Members of the protein kinase C (PKC) family play a key regulatory role in a variety of cellular functions including cell growth and differentiation, gene expression, hormone secretion and membrane function. PKCs were originally identified as serine/threonine protein kinases whose activity was dependent on calcium and phospholipids. Diacylglycerols (DAG) and tumor promoting phorbol esters bind to and activate PKC. PKCs can be subdivided into at least two major classes including conventional PKC isoforms (α, βI, βII and γ) and novel PKC isoforms. Patterns of expression for each PKC isoform differ among tissues and PKC family members exhibit clear differences in their cofactor dependencies. For instance, the kinase activities of nPKC δ and are independent of Ca2+. On the other hand, nPKC δ and ε, as well as all of the cPKC members, possess phorbol ester-binding activities and kinase activities.
