In Memoriam

Saul Winegrad, M.D.

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Department: Physiology

Contact information
B307 Richards Building
University of Pennsylvania School of Medicine
Philadelphia, PA 19104-6085
University of Pennsylvania, 1952.
University of Pennsylvania, 1956.
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Description of Research Expertise

My laboratory is studying the physiological regulation of the properties of the contractile proteins in cardiac muslce, with particular emphasis on the ability of the proteins to generate force and hydrolyze adenosine triphosphate (ATP) as their source of energy.

Completed work has already shown that the sensitivity of the contractile system to its normal activator, calcium ions, is modified by neuroendocrine mechanisms operating through receptors in the cell membrane.

Current work is focused on defining a second regulatory system that modulates the amount of force and the velocity of shortening developed by the contractile proteins in response to a constant level of activator. This system, also under neuroendocrine control, involved an as yet unidentified regulator protein.

The major aims of the laboratory are to isolate the protein, define the molecular basis of its activity and the genetic control of its production, and identify the intracellular structures that are concerned with its sotorage and release. The studies use
physiological and biophysical techniques and computer controlled methods for correlating subcellular structure with biochemical function. Structure function correlations at the resolution of the light and electron microscope are important aspects of the work.

Selected Publications

I. Kulikovskaya, G. McClellan, R. Levine, and S. Winegrad: Effect of extraction of myosin binding protein C on contractility of rat heart. Amer. J. Physiol 2003 Notes: Currently in press.

G. McClellan, I. Kulikovskaya, S. Winegrad: Changes in Cardiac Contractility Related to Calcium Mediated Changes in Phosphorylation of Myosin Binding Protein-C. Biophys. J in press 2001.

R.Levine,A.Weisberg, B.Millman, I.Kulikovskaya, G.McClellan & S.Winegrad: Multiple Structures of Thick Filaments in Resting Cardiac Muscle and their Influence on Cross Bridge Interactions. Biophys. J. in press 2001.

S. Winegrad: Gene Mutation in Cardiac Myosin Binding Protein C. J. Molec. Cell. Cardiol. September 2001 Notes: Currently in press.

Winegrad S.: Myosin binding protein C, a potential regulator of cardiac contractility. [letter; comment]. [Review] [21 refs] Circulation Research 86(1): 6-7, Jan 7-21 2000.

Winegrad S., Henrion D., Rappaport L., Samuel JL.: Self-protection by cardiac myocytes against hypoxia and hyperoxia. Circulation Research 85(8): 690-8, Oct 15 1999.

Winegrad S.: Cardiac myosin binding protein C. [Review] [78 refs] Circulation Research 84(10): 1117-26, May 28 1999.

S. Winegrad: Cardiac myosin binding protein C. Circ. Res 84: 1117-1126, 1999.

S. Winegrad: How actin-myosin interactions differ with different isoforms of myosin. Circ. Res. 82: 1109-1110, 1999.

S Winegrad, D. Henrion, L. Rappaport, J-L. Samuel: Self-protection of cardiac myocytes from hypoxia and hyperoxia. Circ. Res. 85: 690-698, 1999.

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Last updated: 08/30/2004
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