Phospholipase-D activation can be negatively regulated through the action of protein kinase C.
Transient activation of COS-1 cell phospholipase-D (PLD) in response to the protein kinase C (PKC) agonist tetradecanoyl phorbol acetate (TPA) was demonstrated by monitoring the ethanol-dependent accumulation of phosphatidylethanol (PtdEth). Transfection of COS-1 cells with PKC-alpha (wild type and constitutively activated mutants) produced no detectable ptdEth on incubation of transfected cells in the presence of ethanol. However, the response of transfected cells to subsequent TPA stimulation was inhibited, consistent with a role for the PKC-alpha in the suppression of PLD activity.
McKinnon
M
M
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, London, UK.
Parker
P J
PJ
D000818:Animals; D002460:Cell Line; D015536:Down-Regulation; D004789:Enzyme Activation / Q000187:drug effects; D000431:Ethanol / Q000494:pharmacology; D005786:Gene Expression Regulation; D020404:Glycerophospholipids; D010712:Phosphatidic Acids / Q000032:analysis; D010739:Phospholipase D / Q000235:genetics / Q000378:metabolism*; D011493:Protein Kinase C / Q000235:genetics / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014162:Transfection
D020404:Glycerophospholipids; D010712:Phosphatidic Acids; C051521:phosphatidylethanol; D000431:Ethanol; D011493:Protein Kinase C; D010739:Phospholipase D; D013755:Tetradecanoylphorbol Acetate