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Volume 271, Number 27, Issue of July 5, 1996 pp. 16040-16046
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Protein Kinase C- mRNA Is Down-regulated Transcriptionally and Post-transcriptionally by 12-O-Tetradecanoylphorbol-13-acetate

(Received for publication, January 31, 1996, and in revised form, April 1, 1996)

From the Molecular and Cellular Biology Program, Arizona State University, Tempe, Arizona 85287-1501

Activation of protein kinase C- (PKC-) by 12-O-tetradecanoylphorbol-13-acetate (TPA) is followed by a gradual decrease in detectable protein 12-24 h later in the mouse B lymphoma cell line A20. Down-regulation is associated with TPA-induced proteolysis and a 50-86% decrease in PKC- mRNA 0.5-24 h post-treatment which is due to both a 50% decrease in transcription and accelerated degradation of PKC- mRNA as determined using the pulse-chase method. Destabilization of PKC- mRNA is also observed when actinomycin D is added to cells pretreated with TPA for 2 h; however, addition of actinomycin D or cycloheximide prior to TPA treatment blocks destabilization. Addition of PKC inhibitors to TPA-treated cells also blocks destabilization of PKC- mRNA. Cells treated with TPA for 4 h contain an activity not found in control cells which destabilizes PKC- mRNA but not glyceraldehyde-3-phosphate dehydrogenase mRNA in vitro. Addition of TPA to control extracts fails to increase degradation of PKC- mRNA in vitro, suggesting that treatment of intact cells is required to induce the synthesis of a factor(s) that destabilizes PKC- mRNA. This factor(s) then acts along with transcriptional and post-translational regulatory mechanisms to down-regulate PKC-.

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