DOCSLIB.ORG

Tsin-CV; Updated 6/94

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Tsin-CV; Updated 6/94 Updated June, 2019 Andrew Tsin CURRICULUM VITAE Andrew Tsin, Ph.D. Professor and Chair Deaprtment of Molecular Science And Senior Associate Dean of Research School of Medicine The University of Texas Rio Grande Valley (UT Health – Rio Grande Valley) CONTACT INFO: Department of Molecular Science, School of Medicine The University of Texas Rio Grande Valley 1210 W. Schunior St., Edinburg, TX 78541 Phone: (956) 665-6599 Email: [email protected] CITIZENSHIP: USA and CANADA EDUCATION/TRAINING: 1973 BS in Biology, Dalhousie University, Halifax, Nova Scotia, Canada 1976 MS in Zoology (Physiology), The University of Alberta, Edmonton, Alberta, Canada 1979 Ph.D. in Zoology (Physiology), The University of Alberta, Edmonton, Alberta, Canada 1979-81 Postdoctoral Fellow, Cullen Eye Institute, Department of Ophthalmology, Program in Neuroscience, Baylor College of Medicine, Texas Medical Center, Houston, Texas CONTINUED EDUCTION: 2014 Healing Health Care Disparities through Education: An Interdisciplinary Faculty Development Program, Harvard Medical School, Boston, Massachusetts. 2016 Effective Validation of Commercialization Strategy through tactical collection and analysis of data from direct interaction with customer- a short course by The Southwest Node of the National Science Foundation Innovation Corps (I-Corps) Program, The IC2 Institute of the University of Texas at Austin. 2017 Organizational Leadership in Academic Medicine: An Executive Development Seminar for Associate Deans and Department Chairs, AAMC (Association of American Medical Colleges) 1 AWARDS & RECOGNITIONS: 1977-78 National Research Council (Canada) Postgraduate Scholarship 1979-81 Medical Research Council (Canada) Fellowship 1981-82 Alberta Heritage Foundation Medical Research Fellowship 1992 FASEB-MARC Faculty Scholarship 1994 President's Award for Distinguished Achievement in Research 1994,96, 98 Who’s Who Best Teacher Award 1996 UTSA Faculty Development Award 1998 Million Dollar Scholar Award 2009 Distinguished Achievement-University Service (College of Sciences) 2010 Faculty Role Model Award (Minority Access Role Models) 2011 PAESMEM (Presidential Award for Excellence in Science, Mathematics, and Engineering Mentoring) – White House Office of Science and Technology and the National Science Foundation (awarded in person by President Barack Obama) 2014 AAAS (American Association for the Advancement of Science): Mentor Award for Lifetime Achievement 2017 Burroughs Wellcome Fund: BEST Workshop in the AAMC GREAT Professional Development Meeting in Orlando, FL 2018 Ruth Kirschstein Diversity in Science Award, ASBMB (American Association of Biochemistry and Molecular Biology) 2018 Albert Nelson Marquis Lifetime Achievement, Marquis Who’s Who SOCIETY FELLOWS, OFFICE and MEMBERS: 2019 Elected Fellow of the American Physiological Society 2015 Elected Gold Fellow of Assoc. for Research in Vision & Ophthalmology 2013 Elected Fellow of the Linnaean Society of London 2012 Elected Fellow of the Royal Society of Biology (London-UK) 2011 Elected Fellow of the American Assoc. for the Advancement of Science 2011 Elected Fellow of the Royal Society of Medicine (London-UK) 2009 Elected Silver Fellow of Assoc. for Research in Vision and Ophthalmology 2012 Elected President: Alamo Chapter of SigmaXi, The Scientific Research Society (one year term) 2011 Elected Chair: Diversity Issues Committee, ARVO (three-year term) 2007 Elected Board of Director: SACNAS (three-year term) 2014 Member: American Society of Cell Biology 2000 Member: American Evaluation Association 2010 Member: International Society of Eye Research 2010 Member: American Chemical Society 2010 Member: Alamo Chapter of SigmaXi 2010 Member: American Physiological Society 2000 Member: