Title : Protein kinase Calpha is a major mediator of the stimulatory effect of phorbol ester on phospholipase D-mediated hydrolysis of phosphatidylethanolamine.

Pub. Date : 1996 Nov 15

PMID : 8910539






3 Functional Relationships(s)
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1 Stimulation of phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine (PtdCho) by phorbol 12-myristate 13-acetate (PMA) has been shown to be mediated by the alpha- and betaI-isoforms of protein kinase C (PKC). Phosphatidylcholines protein kinase C alpha Homo sapiens
2 Stimulation of phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine (PtdCho) by phorbol 12-myristate 13-acetate (PMA) has been shown to be mediated by the alpha- and betaI-isoforms of protein kinase C (PKC). Phosphatidylcholines protein kinase C alpha Homo sapiens
3 Stable expression of PKC-alpha in MCF-7 cells, which was accompanied by increased levels of the betaI- and theta-isoforms as well, greatly enhanced both PMA-induced PLD-mediated formation of phosphatidylethanol (approximately 5-fold) and the hydrolysis of PtdEtn (2.5-2.9-fold) and PtdCho (5.5-7.2-fold). Phosphatidylcholines protein kinase C alpha Homo sapiens