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• W2106877372 endingPage "1452" @default.
• W2106877372 startingPage "1433" @default.
• W2106877372 abstract "Protein kinase C (PKC) is a multifunctional, cyclic nucleotide-independent protein kinase that phosphorylates serine and threonine residues in many target proteins. This enzyme was identified in bovine cerebellum by Nishizuka and co-workers (Takai et al., 1977; Inoue et al., 1977) as a protein kinase that phosphorylated histone and protamine. Since its discovery, much interest has been shown in PKC and its role in signal transduction. Development (Otte et al., 1991), memory (Alkon, 1989), differentiation (Cutler et al., 1993), proliferation (Murray et al., 1993) and carcinogenesis (Ashendel, 1985) all are processes for which PKC has been implicated. Once thought to be a single protein, PKC is now known to comprise a large family of enzymes that differ in structure, cofactor requirements and function. Indeed, the PKC family is the largest serine/threonine-specific kinase family known (Parker, 1992) to which many cellular responses have been credited (Nishizuka, 1995). This enzyme multiplicity, together with variation in cellular and tissue distribution, and abundance might explain why so many signal transduction functions have been attributed to this kinase. Here we briefly describe the organization and regulation of PKC and review the current understanding of their role in the regulation of airways smooth muscle (ASM) tone and mitogenesis, which have been investigated in some detail." @default.
• W2106877372 created "2016-06-24" @default.
• W2106877372 creator A5005726780 @default.
• W2106877372 creator A5018753336 @default.
• W2106877372 creator A5020153149 @default.
• W2106877372 date "2000-08-01" @default.
• W2106877372 modified "2023-10-01" @default.
• W2106877372 title "Protein kinase C isoenzymes: a review of their structure, regulation and role in regulating airways smooth muscle tone and mitogenesis" @default.
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