American Association for the Advancement of Science 1999 Member: American Society for Biochemistry and Molecular Biology 1989 Member: Society for Advancement of Chicanos & Native Americans in Science 1985 Member: The Society of Integrative and Comparative Biology 2 Updated June, 2019 Andrew Tsin 1981 Member: Association for Research in Vision and Ophthalmology CURRENT ACADEMIC APPOINTMENTS: 2018 - Professor, Department of Molecular Science, School of Medicine, The University of Texas Rio Grande Valley, Edinburg, Texas 2016- Adjunct Professor, Department of Biology, The University of Texas at San Antonio, San Antonio, Texas 2010 - Adjoint Professor, Department of Biochemistry, The University of Texas Health Science Center at San Antonio 1990 - Adjunct Professor, Department of Ophthalmology, The University of Texas Health Science Center at San Antonio CURRENT ADMINISTRATIVE APPOINTMENTS: 2019 - Senior Associate Dean of Research, School of Medicine, The University of Texas Rio Grande Valley, Edinburg, Texas 2018 - Chair, Department of Molecular Science, School of Medicine, The University of Texas Rio Grande Valley, Edinburg, Texas 2018- Interim Chair, Department of Neuroscience, School of Medicine, The Univeristy of Texas Rio Grande Valley, Edinburg, Texas 2018- Interim Director, Institute of Neuroscience, School of Medicine, The Univeristy of Texas Rio Grande Valley, Edinburg, Texas 2018- Director, Center for Brain Health, The University of Texas Rio Grande Valley, Edinburg, Texas PREVIOUS ACADEMIC AND ADMINISTRATIVE APPOINTMENTS: 2016 - 2019 Associate Dean of Research, School of Medicine, The University of Texas Rio Grande Valley, Edinburg, Texas 2016 – 2018 Professor and Inaugural Chair, Department of Biomedical Sciences, School of Medicine, The University of Texas Rio Grande Valley, Edinburg, Texas 2008 - 2016 Principal Investigator and Program Director, NIH-RCMI (Research Centers in Minority Institutions - Center for Interdisciplinary Health Research) at The University of Texas at San Antonio 2007 - 2016 Program Director, NIH-SCORE (Support for Competitive Research) at The University of Texas at San Antonio 1990 - 2016 Professor, Department of Biology, The University of Texas at 3 San Antonio 2007-2014 Founding Director, Center for Research and Training in the Sciences, College of Sciences, The University of Texas at San Antonio 2010 - 2011 Associate Vice President for Health Research, The University of Texas at San Antonio 1991 - 2007 Director, MBRS (Minority Biomedical Research Support Program), The University of Texas at San Antonio 2008 - 2010 Associate Dean of Research, College of Sciences, The University of Texas at San Antonio, 2007 - 2009 Board of Directors, SACNAS (Society for the Advancement of Chicanos and Native Americans in Science) 1993 - 2001 Director, Pfizer/UTSA Scholarship Program The University of Texas at San Antonio 1992 - 1993 Director, Minority High School Student Research Apprentice Program The University of Texas at San Antonio 1992 - 1995 Chair, Dividion of Life Sciences (Department of Biology), The University of Texas at San Antonio 1986 - 1990 Associate Professor, Division of Life Sciences, The University of Texas at San Antonio 1986-1990 Associate Professor, Department of Ophthalmology, The University of Texas Health Science Center-San Antonio 1985-1992 Administrative Officer, Radiation and Laser Safety Program, The University of Texas at San Antonio 1984-1986 Assistant Professor, Department of Ophthalmology, The University of Texas Health Science Center-San Antonio 1981-1986 Assistant Professor, Division of Life Sciences, The University of Texas at San Antonio TEACHING TOPICS: PBL (Problem Based Learning) facilitator of the MBB (Mind, Brain and Behavior) Module (medical students) at the Department of Medical Education in the School of Medicine, University