Effect of genistein, a tyrosine kinase inhibitor, on U46619-induced phosphoinositide phosphorylation in human platelets |
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Authors: | D C Gaudette B J Holub |
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Institution: | Department of Nutritional Sciences, University of Guelph, Ontario, Canada. |
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Abstract: | Recent evidence suggests that the agonist-induced formation of phosphatidylinositol 4-phosphate (PIP) and phosphatidylinositol 4,5-bisphosphate (PIP2) via PI and PIP kinases may play an important role in transmembrane signalling. In the present work, the effect of genistein, a specific inhibitor of protein-tyrosine kinase, on phosphoinositide phosphorylation was studied in human platelets stimulated with the endoperoxide analogue, U46619. At 100 microM concentration, genistein, but not the related compounds, flavone and biochanin A, which possess only weak anti-protein-tyrosine kinase activity, significantly inhibited the U46619-induced accumulation of 3H]PIP (by 71%) and 3H]PIP2. These data suggest that phosphoinositide phosphorylation may be regulated, in part, by tyrosine phosphorylation in U46619-stimulated platelets. |
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