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Am J Physiol Cell Physiol 265: C1681-C1688, 1993;
0363-6143/93 $5.00
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AJP - Cell Physiology, Vol 265, Issue 6 C1681-C1688, Copyright © 1993 by American Physiological Society

ARTICLES

Ni2+ impairs thrombin-induced signal transduction by acting on the agonist and/or receptor in human platelets

F. J. Azula, R. Alonso, A. Marino, M. Trueba and J. M. Macarulla
Department of Biochemistry and Molecular Biology, Faculty of Sciences, University of Basque Country, Bilbao, Spain.

We have investigated the effect of NiCl2 on platelet activation induced by thrombin, phorbol 12-myristate 13-acetate, and calcium ionophores. Besides blocking Ca2+ influx, NiCl2 inhibited platelet aggregation, intracellular Ca2+ mobilization, and phospholipase C activation induced by thrombin in a dose-dependent manner. In contrast to ionomycin, NiCl2 completely blocked the platelet aggregation and intracellular Ca2+ mobilization induced by A23187. A23187 was not able to translocate Ni2+ across the plasma membrane. Ni2+ also inhibited phorbol myristate acetate-induced platelet aggregation. The results with staurosporine and low NiCl2 concentrations are in agreement in that increases in intracellular Ca2+ concentration and protein kinase C activation are necessary for full platelet activation mediated by thrombin.


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