Title : Phorbol ester stimulation of phosphatidylcholine synthesis requires expression of both protein kinase C-alpha and phospholipase D.

Pub. Date : 1998 May 20

PMID : 9593849






6 Functional Relationships(s)
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1 The protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) stimulates both the synthesis and phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine (PtdCho). Tetradecanoylphorbol Acetate glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens
2 The protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) stimulates both the synthesis and phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine (PtdCho). Tetradecanoylphorbol Acetate glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens
3 The protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) stimulates both the synthesis and phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine (PtdCho). Tetradecanoylphorbol Acetate glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens
4 The protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) stimulates both the synthesis and phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine (PtdCho). Tetradecanoylphorbol Acetate glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens
5 In multidrug resistant MCF-7/MDR1 cells, which highly express PKC-alpha but lack the PtdCho-specific PLD activity, 100-nM PMA had relatively small stimulatory effects on the uptake of [14C]choline (approximately 1.5-fold) and [14C]PtdCho synthesis (1.5- to 2-fold). Tetradecanoylphorbol Acetate glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens
6 In NIH 3T3 fibroblasts and MCF-7/PKC-alpha cells, both expressing PKC-alpha and PLD activities at high levels, 10-100-nM PMA enhanced [14C]choline uptake only slightly (1.7- to 2.2-fold), while it had much greater (approximately 4-9-fold) stimulatory effects on PtdCho synthesis. Tetradecanoylphorbol Acetate glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens