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The expression of glycoprotein GMP-140 (P-selectin, CD-62P) is stimulated in human platelets by vasopressin via G protein-coupled receptors. In order to clarify the subsequent intracellular signal pathway, we examined the role of protein kinases in vasopressin action on thrombocytic CD62P expression in normal subjects. Staurosporine, a protein kinase (PK) C inhibitor, inhibited platelet aggregation and CD62P expression, whereas phorbol ester (PMA), a PKC stimulator, provoked them. On the other hand, 8-bromo-adenosine-3′,5′-monophosphate-cyclic AMP (8-Br-cAMP), a membrane permeant cAMP analogue, had no effect on platelet activation. PMI, a PKA inhibitor, had a little effect on them. From these results, it is suggested that PKC plays a dominant role in AVP action on platelet aggregation and CD62P expression. |
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