of Texas Rio Grande Valley; Grand round faculty (ophthalmology residents) on “Visual Biochemistry and Retinal Physiology” at the Department of Ophthalmology in the School of Medicine at the University of Texas Health Science Center at San Antonio; Course instructor at the Department of Biology at University of Texas at San Antonio: Graduate Level - Protein Structure and Function; Graduate Biochemistry, Sensory Physiology, Graduate Animal Physiology, Neurophysiology, Enzymes, Seminar in Life Sciences, Colloquium in Vision 4 Updated June, 2019 Andrew Tsin Research, MS research, MS thesis, Doctoral Research, Doctoral Dissertation. Undergraduate Level - General Physiology, Human Biology, Anatomy and Physiology, Biochemistry, Comparative Animal Physiology, Contemporary Biology (for freshmen, non-Biology Major); Course instructor at the Department of Zoology at the University of Alberta: Plant and Animal Functions, Comparative Anatomy of the Vertebrates, Evolutionary Biology, Comparative Animal Physiology. RESEARCH INTERESTS: Cell Biology of the Retina/Brain Diseases: Neurobilogy of Photoreceptors, Muller Cells, Retinal Pericytes, Retinal Pigment Epithelial and Retinal Endothelial Cells (signaling pathways, receptors, angiogenic cytokines related to diabetic retinopathy and macular degeneration); Biochemistry of Rod and Cone Visual Cycles: Membrane Proteins (Rhodopsin); Metabolism of Retinoid (Vitamin A Compounds); Comparative Animal (Vertebrate and System) Physiology; Environmental and Evolutionary Biology. EDITORIAL BOARD: Annual Review and Research in Biology (Associate Editor); Current Vascular Pharmacology; World Journal of Ophthalmology; Investigative Ophthalmology and Visual Science (Guest Editor); Open Journal of Ophthalmology, International Journal of Ophthalmology and Eye Science; Journal of Ophthalmology (Guest Editor). Journal of Advances in Biology & Biotechnology; Journal of Cell Biology and Cell Metabolism (CBCM), International Journal of Diabetology
Load more

Recommended publications
  • Dominant Retinas: a Novel Pathway for Visual- Pigment Regeneration in Daylight
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Neuron, Vol. 36, 69–80, September 26, 2002, Copyright 2002 by Cell Press Isomerization and Oxidation of Vitamin A in Cone- Dominant Retinas: A Novel Pathway for Visual- Pigment Regeneration in Daylight Nathan L. Mata,1 Roxana A. Radu,1 cis-retinaldehyde through a multistep pathway called Richard S. Clemmons,3 and Gabriel H. Travis1,2,4 the visual cycle (Figure 1B). Most of what is known about 1Jules Stein Eye Institute the visual cycle has come from the study of rod-domi- 2 Department of Biological Chemistry nant species such as cattle and rodents. UCLA School of Medicine Several lines of evidence suggest that rod and cone Los Angeles, California 90095 photopigments regenerate by different mechanisms. In 3 Center for Basic Neuroscience frog retinas separated from the retinal pigment epithe- UT Southwestern Medical Center lium (RPE), cone opsin, but not rhodopsin, regenerates Dallas, Texas 75235 spontaneously (Goldstein and Wolf, 1973; Hood and Hock, 1973). After bleaching, isolated salamander cones, but not rods, recover sensitivity with addition of Summary 11-cis-retinol (Jones et al., 1989). Cultured Mu¨ ller cells isomerize all-trans-retinol to 11-cis-retinol, which they The first step toward light perception is 11-cis to all- secrete into the medium (Das et al., 1992). Mu¨ ller cells, trans photoisomerization of the retinaldehyde chro- in addition to RPE cells, contain cellular retinaldehyde mophore in a rod or cone opsin-pigment molecule. binding protein (CRALBP), which specifically binds 11- Light sensitivity of the opsin pigment is restored cis-retinoids (Bunt-Milam and Saari, 1983; Saari and through a multistep pathway called the visual cycle, Bredberg, 1987).
