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- W1532482198 abstract "A prolonged cell exposure of all examined cell types to tumour-promoting phorbol esters leads to a substantial inactivation and degradation of protein kinase C (PKC), a phenomenon known as down-regulation. With a combination of one- and two-dimensional immunoblot analyses we have previously shown the existence in PC12 cells of distinct PKC-alpha forms that differentially respond to cell treatment with phorbol ester [Gatti, A. & Robinson, P. J. (1996) J. Biol. Chem. 271, 31 718-31722]. Using the same experimental model, in the present study we investigated a possible relationship between PKC-alpha phosphorylation and its down-regulation. The exposure of PC12 cells to okadaic acid, a potent inhibitor of biologically relevant protein phosphatases, was found to partially protect PKC-alpha against phorbol-ester-mediated down-regulation. Further, a similar protective effect of okadaic acid was observed for PKC-delta and PKC-epsilon, which are also expressed in PC12 cells. These results indicate that the tumour-promoting activity of okadaic acid itself may be due to a sustained phosphorylation of PKC." @default.
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- W1532482198 date "1997-10-01" @default.
- W1532482198 modified "2023-10-14" @default.
- W1532482198 title "Okadaic Acid Interferes with Phorbol-Ester-Mediated Down-Regulation of Protein Kinase C-alpha, C-delta and C-e" @default.
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- W1532482198 doi "https://doi.org/10.1111/j.1432-1033.1997.t01-1-00092.x" @default.
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