The bisindolylmaleimide GF 109203X, a selective inhibitor of protein kinase C, does not inhibit the potentiating effect of phorbol ester on ethanol-induced phospholipase C-mediated hydrolysis of phosphatidylethanolamine.
In fibroblasts, the protein kinase C (PKC) activator phorbol 12-myristate (PMA) either inhibits or stimulates phospholipase C-mediated hydrolysis of phosphatidylethanolamine in the absence or presence of ethanol, respectively. Here, we demonstrate that the specific PKC inhibitor bisindolylmaleimide GF 109203X prevents only the inhibitory, but not the stimulatory, PMA effect.
Hormel Institute, University of Minnesota, Austin 55912.
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D016475:3T3 Cells; D000818:Animals; D000431:Ethanol / Q000494:pharmacology*; D004983:Ethanolamines / Q000378:metabolism; D007211:Indoles / Q000494:pharmacology*; D008301:Maleimides / Q000494:pharmacology*; D051379:Mice; D010714:Phosphatidylethanolamines / Q000378:metabolism*; D011493:Protein Kinase C / Q000037:antagonists & inhibitors*; D013755:Tetradecanoylphorbol Acetate / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D010738:Type C Phospholipases / Q000378:metabolism*
D004983:Ethanolamines; D007211:Indoles; D008301:Maleimides; D010714:Phosphatidylethanolamines; D000431:Ethanol; C005448:phosphorylethanolamine; D011493:Protein Kinase C; D010738:Type C Phospholipases; C070515:bisindolylmaleimide I; D013755:Tetradecanoylphorbol Acetate