    [Show full text]
  • Retinoid Isomerase Inhibitors Impair but Do Not Block Mammalian Cone Photoreceptor Function
    Published Online: 2 March, 2018 | Supp Info: http://doi.org/10.1085/jgp.201711815 Downloaded from jgp.rupress.org on April 2, 2018 RESEARCH ARTICLE Retinoid isomerase inhibitors impair but do not block mammalian cone photoreceptor function Philip D. Kiser1,2, Jianye Zhang2, Aditya Sharma3, Juan M. Angueyra4, Alexander V. Kolesnikov3, Mohsen Badiee5, Gregory P. Tochtrop5, Junzo Kinoshita6, Neal S. Peachey1,6,7, Wei Li4, Vladimir J. Kefalov3, and Krzysztof Palczewski2 Visual function in vertebrates critically depends on the continuous regeneration of visual pigments in rod and cone photoreceptors. RPE65 is a well-established retinoid isomerase in the pigment epithelium that regenerates rhodopsin during the rod visual cycle; however, its contribution to the regeneration of cone pigments remains obscure. In this study, we use potent and selective RPE65 inhibitors in rod- and cone-dominant animal models to discern the role of this enzyme in cone-mediated vision. We confirm that retinylamine and emixustat-family compounds selectively inhibit RPE65 over DES1, the putative retinoid isomerase of the intraretinal visual cycle. In vivo and ex vivo electroretinography experiments in Gnat1−/− mice demonstrate that acute administration of RPE65 inhibitors after a bleach suppresses the late, slow phase of cone dark adaptation without affecting the initial rapid portion, which reflects intraretinal visual cycle function. Acute administration of these compounds does not affect the light sensitivity of cone photoreceptors in mice during extended exposure to background light, but does slow all phases of subsequent dark recovery. We also show that cone function is only partially suppressed in cone-dominant ground squirrels and wild-type mice by multiday administration of an RPE65 inhibitor despite profound blockade of RPE65 activity.
    [Show full text]
  • Key Enzymes of the Retinoid (Visual) Cycle in Vertebrate Retina☆
    Biochimica et Biophysica Acta 1821 (2012) 137–151 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal homepage: www.elsevier.com/locate/bbalip Review Key enzymes of the retinoid (visual) cycle in vertebrate retina☆ Philip D. Kiser a,1, Marcin Golczak a,1, Akiko Maeda a,b,⁎, Krzysztof Palczewski a,⁎⁎ a Department of Pharmacology, Case Western Reserve University, Cleveland, OH, 44106-4965, USA b Department of Ophthalmology and Vision Sciences, Case Western Reserve University, Cleveland, OH, 44106-4965, USA article info abstract Article history: A major goal in vision research over the past few decades has been to understand the molecular details of Received 19 January 2011 retinoid processing within the retinoid (visual) cycle. This includes the consequences of side reactions that Received in revised form 8 March 2011 result from delayed all-trans-retinal clearance and condensation with phospholipids that characterize a Accepted 22 March 2011 variety of serious retinal diseases. Knowledge of the basic retinoid biochemistry involved in these diseases is Available online 5 April 2011 essential for development of effective therapeutics. Photoisomerization of the 11-cis-retinal chromophore of rhodopsin triggers a complex set of metabolic transformations collectively termed phototransduction that Keywords: RPE65 ultimately lead to light perception. Continuity of vision depends on continuous conversion of all-trans-retinal Retinol dehydrogenase back to the 11-cis-retinal isomer. This process takes place in a series of reactions known as the retinoid cycle, Visual cycle which occur in photoreceptor and RPE cells. All-trans-retinal, the initial substrate of this cycle, is a chemically Retinoid cycle reactive aldehyde that can form toxic conjugates with proteins and lipids.
