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 nutrient and oxygen rich blood to the rest of the body. How well the heart functions (e.g. pumps blood) is largely determined by the ability of the heart cells to shortening and generate the necessary pressures required to circulate blood. Cellular shortening (contraction) is mediated by interaction of the molecular motor myosin with actin which is regulated by calcium binding to the regulatory protein troponin to induce the release of its inhibition. The degree of muscle cell shortening, and therefore cardiac contraction, can therefore be modulated by: 1) Altering the activity of the myosin motor. 2) Altering the intracellular calcium concentration. 3) Altering the response of the muscle thin filament regulatory proteins (troponin) to calcium.
My laboratory is interested in understanding the role of protein modifications to alter the muscle’s regulatory protein response to calcium and their effect on cardiac contractile function. Specifically, I am interested in understanding the physiological and pathological effects of stress induced cardiac muscle regulatory protein (troponin and tropomyosin) phosphorylation modification to modulate the interaction of myosin with actin and their effect on cardiac contractility.
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Education and Training
PhD, Case Western Reserve University
Post Doctoral, University of Illinois at Chicago