Role of protein kinase C in phytohemagglutinin-stimulated induction of spermidine/spermine N1-acetyltransferase.
We studied the involvement of protein kinase C in the induction of spermidine/spermine N1-acetyltransferase, a rate-limiting enzyme of polyamine degradation, in bovine lymphocytes. When phytohemagglutinin (PHA) and H-7, a protein kinase inhibitor, were added simultaneously to lymphocyte cultures, the elevation caused by PHA of spermidine/spermine N1-acetyltransferase activity at 24 h after administration was reduced. In cells treated with a lower concentration of PHA, the acetyltransferase activity was enhanced with 12-o-tetradecanoyl phorbol-13-acetate (TPA), an activator of protein kinase C, and reached the level of cells with a higher concentration of PHA. PHA did not cause maximum induction of the enzyme in cells treated with 160 ng/ml TPA. The induction of this acetyltransferase with PHA is probably mediated by protein kinase C.
Matsui-Yuasa
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Department of Biochemistry, Osaka City University Medical School, Japan.
Otani
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Morisawa
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D000123:Acetyltransferases / Q000096:biosynthesis / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D004790:Enzyme Induction / Q000187:drug effects; D066298:In Vitro Techniques; D007202:Indicators and Reagents; D008214:Lymphocytes / Q000201:enzymology*; D010835:Phytohemagglutinins / Q000494:pharmacology*; D011493:Protein Kinase C / Q000502:physiology*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D000099228:Diamine N-Acetyltransferase
D000123:Acetyltransferases; D007202:Indicators and Reagents; D010835:Phytohemagglutinins; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate; D000099228:Diamine N-Acetyltransferase