Physiology and Biophysics Faculty

Research Interests

The primary research program in this laboratory is concerned with the regulation of contractile protein interactions. Contractile protein (actin and myosin) interactions are responsible for the contraction of muscle and many other motile processes of cells. Most of my studies are concerned with the regulation of muscle contraction in both smooth (vascular and intestinal) and striated (skeletal and cardiac) muscle. Some additional studies are also concerned with contractile processes involving the cytoskeleton. Most of my research involves the use of permeabilized cells of muscle which allow the investigator to control the intracellular concentration of ions, and proteins surrounding the regulatory and contractile proteins. In addition we are able to selectively remove regulatory proteins and to replace them with other regulatory proteins which have been genetically and modified or labeled with fluorescence probes.

In pieces of cells or bundles of permeabilized cells we are able to measure the mechanical parameter of muscle contraction and at the same time measure such parameters as Ca2+ binding to regulatory proteins, protein-protein interactions myosin light-chain phosphorylation, and energy usage(ATP hydrolysis) which are monitored by fluorescence. Collaborative studies with other investigators are concerned with the role of protein kinase C, cyclic ATP dependent protein kinase, caldesmon, IP3, diacylglycerol, and other regulatory factors play in the regulation of muscle contraction and cell motility.

• Google Scholar Citations
• PubMed Citations

Selected Publications

1. Hernandez O, Szczesna-Cordary D, Knollmann BC, Miller T, Bell M, Zhao J, Sirenko SG, Diaz Z, Guzman G, Xu Y, Wang Y, Kerrick WG, Potter JD (2005) F110I and R278C troponin T mutations that cause familial hypertrophic cardiomyopathy affect muscle contraction in transgenic mice and reconstituted human cardiac fibers. J Biol Chem. (In Press).
2. Venkatraman G, Gomes AV, Kerrick WG, Potter JD (2005) Characterization of troponin T dilated cardiomyopathy mutations in the fetal troponin isoform. J Biol Chem 280(18):17584-92.
3. Kerrick WG, Xu Y (2004) Inorganic phosphate affects the pCa-force relationship more than the pCa-ATPase by increasing the rate of dissociation of force generating cross-bridges in skinned fibers from both EDL and soleus muscles of the rat. J Muscle Res Cell Motil. 25(2):107-17.
4. Venkatraman G, Harada K, Gomes AV, Kerrick WG, Potter JD (2003) Different functional properties of troponin T mutants that cause dilated cardiomyopathy. J Biol Chem. 278(43):41670-6.
5. Allen K, Xu YY, Kerrick WG (2000) Ca²⁺ measurements in skinned cardiac fibers: effects of Mg²⁺ on Ca²⁺ activation of force and fiber ATPase. J Appl Physiol 88(1):180-5.
6. Wang Y, Xu Y, Guth K, Kerrick WG (1999) Troponin C regulates the rate constant for the dissociation of force-generating myosin cross-bridges in cardiac muscle. J Muscle Res Cell Motil 20(7):645-53.

Curriculum Vitae

• 1961 B.S. Geology/Mathematics, University of Puget Sound, Tacoma, WA
• 1971 Ph.D. Physiology and Biophysics, University of Washington 1971-1972 Postdoctoral Fellow, Physiology and Biophysics, University of Washington
• 1972-1979 Assistant Professor, Physiology and Biophysics, University of Washington
• 1979-1981 Associate Professor, Physiology and Biophysics, University of Washington
• 1982-present Professor, Physiology and Biophysics, University of Miami School of Medicine
• 1983-present Professor, Molecular and Cellular Pharmacology, University of Miami School of Medicine