Protein kinase C modulates phospholipase C and increases arachidonic acid release in bradykinin stimulated MDCK cells

Didier Portilla, Mary Mordhorst, William Bertrand, Aubrey R. Morrison

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

The tumor promoter phorbol ester (PMA) has been shown to stimulate protein kinase C (PKC) in MDCK cells. At the concentrations that produce stimulation of PKC, PMA (100μM) inhibits BK-induced I1,4,5P3 (IP3) formation and calcium transients in these cells. 1-5-isoquinolinyl-2-methyl-piperazine (H7) a known inhibitor of PKC in MDCK cells reverses the effect of PMA on BK-stimulated IP3 formation and Ca+2 transients in these cells. PMA also stimulates arachidonate release which can be inhibited by preincubation with H7. A dual mechanism of regulation by PKC at the level of phospholipase C (down regulation) and phospholipase A2 (stimulation) is suggested in these cells.

Original languageEnglish
Pages (from-to)454-462
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume153
Issue number1
DOIs
StatePublished - May 31 1988

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