Dr. Terry Rogers Professor 108 N. Greene Street Baltimore, MD 21201 Phone: 410-706-3169 Fax: 410-706-8297 email: trogers@som.umaryland.edu EDUCATION 1970          BA, Chemistry, Cornell University, Ithaca, NY 1974          MS, Food Science, University of California, Davis, CA 1977          Ph.D., Biochemistry, University of California, Davis, CA POST GRADUATE EDUCATION 1977-1978   NSF Postdoctoral Fellow (mentor Dr. Michel Lazdunski)                   Centre de Biochimie, Universite de Nice, Nice, France 1979-1980   NIH Postdoctoral Fellow (mentor Dr. Solomon H. Snyder)                   Departments of Pharmacology & Neuroscience, Johns Hopkins                   University School of Medicine, Baltimore, Maryland PROFESSIONAL EXPERIENCE Faculty Appointments 1980-1986         Assistant Professor, University of Maryland School                         of Medicine 1986-1992         Associate Professor, University of Maryland School                         of Medicine 1992-present     Professor, University of Maryland School of Medicine 1997-present     Director, M.D. Ph.D. Program, University of Maryland                         School of Medicine

ASSOCIATED SITES      Program Project: Local Signals and Macromolecular Architecture in Heart M.D., Ph.D Degree Program

Research Description

We study the fundamental properties of heart cells and the impact of intracellular signaling mechanisms on the regulation of cardiac myocyte function.  Calcium is a central signaling ion in heart muscle and over the years many investigations have helped to define the molecular elements underlying calcium signaling in cardiac cells.   During excitation-contraction (EC) coupling in cardiac myocytes the influx of Ca²⁺ ions carried by the Ca²⁺ current (I_Ca) activates a large release of Ca²⁺ from intracellular stores in the sarcoplasmic reticulum (SR) via the SR Ca²⁺ release channel. The subsequent declining phase of this [Ca²⁺]_i transient is due, in part, to Ca²⁺ reuptake mediated by the SR Ca²⁺ pump.  Thus this movement of Ca²⁺ ions is a central feature of heart cell function.  Over the years our laboratory has focused on intracellular signaling pathways that contribute to the precise physiological control of Ca²⁺ signaling in heart.

Angiotensin II signaling in Heart Cells -- In one series of projects we have defined how the hormone, angiotensin II, increases contractility by regulating Ca²⁺ currents, various protein kinases and phospholipases in intact cardiac cells.  These studies have defined intracellular signaling cascades in cardiac myocytes that are activated by several distinct hormone receptors located on the cell surface.  These studies not only reveal how this hormone regulates heart cell contractility but also provide insight into mechanisms that may underlie pathological processes such as heart failure or cardiomyopathy.

Role of Protein Phosphatases in Cardiac Cell Function  -- Through experiments in which we directly injected proteins into intact heat cells, we have recently discovered a crucial role of phosphatase enzymes in controlling EC coupling. Thus it is clear that protein dephosphorylation reactions are important regulatory mechanisms in heart.  These results have led to studies in which we are examining the localization and expression of several protein phosphatase enzymes in cardiac cells.  These studies may have important implications in the pathology associated with failing heart.

Potassium Channel Regulation in heart cells -- Outward rectifying potassium channels play a crucial role in repolarizing the heart cell leading to relaxation during each beat.  Recently we have found a novel regulatory mechanism that inhibits several K channels and leads to enhanced contractility as a result.  This mechanism is mediated by a cellular protein known as FKBP12.  Ongoing research is focused on studying the mechanism of K channel regulation in heart. 

Laboratory Techniques

As reflected in the references listed below, our laboratory is interdisciplinary in nature.  Thus training in our laboratory capitalizes on a novel integrated strategy that uses an array of techniques to address important problems in cardiac biology.  These methods include biochemical techniques such as: enzyme assays, Western blot protein analysis, immunoprecipitations and protein fractionation.  We use molecular biology methods the study protein expression including, PCR analysis, Northern blot assays and gene transfection methods to express heterologous proteins in cultured heart cells.  We also use single cell methods that provide functional information to complement these molecular approaches including: edge detection video microscopy to measure contractility, single cell voltage clamp electrophysiology, intracellular Ca measurements with fluorescent indicators, and high-resolution confocal Ca²⁺ imaging

ASSOCIATED SITES     Program Project: Local Signals and Macromolecular Architecture in Heart

                                    M.D., Ph.D. Program     

Selected Publications:

Gigena, M.S, Ito, A., Nojima, H., Rogers, T.B. (2005) A B56 regulatory subunit of protein phosphatase 2A localizes to nuclear speckles in cardiomyocytes, Am.J. Physiol. 289, H285-H294.

duBell, W.H., and Rogers, T.B. (2004)  Protein Phosphatase 1 and an Opposing Protein Kinase Regulate Steady- State L-Type Ca Current in Mouse Cardiac Myocytes .  J. Physiol. 556 ,79-93.

Mohler, P.J. ,  Schott,J.-J., Gramolini,A.O., Dilly, K.W., Guatimosim, S., duBell, W.H., Song, L.-S., Haurogné, K.,  Kyndt, F., Ali, M.E., Rogers,T.B., Lederer, W.J., Escande, D., Le Marec, H., Bennett,V. (2003) Ankryin-B Mutation Causes Type 4 Long QT Cardiac  Arrhythmia and Sudden Cardiac  Death, Nature, 421, 634-639.

Wright, G., Singh,I.S., Hasday, J.D., Farrance, I.K., Hall,G., Cross, A.S. and  Rogers, T.B. (2002) Endotoxin Stress-Response in Cardiomyocytes: NF-kB Activation and Tumor Necrosis Factor-a Expression, Am.J.Physiol. 282, H872-H879.

Zhang,T., Johnson, E.N., Gu, Y., Morissette, M.R., Sah, V.P., Gigena, M.S., Belke,D.D.,  Dillmann, W.H., Rogers, T.B., Schulman, H., Ross,J. Jr, and Brown, J.H.  (2002) The Cardiac-Specific Nuclear B Isoform of Ca²+/Calmodulin-dependent protein kinase II induces hypertrophy and dilated cardiomyopathy associated with increased PP2A activity, J.Biol. Chem., 277, 1261-1267.