    [Show full text]
  • ANNUAL REPORT 2014–2015 Stein Eye Institute ANNUAL REPORT
    ANNUAL REPORT 2014–2015 Stein Eye Institute ANNUAL REPORT July 1, 2014–June 30, 2015 Director Bartly J. Mondino, MD Faculty Advisor Debora B. Farber, PhD, DPhhc Managing Editor Tina-Marie Gauthier c/o Stein Eye Institute 100 Stein Plaza, UCLA Los Angeles, California 90095–7000 Email: [email protected] Editors Teresa Closson Susan Ito Rosalie Licht Peter J. López Ellen Pascual Debbie Sato M. Gail Summer Guest Writer Dan Gordon Photography Reed Hutchinson J. Charles Martin Robin Weisz Design Robin Weisz/Graphic Design Printing Colornet Press Send questions, comments, and updates to: [email protected]. To view the Annual Report online, visit: jsei.org/annual_report.htm. For more information about the Institute, see: www.jsei.org. ©2015 by the Regents of the University of California. All rights reserved. On the cover: Signature eyewear worn by philanthropists Edie and Lew Wasserman dominate the lobby of the Edie & Lew Wasserman Building, paying homage to the couple’s infinite vision and long- standing commitment to preventing blindness and restoring eyesight. A Year in Review 1 Stein Eye Institute 2 Transitions 6 Alumni News 6 Honors and Awards 8 Research 11 Education 13 Community Outreach 15 Philanthropy 17 Thank You 19 Jules and Doris Stein 24 Board of Trustees and Executive Committee 26 Faculty 29 Programs 87 Patient Care Services 88 Research and Treatment Centers 90 Clinical Laboratories 95 Training Programs 97 Appendices 101 Volunteer and Consulting Faculty 102 Residents and Fellows 104 Educational Offerings 105 Research Contracts and Grants 107 Clinical Research Studies 116 Publications of the Full-Time Faculty 123 Giving Opportunities 130 Dear Friends, The 2014–2015 academic term stands as a banner year for the Stein Eye Institute.
    [Show full text]
  • Processing and Transport of Retinoids by the Retinal Pigment Epithelium
    Eye (1990) 4, 326-332 Processing and Transport of Retinoids by the Retinal Pigment Epithelium DE AN BOK Los Angeles Summary Recent developments regarding our understanding of retinoid processing and trans­ port during the visual cycle and related events are reviewed. Retinoids are bound and protected by a cohort of retinoid binding proteins, each of whiCh is unique. The production of retinol (Vitamin A) derivatives is accomplished by a group of mem­ brane-bound enzymes, some of which appear to be coupled in their actions. Historical Perspectives on a series of biochemical reactions involving The photopigments of all organisms studied the coordinated activity of the retinal pigment to date consist of a chromophore derived from epithelium (RPE) and the photoreceptors.3 Vitamin A (Retinol)! covalently bound to a These events begin with the photobleaching protein by a protonated aldimine bond of rhodopsin to form opsin and all-trans·ret· (Schiff's base).2 The chromophore or pros­ inal, the production of various retinol deriva­ thetic group is, in all cases, retinaldehyde (ret­ tives, the regeneration of ll-cis-retinal and inal) the oxidised form of retinol. Retinol and ultimately, the regeneration of the photopig­ its derivatives are collectively referred to as ment itself. This complex series of interac­ retinoids and the proteins that covalently bind tions is known as the visual cycle. In retinal are called opsins. Both the retinoids Dowling's original observations, light was and the opsins are hydrophobic molecules, found to cause a cis to trans isomerisation of retinol being a fat-soluble vitamin, and the opsin-bound retinal following which retinal opsins belonging to a class of membrane com­ dissociated from the protein and was reduced ponents collectively known as intrinsic pro­ to form all-trans-retinol.
