Long-term phorbol ester treatment dissociates phospholipase D activation from phosphoinositide hydrolysis and prostacyclin synthesis in endothelial cells stimulated with bradykinin |
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Authors: | T W Martin D R Feldman K E Goldstein J R Wagner |
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Institution: | Department of Pathology, St. Louis University School of Medicine, Missouri 63104. |
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Abstract: | Bovine pulmonary artery endothelial cells (BPAEC) were prelabeled with 3H]choline or 3H]myristic acid to selectively label endogenous phosphatidylcholine. BPAEC were stimulated with ATP and bradykinin (BK), and phospholipase D (PLD) activation was detected as a 4-fold increase in 3H]choline in cells prelabeled with 3H]choline or as a 2- to 3-fold increase in 3H]phosphatidylethanol in cells prelabeled with 3H]myristic acid and stimulated in the presence of ethanol. Pretreatment of BPAEC with 0.1 microM phorbol 12-myristate 13-acetate (PMA) for 22 hr completely inhibited agonist-induced PLD activation, whereas prostacyclin synthesis and 3H]phosphoinositide (3H]PIns) hydrolysis were enhanced in pretreated cells. Long-term PMA treatment thus dissociates agonist-induced PLD activation from 3H]PIns hydrolysis, and agonist-induced prostacyclin synthesis is not dependent upon PLD activation. |
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