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Biochem Biophys Res Commun. 1995 Jan 5;206(1):429-36.

A protein kinase C isozyme, nPKC epsilon, is involved in the activation of NF-kappa B by 12-O-tetradecanoylphorbol-13-acetate (TPA) in rat 3Y1 fibroblasts.

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Department of Molecular Biology, Yokohama City University School of Medicine, Japan.


In order to examine whether PKC is involved in the activation of NF-kappa B by TPA, we overexpressed a variety of PKC isozymes in rat 3Y1 fibroblasts and monitored the expression of the co-transfected reporter NF-kappa B gene. In contrast to TPA response element (TRE), where overexpression of a variety of PKC isozymes results in enhanced activation by TPA, activation of NF-kappa B by TPA is not enhanced by overexpression of PKC isozymes such as cPKC alpha, nPKC delta, or nPKC theta. However, the overexpression of nPKC epsilon does result in enhancement. A kinase-negative point mutant of nPKC epsilon, where Lys at the ATP binding site is altered to Arg, does not cause this enhancement of NF-kappa B activation. Further, the kinase-negative nPKC epsilon partially suppresses endogenous NF-kappa B activity. These results suggest that nPKC epsilon is specifically involved in the activation of NF-kappa B when cells are treated with TPA.

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