    [Show full text]
  • O O2 Enzymes Available from Sigma Enzymes Available from Sigma
    COO 2.7.1.15 Ribokinase OXIDOREDUCTASES CONH2 COO 2.7.1.16 Ribulokinase 1.1.1.1 Alcohol dehydrogenase BLOOD GROUP + O O + O O 1.1.1.3 Homoserine dehydrogenase HYALURONIC ACID DERMATAN ALGINATES O-ANTIGENS STARCH GLYCOGEN CH COO N COO 2.7.1.17 Xylulokinase P GLYCOPROTEINS SUBSTANCES 2 OH N + COO 1.1.1.8 Glycerol-3-phosphate dehydrogenase Ribose -O - P - O - P - O- Adenosine(P) Ribose - O - P - O - P - O -Adenosine NICOTINATE 2.7.1.19 Phosphoribulokinase GANGLIOSIDES PEPTIDO- CH OH CH OH N 1 + COO 1.1.1.9 D-Xylulose reductase 2 2 NH .2.1 2.7.1.24 Dephospho-CoA kinase O CHITIN CHONDROITIN PECTIN INULIN CELLULOSE O O NH O O O O Ribose- P 2.4 N N RP 1.1.1.10 l-Xylulose reductase MUCINS GLYCAN 6.3.5.1 2.7.7.18 2.7.1.25 Adenylylsulfate kinase CH2OH HO Indoleacetate Indoxyl + 1.1.1.14 l-Iditol dehydrogenase L O O O Desamino-NAD Nicotinate- Quinolinate- A 2.7.1.28 Triokinase O O 1.1.1.132 HO (Auxin) NAD(P) 6.3.1.5 2.4.2.19 1.1.1.19 Glucuronate reductase CHOH - 2.4.1.68 CH3 OH OH OH nucleotide 2.7.1.30 Glycerol kinase Y - COO nucleotide 2.7.1.31 Glycerate kinase 1.1.1.21 Aldehyde reductase AcNH CHOH COO 6.3.2.7-10 2.4.1.69 O 1.2.3.7 2.4.2.19 R OPPT OH OH + 1.1.1.22 UDPglucose dehydrogenase 2.4.99.7 HO O OPPU HO 2.7.1.32 Choline kinase S CH2OH 6.3.2.13 OH OPPU CH HO CH2CH(NH3)COO HO CH CH NH HO CH2CH2NHCOCH3 CH O CH CH NHCOCH COO 1.1.1.23 Histidinol dehydrogenase OPC 2.4.1.17 3 2.4.1.29 CH CHO 2 2 2 3 2 2 3 O 2.7.1.33 Pantothenate kinase CH3CH NHAC OH OH OH LACTOSE 2 COO 1.1.1.25 Shikimate dehydrogenase A HO HO OPPG CH OH 2.7.1.34 Pantetheine kinase UDP- TDP-Rhamnose 2 NH NH NH NH N M 2.7.1.36 Mevalonate kinase 1.1.1.27 Lactate dehydrogenase HO COO- GDP- 2.4.1.21 O NH NH 4.1.1.28 2.3.1.5 2.1.1.4 1.1.1.29 Glycerate dehydrogenase C UDP-N-Ac-Muramate Iduronate OH 2.4.1.1 2.4.1.11 HO 5-Hydroxy- 5-Hydroxytryptamine N-Acetyl-serotonin N-Acetyl-5-O-methyl-serotonin Quinolinate 2.7.1.39 Homoserine kinase Mannuronate CH3 etc.
    [Show full text]
  • 12) United States Patent (10
    US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S.
    [Show full text]
  • UNIVERSITY of CALIFORNIA Los Angeles New Mechanisms for Regeneration of Visual Pigments in the Vertebrate Retina a Dissertation
    UNIVERSITY OF CALIFORNIA Los Angeles New Mechanisms for Regeneration of Visual Pigments in the Vertebrate Retina A dissertation submitted in partial satisfaction of the requirements for the degree Doctor of Philosophy in Molecular, Cellular, and Integrative Physiology by Tongzhou Xu 2017 © Copyright by Tongzhou Xu 2017 ABSTRACT OF THE DISSERTATION New Mechanisms for Regeneration of Visual Pigments in the Vertebrate Retina by Tongzhou Xu Doctor of Philosophy in Molecular, Cellular, and Integrative Physiology University of California, Los Angeles, 2017 Professor Gabriel H. Travis, Chair Vision begins when a photon is captured by a visual pigment in a photoreceptor cell. For most vertebrates, the light-sensitive chromophore in the visual pigment is 11-cis- retinaldehyde (11-cis-retinal), which is covalently bound to the protein moiety, opsin, through a Schiff base linkage. The absorption of a photon isomerizes 11-cis-retinal to its all-trans-isomer and activates the visual pigment. In vertebrate ciliary photoreceptors, after a brief activation, the pigment decays to yield apo-opsin and free all-trans-retinal. Light sensitivity restoration in photoreceptor cells occurs following re-isomerization of all-trans-retinal to 11-cis-retinal by enzymatic pathways termed “visual cycles”. At present, two visual cycles have been established: (1) A well understood canonical visual cycle between RPE cells and photoreceptors, with RPE65 as its retinoid isomerase (Isomerase I); (2) A relatively under characterized alternate visual cycle between Müller cells and cones, with an unknown retinoid isomerase (Isomerase II). Recently, we have identified dihydroceramide desaturase-1 (DES1) as a novel retinoid isomerase and a strong candidate for Isomerase II.
