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Protein kinase C‐dependent stimulation of phospholipase D in phospholipase C‐treated fibroblasts
Author(s) -
Kiss Zoltan,
Garamszegi Nandor
Publication year - 1993
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536077
Subject(s) - phosphatidylethanol , phospholipase d , protein kinase c , phospholipase c , activator (genetics) , phospholipase , chemistry , phorbol , biochemistry , stimulation , bisindolylmaleimide , phosphatidic acid , microbiology and biotechnology , phosphorylation , enzyme , biology , phospholipid , receptor , endocrinology , membrane
Treatment of [ 14 C]choline‐ or [ 14 C]ethanolamine‐labeled NIH 3T3 fibroblasts with Bacillus cereus phosphatidylcholine‐specific phospholipase C (PLC) enhanced phospholipase D (PLD)‐mediated hydrolysis of the respective 14 C‐labeled phospholipids. PLD activity was stimulated by 1.5 U/mL of POLC and by 100 nM of the protein kinase C (PKC) activator phorbol 12‐myristate 13‐acetate (PMA) to similar extents. Treatment of 14 C]palmitic acid‐labeled fibroblasts with PLC in the presence of ethanol also enhanced PLD‐mediated formation of phosphatidylethanol; the effects of PLC and PMA were nonadditive. PLC had no effect on PLD activity in fibroblasts in which PKC was down‐regulated by prolonged (24 h) treatment with 300 nM PMA. These data indicate that treatment of fibroblasts with exogenous PLC results in PKC‐dependent activation of PLD.