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Annual JMBGSA Research Symposium Table of Contents Letter from Organizers ………………………… 2-3 Symposium Schedule …………………………….. 4 Annual JMBGSA Keynote Address ……………………………….. 5-6 Research Abstracts – Oral ………………………………. 7-10 Symposium Abstracts – Poster …………………………… 11-23 Participants ……………………………………… 24 Sponsors …………………………………………. 27 Friday March 24, 2017 10:00AM - 4:30PM Atrium – Life Sciences Building Busch Campus, Rutgers University 1 Letter from Organizers participate as judges and give students feedback on their work. Since this event would not be possible without the participation of Welcome to the 11th Annual Graduate Student Symposium our fellow graduate students, we applaud their efforts and thank hosted by the Joint Molecular Biosciences Graduate Student them for their poster presentations and talks. We would like to Association (JMBGSA) of Rutgers University. We are delighted to offer a very special thank you to all our generous sponsors as well have you join us today to support the outstanding work that for supporting graduate student research at Rutgers. Thank you for graduate students in the Molecular Biosciences Graduate Programs joining us for this symposium and we hope you enjoy your time have been producing throughout their different stages of graduate spent here today! learning. As a student organization, the goal of JMBGSA is to Sincerely, facilitate the professional development of graduate students and JMBGSA Executive Board 2016-2017 promote opportunities for social interaction with their peers. By presenting their work to a critical audience, graduate students are able to hone important presentation skills and receive input on their work from faculty and peers from various departments. With these goals in mind, we organize the annual symposium and look to the university community to make it a success. Through this symposium, we hope to not only showcase the graduate student research, but also to provide a platform for professional interaction between students, faculty and administration. We are proud to be able to provide the avenue for students from different fields of bioscience research to showcase their scientific endeavors. Through both the oral and poster presentations, we seek to highlight some of the interesting basic and translational research that is being conducted at Rutgers. We want to take this opportunity to acknowledge our gratitude to our faculty advisor, Dr. Janet Alder, for her incredible guidance and support during the planning process of this and other events throughout the year. We also want to thank the graduate student offices of both the Graduate School – New Brunswick (GSNB) and the Graduate School of Biomedical Sciences (GSBS) for their help and support. We gratefully acknowledge the faculty members who have taken time out from their busy schedules to 2 3 Symposium Schedule Keynote Address Dr. Steven K. Libutti Registration and 9:30 - 10:00AM Introduction Director of Rutgers Cancer Institute of New Jersey Vice Chancellor for Cancer Programs for Rutgers Biomedical and Health Sciences at Rutgers University 10:00 - 11:00AM Oral Presentations I "Of Mice and Men(in) and What I 11:00 - 12:00PM Poster Presentations I have Learned from Both” 12:00 - 1:00PM Keynote Address A graduate of Harvard College, Dr. Steven Libutti received his MD from the Columbia University College of 1:00 - 2:00PM LUNCH Physicians and Surgeons. Following his residency in surgery, he completed a fellowship in Surgical Oncology and 2:00 - 3:00PM Poster Presentations II Endocrine Surgery in the Surgery Branch of the National Cancer Institute and was ultimately a tenured Senior 3:00 - 4:00PM Oral Presentations II Investigator and Chief of the Tumor Angiogenesis Section in the Surgery Branch, NCI. Dr. Libutti served as Director for the Montefiore Einstein Center for Cancer Care in New York City and 4:00 - 4:30PM Award Ceremony was a Professor and Vice Chairman of the Department of Surgery and a Professor in the Department of Genetics at Albert Einstein College of Medicine and Montefiore Health System. In January 2017, he became the Director of Rutgers Cancer Institute of New Jersey. 