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doi: 10.1007/bf02536077
pmid: 8355574
AbstractTreatment of [14C]choline‐ or [14C]ethanolamine‐labeled NIH 3T3 fibroblasts withBacillus cereus phosphatidylcholine‐specific phospholipase C (PLC) enhanced phospholipase D (PLD)‐mediated hydrolysis of the respective14C‐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 of14C]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.
Dose-Response Relationship, Drug, Hydrolysis, Phosphatidylethanolamines, Phosphorylcholine, 3T3 Cells, Fibroblasts, Choline, Mice, Type C Phospholipases, Phosphatidylcholines, Phospholipase D, Animals, Tetradecanoylphorbol Acetate, Phospholipids, Protein Kinase C
Dose-Response Relationship, Drug, Hydrolysis, Phosphatidylethanolamines, Phosphorylcholine, 3T3 Cells, Fibroblasts, Choline, Mice, Type C Phospholipases, Phosphatidylcholines, Phospholipase D, Animals, Tetradecanoylphorbol Acetate, Phospholipids, Protein Kinase C
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