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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. Three categories exist, conventional PKC (cPKC), novel PKC (nPKC), and atypical PKC (aPKC). These proteins are products of multiple genes and alternative splicing and have different modes of activation. For example, cPKC's members (α, βI, βII, and γ) are calcium activated, phospholipid-dependent serine/threonine specific enzymes which can also be activated by phorbol esters. However, the novel PKC (nPKC) subfamily members (δ , ε, π, and θ isoforms) and the atypical PKC (PKC) subfamily members (ζ , f , andλ isoforms) are Ca2 ; independent. The aPKC members are unique in that their activity is independent of diacylglycerols and phorbol esters. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters and growth factors. PKCθ transcripts are expressed in most tissues with the highest levels being found in hematopoietic tissues and cell lines, including T cells and thymocytes. PKCθ RNA is readily detectable in skeletal muscle, lung, and brain. However, PKCθ expression is not detected in several human carcinoma cell lines. Abundant expression of this PKC isozyme in hematopoietic cells suggests that it may have a role in growth and differentiation processes of these cells. The 9/PKC monoclonal antibody recognizes the phosphorylated threonine 538 (pT538) of human PKCθ.Western Blotting