4 5 In addition to being an accomplished clinical surgeon, Dr. Oral Presentations Libutti is a world-renowned scientist. The goal of Dr. Libutti's research program is to develop novel cancer therapies through a #1. Preclinical Analysis of the Notch Gamma Secretase Inhibitor BMS- better understanding of the complex interactions within the tumor 906024 in Combination with Chemotherapy in the Treatment of Lung Adenocarcinoma microenvironment. He is particularly interested in understanding of Authors: Morgan KM., Lee F., Michaud E., Fischer BS., Pine SR. tumor neovascular formation and the interaction between tumor Notch signaling is aberrantly activated in approximately one third of non-small cells, endothelial cells and the components of the tumor cell lung cancer (NSCLC) cases, primarily through loss of the endogenous microenvironment including fibroblasts and cancer stem cells. Dr. inhibitor, Numb, or via gain-of-function mutations in the Notch1 receptor, and is Libutti's approach to the study of these interactions has been associated with poor overall survival. We characterized the interaction between BMS-906024, a clinically relevant gamma secretase inhibitor (GSI) that inhibits through the utilization of a variety of in vitro and in vivo model Notch activation, and front-line chemotherapy in preclinical models of NSCLC. systems. Drug synergy MTS assays consisting of treatment with BMS-906024, cisplatin or paclitaxel, or the combination of GSI and chemotherapy were performed on a panel of human NSCLC cell lines, most of which were derived from Dr. Libutti has authored more than 270 peer reviewed adenocarcinomas. Analysis of the drug effects with CalcuSyn yielded journal articles and holds seven U.S. patents. He also serves as significantly greater synergy for the GSI BMS-906024 combined with paclitaxel Editor-in-Chief of Cancer Gene Therapy. He is the recipient of than with cisplatin (average CI = 0.54 vs 0.85, respectively; P = 0.001). Additionally, MTS assays performed on an extended panel of 31 NSCLC cell both the National Cancer Institute and National Institutes of Health lines demonstrated that the synergy between BMS-906024 and paclitaxel was Director’s Awards and has been recognized as a top doctor and top significantly greater in Kras/Braf-wildtype than –mutant cells (average CI = 0.43 vs 0.90, respectively; P=0.0026), while there was no correlation with EGFR cancer doctor by Castle Connelly as well as one of the best doctors or TP53 status. Treatment of cell line- and patient-derived lung adenocarcinoma in New York by New York Magazine. xenografts in mice confirmed enhanced antitumor activity for the combination of BMS-906024 and paclitaxel via decreased cell proliferation and increased apoptosis. These results are a step toward identification of the optimal combination of the GSI BMS-906024 with standard chemotherapies, as well as potential biomarkers that may predict patient response to Notch-targeted therapy. Funding: National Cancer Institute (KMM, SRP); Bristol-Myers Squibb (SRP) #2. Mass Spectrometric Analysis of TRPM7 Phosphorylation Reveals Regulatory Mechanisms of the Channel-Kinases Authors: Cai N., Bai Z., Nanda V., Runnels L.W. Transient Receptor Potential Melastatin 7 (TRPM7) was the first ion channel identified to contain a functional kinase domain. As a cation-permeating channel, TRPM7 is essential for controlling whole-body magnesium homeostasis and is involved in various cellular processes such as cell proliferation, adhesion, and migration. While much progress has been made in elucidating the function of the channel, little is known about the function and regulation of the kinase domain. To fill this gap in knowledge, we performed a comprehensive mass spectrometric analysis of TRPM7 phosphorylation and 6 7 uncovered multiple in vivo autophosphorylation sites on TRPM7. To test represent novel therapeutic opportunities to improve prognosis for these whether autophosphorylation affects the function of TRPM7’s kinase, we patients. conducted a series of amino acid substitution analyses and identified two potential regulatory autophosphorylation sites: S1565, located on the exchange #4. Cellular Zinc Homeostatic Mechanisms Function as an On/Off Switch domain outside of the kinase’s catalytic core, and S1777, located at the catalytic for Zinc Metallochaperone Mediated Reactivation of Mutant p53 center of the kinase domain. When phosphomimetic substitutions of either Authors: Samuel Kogan, Xin Yu, Darren Carpizo glutamate or aspartate were introduced at these two sites, the kinase activities of the proteins were severely compromised as assessed by in vitro kinase assays. TP53 is the most commonly mutated gene in cancer; however, no effective anti- This analysis in addition to structural modeling suggests a novel mechanism of cancer drug targeting mutant p53 exists. Restoring wild type structure and TRPM7 autophosphorylation in controlling TRPM7 kinase activity. This study function to mutant p53 has been one of the holy grails of cancer drug research. will serve as the first step towards understanding the regulatory mechanisms of We recently discovered a class of small molecules (zinc metallochaperones, the channel-kinase and further allow us to investigate how this unique ion ZMC), which restores wild type structure and function specifically to zinc- channel takes part in various important cellular processes. deficient p53 mutants by delivering zinc
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