Feedback regulation of phospholipase C-beta by protein kinase C.
作者： S H Ryu , U H Kim , M I Wahl , A B Brown , G Carpenter
DOI: 10.1016/S0021-9258(18)38254-1
关键词:
摘要: Treatment of a variety cells and tissues with 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator protein kinase C (PKC) results in the inhibition receptor-coupled inositol phospholipid-specific phospholipase (PLC) activity. To determine whether or not targets TPA-activated PKC include one more isozymes PLC, studies were carried out PC12, C6Bu1, NIH 3T3 cells, which contain at least three PLC isozymes, PLC-beta, PLC-gamma, PLC-delta. TPA stimulated phosphorylation serine residues but state PLC-gamma PLC-delta was changed significantly. Phosphorylation bovine brain PLC-beta by vitro resulted stoichiometric incorporation phosphate 887, without any concomitant effect on We propose, therefore, that rather than having direct enzyme activity, may alter its interaction putative guanine nucleotide-binding regulatory thereby prevent activation.
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