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Brandon Biesiadecki, Ph.D.
Assistant Professor
The Ohio State University
Physiology and Cell Biology
404 Hamilton Hall
1645 Neil Ave.
Columbus, OH 43210
Office Phone: (614) 247-4091
Email: biesiadecki.1@osu.edu
Web: http://biomed.osu.edu/physiology/13796.cfm
Education & Training:
Alma College, Alma, MI 1996, B.S. Biology
Medical College of Ohio, Toledo, OH, 1998, M.S. Biomedical Science
Case Western Reserve University, Cleveland, OH, 2003, Ph.D. Physiology
Case Western Reserve University, Cleveland, OH, 2003-2004 Postdoctoral Fellow
University of Illinois at Chicago, Chicago, OH, 2004-2009 Postdoctoral Fellow
Research Interest:
Research in my laboratory is focused on understanding the molecular mechanisms of how muscle protein post-translational modifications (phosphorylation, radical modification, degradation, ect.) alter heart function. Key to this focus is employing an integrated and multi-level experimental approach of molecular biology, biochemistry and physiology to provide a comprehensive understanding towards the development of novel treatments for heart dysfunction.
The function of the heart as an organ is determined by its ability to pump oxygen rich blood to the organs of the body. How well the heart functions (i.e. pumps blood) is largely determined by the ability of the heart cells to produce force by shortening and generate the necessary pressures required to circulate blood. Cellular shortening is mediated by an interaction of the molecular motor myosin with actin and is regulated through the signaling molecule calcium. Muscle cell contraction can be modulated by: 1) Altering the intracellular calcium concentration. 2) Altering the response of the muscle to calcium. 3) Altering the activity of the myosin motor. My laboratory is interested in understanding the role of protein modifications to alter the muscle’s response to calcium and affect heart function. Specifically, I am interested in understanding the physiological and pathological effects of regulated or stress induced phosphorylation and radical mediated post-translational modification of the muscle proteins that regulate the interaction of myosin with actin and their effect on cardiac contractility.
Selected Publications:
- Biesiadecki, B.J., Tachampa, K., Yuan, C., de Tombe, P.P. and Solaro, R.J. (2010) Removal of the cardiac troponin I N-terminal extension improves cardiac function in aged mice. J Biol Chem 285(25):19688-19698.
- Monasky, M.M., Biesiadecki, B.J. and Janssen, P.M.L. (2010) Increased phosphorylation of tropomyosin, troponin I and myosin light chain-2 after stretch in rabbit ventricular myocardium under physiological conditions. JMCC 48(5):1023-1028.
- Biesiadecki, B.J., Kobayashi, T., Walker, J.S., Solaro, R.J., de Tombe, P.P. (2007) Troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser-23/24 phosphorylation. Circulation Research 100(10):1486-1493.
- Biesiadecki, B.J., Nosek, T.M. and Jin, J.-P. (2007) Functional effect of the NH2-terminal variable region of troponin T. Biochemistry 46(5):1368-1379.
- Biesiadecki, B.J., Schneider, K.L., Yu, Z.-B., Chong, S.M. and Jin, J.-P. (2004) An R111C polymorphism in wild turkey cardiac Troponin I accompanying the dilated cardiomyopathy-related abnormal splicing variant of cardiac troponin T with potentially compensatory effects. J. Biol. Chem. 279(14):13825-13832.
- Biesiadecki, B.J., Elder, B.D., Yu, Z.B. and Jin, J.-P. (2002) Cardiac troponin T variants produced by aberrant splicing of multiple exons in animals with high instances of dilated cardiomyopathy. J Biol Chem. 277(52):50275-50285.
- Biesiadecki B.J. and Jin J.-P. (2002) Exon skipping in cardiac troponin T of turkeys with inherited dilated cardiomyopathy. J Biol Chem. 277(21):18459-18468.
- Biesiadecki, B.J., Brand, P.H., Koch, L.G., Metting, P.J. and Britton, S.L. (1999) Phenotypic variation in sensorimotor performance among eleven inbred rat strains. American Journal of Physiology 276(5 Pt 2):R1383-R1389.
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