PuSH - Publication Server of Helmholtz Zentrum München: Phorbol Ester-induced Myeloid Differentiation is Mediated by Protein Kinase C-Alpha and-Delta and not by Protein Kinase C-BetaII, -Epsilon, -Zeta, and -Eta.

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Mischak, H. ; Pierce, J.H. ; Goodnight, J. ; Kazanietz, M.G. ; Blumberg, P.M. ; Mushinski, J.F.

Phorbol Ester-induced Myeloid Differentiation is Mediated by Protein Kinase C-Alpha and-Delta and not by Protein Kinase C-BetaII, -Epsilon, -Zeta, and -Eta.

J. Biol. Chem. 268, 20110-20115 (1993)

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It is generally accepted that the multiple, similar protein kinase C (PKC) isoq mes are responsible for different specialized physiol < gical processes, but evidence that directly assigns specific functions to specific isozymes is scarce. To test whether specific PKC isozymes are involved in myeloid differentiation, we have studied the effect of overexpression of PKC-a, -011, -6, -6, -( and -q in 32D, a mouse myeloid progenitor cell line that does not differentiate in response to 12-0-tetradecanoylphorbol-13-acetate (TPA). No significant morphological or phenotypic changes could be observed in unstimulated cells that overexpress any of these isozymes. However, the cell lines that overexpressed PKC-a or -6 had acquired the ability to become mature macrophages 2-6 h after TPA stimulation. The overexpression of PKC-BII, -6, -f, or -q, in contrast, did not permit TPA-induced differentiation. These results indicate that only these two members of the PKC gene family can participate in TPA-induced myeloid differentiation

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