| Research Abstract |
Protein kinase C (PKC) is one of the hub enzyme of the variety of subcellular signaling which includes cell growth, cell differentiation, and cell motion. However, the role of PKC in the adult cardiomyocyte has not been fully elucidated. The cardiomyocytes is one of the terminally differentiated cells specialized for mechanical contraction and relaxation by using calcium as the rapid cellular signal. Since the classical PKCs are well characterized as the calcium-regulated enzymes, changes in the intracellular calcium dynamics might affect the PKC activation. This study focused the interaction of PKC with cytosolic calcium by using the in vivo determination of their concentrations and distribution with fluorescent probes. We developed the simultaneous loading of their specific fluorescent probes into the single myocytes which was perfused in the chamber on the stage of the confocal microscope. The calcium was visualized by indo 1, and the PKC was by a BOBIPY-phorbor-acetate derivative. Now it became possible to determine the PKC activation along with the changes of the cytosolic calcium concentration in various pathophysiological states such as ischemia or hypertrophy. We also found that in histological staining of specific PKC isoforms, delta PKC activation is the critical factor for the myocardial protection during the ischemic preconditioning.
|
