Regulation of phospholipase C activity in human platelets inhibitory action of cyclic AMP.
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Phospholipase C activity in membranes obtained from untreated platelets was stimulated by GTP and its analogs in a dose-dependent manner. On the other hand, membranes from dibutyryl-cyclic AMP (dbcAMP)-pretreated cells did not cause enhancement of the enzyme activity. The basal phospholipase C activity without GTPγS was not changed but the GTPγS-stimulated phospholipase C activity was markedly suppressed. However, in the the presence of a protein kinase inhibitor (H-8), this inhibitory action of cyclic AMP was not observed. The pretreatment of platelets with dbcAMP did not prevent the thrombin-induced increase in GTPγS-binding and GTPase activities. Thus, these results suggest that G-protein itself and its coupling with thrombin-receptor may not be influenced by dbcAMP pretreatment. Experiments of photoaffinity labelling with 8-N3-[γ-32P] GTP demonstrated that the membranes from dbcAMP-pretreated cells exhibited much more labelling of 240-kDa band when compared to control membranes. The 240-kDa photolabelled protein showed identifical mobility with the protein phosphorylated by cyclic AMP-dependent protein kinase.
- 一般社団法人 日本血栓止血学会の論文
一般社団法人 日本血栓止血学会 | 論文
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