Abstract:
:The lectin wheat germ agglutinin (WGA) elicited a prompt and sharp increase in intracellular Ca2+ concentration in human platelets. The WGA-induced Ca2+ mobilization was markedly inhibited by a protein kinase inhibitor staurosporine, whereas Ca2+ mobilization by receptor-mediated agonists, including thrombin, platelet-activating factor, and arginine-vasopressin, was not. In contrast, the lectin-induced Ca2+ mobilization was resistant to cyclic AMP inhibition, compared with that induced by receptor-mediated agonists. These findings indicate that the mechanism of intracellular Ca2+ mobilization, or possibly phospholipase C activation, induced by WGA is different from that induced by receptor-mediated agonists in human platelets.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Yatomi Y,Ozaki Y,Koike Y,Satoh K,Kume Sdoi
10.1006/bbrc.1993.1239subject
Has Abstractpub_date
1993-03-15 00:00:00pages
453-8issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(83)71239-8journal_volume
191pub_type
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