Sinai Institute of Technology (MSIT).

Announced today as part of a $100 million public-private initiative to boost biotechnology innovation in New York, MSIT aims to educate a new generation of experts and create new technologies to help address and solve the world’s most critical health-care challenges. See the full announcement at:

MSIT is supported by $5 million from the city of New York.

“The Mount Sinai Institute of Technology is a robust extension of our partnership with the Icahn School of Medicine,” said Rensselaer President Shirley Ann Jackson. “This research and technology hub will enable innovation and discovery in biomedical technologies, health-care analytics, and education, and will drive economic development and improved health care. Rensselaer will work closely with Mount Sinai to foster the growth of the MSIT, while expanding opportunities to build Rensselaer-driven biomedical technologies upstate.”

“We are grateful to the New York City Economic Development Corporation and the administration of Mayor Michael R. Bloomberg for their generous support in helping to make MSIT a reality,” said Dennis S. Charney, the Anne and Joel Ehrenkranz Dean of Icahn School of Medicine at Mount Sinai and executive vice president for academic affairs at the Mount Sinai Medical Center. “The city has long recognized the need to expand applied science education and to establish research facilities for these efforts. The work that we’ll carry out at the Institute – from basic research to developing medical technology and devising effective treatments – will ultimately go a long way toward helping improve patient outcomes and the quality of life for people in New York City and beyond.”

MSIT seeks to transform biomedicine through discovery and development of technology-based solutions to critical unmet health-care needs. Students and faculty will engage in academic research, product development, and active entrepreneurship in areas including Big Data, cloud computing, social networking, scientific and clinical simulation, tissue engineering, sensors, microprocessors, robotics, mechatronics, drug delivery and nanomedicine, and other areas, ultimately conferring graduate degrees in Design, Technology, and Entrepreneurship (Ph.D.) and Biomedical Informatics (M.S.).

As part of the MSIT program, which will begin in the fall of 2014, Rensselaer and Mount Sinai will collaborate on the creation of five multidisciplinary research teams. Comprised of faculty members, post-doctoral scholars, and students from both institutions, each team will be devoted to solving a specific technology problem.

This collaboration furthers the partnership between Rensselaer and Mount Sinai, which in May 2013  announced an affiliation agreement to collaborate on educational programs, research, and development of new diagnostic tools and treatments that promote human health. The affiliation leverages the expertise of Rensselaer in engineering and invention prototyping and the expertise of Mount Sinai in biomedical research and patient care to develop joint educational programs, create complementary research programs, and to seek joint research funding.

The affiliation expands the research conducted at both institutions in the areas of neuroscience and neurological diseases, genomics, imaging, orthopaedics, cancer, cardiovascular disease, and scientific and clinical targets. Funding for projects will be sought on topics including precision medicine, drug discovery, stem cell biology, robotics and robotic surgery, novel imaging techniques, cellular engineering, and computational neurobiology.

Big Data, broad data, high performance computing, data analytics, and Web science are creating a significant transformation globally in the way we make connections, make discoveries, make decisions, make products, and, ultimately, make progress. The collaboration with Mount Sinai on MSIT, under the auspices of the Rensselaer Institute for Data Exploration and Applications – or The Rensselaer IDEA, is part of the university-wide effort at Rensselaer to maximize the capabilities of these tools and technologies for the purpose of expediting scientific discovery and innovation, developing the next generation of these digital enablers, and preparing our students to succeed and lead in this new data-driven world.

For more on the alliance between Rensselaer and Mount Sinai, see:

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