    [Show full text]
  • Transforming Eye Care
    Stein Eye Institute Annual Report 2013–2014 Annual Report 2013–2014 TRANSFORMING EYE CARE LOS ANGELES AND BEYOND The Stein Eye Institute is a proud affiliate of the Doheny Eye Institute. David Geffen School of Medicine at UCLA University of California, Los Angeles Stein Eye Institute Annual Report July 1, 2013–June 30, 2014 Director Bartly J. Mondino, MD Faculty Advisor Debora B. Farber, PhD, DPhhc Managing Editor Tina-Marie Gauthier c/o Stein Eye Institute 100 Stein Plaza, UCLA Los Angeles, California 90095–7000 Email: [email protected] Editors Teresa Closson Ellen Haupt Rosalie Licht Peter J. López Debbie Sato M. Gail Summers Guest Writer Dan Gordon Photography Reed Hutchinson J. Charles Martin ASUCLA Photography Design Robin Weisz/Graphic Design Printing Colornet Press Send questions, comments, and updates to: [email protected]. To view the Annual Report online, visit: jsei.org/annual_report.htm. For more information about the Institute, see: www.jsei.org. ©2014 by the Regents of the University of California. All rights reserved. A Year in Review 1 Stein Eye Institute 2 Transitions 4 Honors and Awards 5 Research 8 Education 10 Community Outreach 13 Philanthropy 15 Thank You 18 Jules and Doris Stein 25 Board of Trustees and Executive Committee 26 Faculty 29 Programs 81 Patient Care Services 82 Research and Treatment Centers 84 Clinical Laboratories 89 Training Programs 91 Appendices 95 Volunteer and Consulting Faculty 96 Residents and Fellows 98 Educational Offerings 99 Research Contracts and Grants 101 Clinical Research Studies 106 Publications of the Full-Time Faculty 112 Giving Opportunities 118 Dear Friends, In November 1966 the doors of the Jules Stein Eye Institute opened on the grounds of UCLA, and with dedication of purpose, the Institute has continued to grow in its commitment to further vision-science re- search, ophthalmic education, and patient care.
    [Show full text]
  • Identification of the 11-Cis-Specific Retinyl-Ester Synthase in Retinal Müller Cells As Multifunctional O-Acyltransferase (MFAT)
    Identification of the 11-cis-specific retinyl-ester synthase in retinal Müller cells as multifunctional O-acyltransferase (MFAT) Joanna J. Kaylora, Jeremy D. Cooka, Jacob Makshanoffa, Nicholas Bischoffa, Jennifer Yonga, and Gabriel H. Travisa,b,1 aJules Stein Eye Institute and bDepartment of Biological Chemistry, University of California, Los Angeles School of Medicine, Los Angeles, CA 90095 Edited by Robert S. Molday, University of British Columbia, Vancouver, Canada, and accepted by the Editorial Board April 11, 2014 (received for review October 11, 2013) Absorption of a photon by a rhodopsin or cone-opsin pigment pathway is dihydroceramide desaturase (DES1) (11). DES1 cata- isomerizes its 11-cis-retinaldehyde (11-cis-RAL) chromophore to lyzes rapid equilibrium isomerization of retinol (11). At equilibrium, all-trans-retinaldehyde (all-trans-RAL), which dissociates after a 11-cis-ROL is much less abundant than all-trans-ROL, due to the brief period of activation. Light sensitivity is restored to the 4.1 kcal/mole difference in free energy between these isomers (14). resulting apo-opsin when it recombines with another 11-cis-RAL. Accordingly, a secondary source of energy is required to drive Conversion of all-trans-RAL to 11-cis-RAL is carried out by an en- the conversion of all-trans-ROL to 11-cis-ROL by DES1. zyme pathway called the visual cycle in cells of the retinal pigment Retinas from cone-dominant species contain 11-cis-retinyl esters epithelium. A second visual cycle is present in Müller cells of the (11-cis-REs), whereas retinyl esters are much less abundant in retina.
