Phosphatidylinositol-specific phospholipase-C of platelets: association with 1,2-diacyglycerol-kinase and inhibition by cyclic-AMP. |
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Authors: | M M Billah E G Lapetina P Cuatrecasas |
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Institution: | Department of Molecular Biology, The Wellcome Research Laboratories, 3030 Cornwallis Road, Research Triangle Park, North Carolina 27709, U.S.A. |
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Abstract: | Horse platelets prelabeled with 14C]arachidonate (AA) rapidly degrade 14C]phosphatidylinositol (PI) to 14C]1,2-diacylglycerol (DG) upon treatment with deoxycholate (DOC). This phospholipase-C (PLC) activity is specific for PI since other phospholipids or neutral lipids are not affected. Although exogenous Ca2+ is not required for activity, EGTA or EDTA abolishes PI degradation. Addition of Mg2+ (1 mM) and ATP (1 mM) results in phosphorylation of the DG and production of phosphatidic acid (PA). Higher concentrations of DOC inhibit DG-kinase. These observations, together with the fact that different platelet agonists induce a rapid degradation of PI and production of PA, indicate that PLC and DG-kinase activities are intimately linked. Incubation of platelets with dibutyryl cyclic-AMP, cyclic AMP-phosphodiesterase inhibitors and pyridoxal-5′-phosphate, which prevent platelet aggregation, inhibits the DOC-dependent conversion of PI to DG. The activity of PLC may play a central role in mediating platelet function and aggregation. |
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Keywords: | Phosphatidylinositol PI 1 2-diacylglycerol DG phosphatidic acid PA deoxycholate DOC phospholipase-C PLC arachidonic acid AA TM O3B-208/1/lr |
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