Protein kinase C-epsilon anchors at key sites on the sarcomere and enhances myocyte function in the short term by phosphorylating specific calcium channels and contractile proteins. Protein kinase C-delta translocates to the nucleus where it regulates gene expression for longer term changes in myocyte physiology. These hypotheses are being tested by biophysical, imaging and molecular approaches with an emphasis on identifying and manipulating organelle-specific anchoring proteins, and creating mutations in critical phosphorylation sites in cultured myocytes and in mouse hearts. The laboratory is also actively involved in the development of optical probes so that signaling mechanisms can be dissected with high temporal and spatial resolution using modern light microscopy. Positive inotropy mediated by diacylglycerol in rat ventricular myocytes.
Arachidonic acid stimulates protein kinase C-epsilon redistribution in heart cells.
J. Cell Sci. Biologically active peptides caged on tyrosine. Signaling pathways underlying Eosinophil motility revealed using caged peptides. Role of intracellular calcium and pH in the positive inotropic response of cardiomyocytes to diacylglycerol. American Journal of Physiology.