The Protein Kinase C (PKC) family of homologous serine/threonine protein kinases is involved in a number of processes such as growth, differentiation, and cytokine secretion. At least eleven isozymes have been described. PKC consists of a single polypeptide chain containing four conserved regions (C) and five variable regions (V). The N-terminal half interacts with PKC activators Ca2+, phospholipid, diacylglycerol, or phorbol ester, while the C-terminal half contains the catalytic domain. The conventional PKC subfamily (alpha, beta1, betaII, and gamma) is regulated by both Ca2+ and diacylglycerol. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters, and growth factors. The phosphorylation of multiple sites in PKCs regulates their activity
