Protein kinase C-dependent stimulation of phospholipase D in phospholipase C-treated fibroblasts.
Treatment of [14C]choline- or [14C]ethanolamine-labeled NIH 3T3 fibroblasts with Bacillus cereus phosphatidyl-choline-specific phospholipase C (PLC) enhanced phospholipase D (PLD)-mediated hydrolysis of the respective 14C-labeled phospholipids. PLD activity was stimulated by 1.5 U/mL of PLC and by 100 nM of the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) to similar extents. Treatment of [14C]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.
Kiss
Z
Z
Hormel Institute, University of Minnesota, Austin 55912.
Garamszegi
N
N
D016475:3T3 Cells; D000818:Animals; D002794:Choline / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D005347:Fibroblasts / Q000187:drug effects / Q000201:enzymology*; D006868:Hydrolysis; D051379:Mice; D010713:Phosphatidylcholines / Q000378:metabolism; D010714:Phosphatidylethanolamines / Q000378:metabolism; D010739:Phospholipase D / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D010767:Phosphorylcholine / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D010738:Type C Phospholipases / Q000494:pharmacology*
D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D010743:Phospholipids; D010767:Phosphorylcholine; D011493:Protein Kinase C; D010738:Type C Phospholipases; D010739:Phospholipase D; D002794:Choline; D013755:Tetradecanoylphorbol Acetate