PMID: 8589361Oct 1, 1995Paper

Phosphoinositide metabolism triggered by wheat germ agglutinin in human platelets

International Journal of Hematology
Y YatomiS Kume

Abstract

The lectin wheat germ agglutinin (WGA) has been shown to elicit platelet functional responses such as aggregation and release reaction as a consequence of binding several cell surface glycoproteins in platelets, whereas physiological activators act on their specific receptors. To examine the mechanism of WGA-induced platelet activation, we analyzed phosphoinositide metabolism triggered by this lectin. The binding of WGA to human platelets induced a rapid and dose-dependent surge in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) hydrolysis, as monitored by an increase in [Ca2+]i and phosphatidic acid production. Furthermore, it similarly elicited the synthesis of PtdIns(3,4)P2, which is a major 3-phosphorylated phosphoinositide in platelets. This 3-phosphorylated lipid generation induced by WGA was very strong and did not appear to be a consequence of the classical PtdIns(4,5)P2 hydrolysis. WGA also induced a marked increase in the degree of tyrosine phosphorylation of proteins in platelets, and this increase was correlated with the phosphoinositide metabolism, i.e. PtdIns(4,5)P2 breakdown and PtdIns(3,4)P2 synthesis. The non-selective inhibitor of protein kinases, staurosporine, inhibited similarly both the increase in t...Continue Reading

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