    [Show full text]
  • Substrate Specificity and Reaction Mechanism of Vertebrate Carotenoid Cleavage
    Substrate specificity and reaction mechanism of vertebrate carotenoid cleavage oxygenases DISSERTATION Presented in Partial Fulfillment of the Requirements for the Degree Doctor of Philosophy in the Graduate School of The Ohio State University By Carlo C. dela Seña The Ohio State Biochemistry Program The Ohio State University 2014 Dissertation Committee: Earl H. Harrison, Ph.D., Adviser Robert W. Curley, Jr., Ph.D. Ross E. Dalbey, Ph.D. Steven J. Schwartz, Ph.D Copyright by Carlo C. dela Seña 2014 i Abstract Carotenoids are yellow, orange and red pigments found in fruits and vegetables. Some carotenoids can act as dietary precursors of vitamin A. Humans and other animals generate retinal (vitamin A aldehyde) from provitamin A carotenoids by oxidative cleavage of the central 15-15′ double bond by the enzyme β-carotene 15-15′-oxygenase (BCO1). Another carotenoid oxygenase, β-carotene 9′-10′-oxygenase (BCO2), catalyzes the oxidative cleavage of the 9′-10′ double bond of various carotenoids to yield apo-10′- carotenals and ionones. In this dissertation, we elucidate the substrate specificity of these two enzymes. Recombinant His-tagged human BCO1 was expressed in Escherichia coli strain BL21- Gold (DE3) and purified by cobalt ion affinity chromatography. The enzyme was incubated with various dietary carotenoids and β-apocarotenals, and the reaction products were analyzed by reverse-phase high-performance liquid chromatography (HPLC). We found that BCO1 catalyzes the oxidative cleavage of only provitamin A dietary carotenoids and β-apocarotenals specifically at the 15-15′ double bond to yield retinal. A notable exception is lycopene, which is cleaved by BCO1 to yield two molecules of acycloretinal.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur Et Al
    US 20150240226A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur et al. (43) Pub. Date: Aug. 27, 2015 (54) NUCLEICACIDS AND PROTEINS AND CI2N 9/16 (2006.01) METHODS FOR MAKING AND USING THEMI CI2N 9/02 (2006.01) CI2N 9/78 (2006.01) (71) Applicant: BP Corporation North America Inc., CI2N 9/12 (2006.01) Naperville, IL (US) CI2N 9/24 (2006.01) CI2O 1/02 (2006.01) (72) Inventors: Eric J. Mathur, San Diego, CA (US); CI2N 9/42 (2006.01) Cathy Chang, San Marcos, CA (US) (52) U.S. Cl. CPC. CI2N 9/88 (2013.01); C12O 1/02 (2013.01); (21) Appl. No.: 14/630,006 CI2O I/04 (2013.01): CI2N 9/80 (2013.01); CI2N 9/241.1 (2013.01); C12N 9/0065 (22) Filed: Feb. 24, 2015 (2013.01); C12N 9/2437 (2013.01); C12N 9/14 Related U.S. Application Data (2013.01); C12N 9/16 (2013.01); C12N 9/0061 (2013.01); C12N 9/78 (2013.01); C12N 9/0071 (62) Division of application No. 13/400,365, filed on Feb. (2013.01); C12N 9/1241 (2013.01): CI2N 20, 2012, now Pat. No. 8,962,800, which is a division 9/2482 (2013.01); C07K 2/00 (2013.01); C12Y of application No. 1 1/817,403, filed on May 7, 2008, 305/01004 (2013.01); C12Y 1 1 1/01016 now Pat. No. 8,119,385, filed as application No. PCT/ (2013.01); C12Y302/01004 (2013.01); C12Y US2006/007642 on Mar. 3, 2006.
    [Show full text]