Abstract
The lectin wheat germ agglutinin (WGA) elicited a prompt and sharp increase in intracellular Ca 2+ concentration in human platelets. The WGA- induced Ca 2+ mobilization was markedly inhibited by a protein kinase inhibitor staurosporine, whereas Ca 2+ mobilization by receptor-mediated agonists, including thrombin, platelet-activating factor, and arginine-vasopressin, was not. In contrast, the lectin-induced Ca 2+ mobilization was resistant to cyclic AMP inhibition, compared with that induced by receptor-mediated agonists. These findings indicate that the mechanism of intracellular Ca 2+ mobilization, or possibly phospholipase C activation, induced by WGA is different from that induced by receptor-mediated agonists in human platelets.
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