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Phosphorylation of phosphoinositides in human platelets

Journal Article · · Thromb. Res.; (United States)

32P-labelling of phosphatidylinositol (PI), PI-4-monophosphate (PIP), PI-4,5-bisphosphate (PIP2) and phosphatidic acid (PA) in /sup 32/P-labelled intact human platelets was investigated in the presence of various agents which alter intracellular level of cAMP or Ca/sup 2 +/. Addition of dibutyryl cAMP to intact platelets pre- or pulse labelled with /sup 32/P resulted in increased /sup 32/P-labelling of PIP and in concomitant decreased /sup 32/P-labelling of PI without affecting that of PIP2 or PA. Similar changes were observed in intact platelets treated by prostaglandin I2 (PGI2) or a new low Km phosphodiesterase inhibitor (DN-9693). When intracellular Ca/sup 2 +/ was chelated by loading quin 2-AM to intact platelets, /sup 32/P-labelling of PIP was significantly increased in a dose related manner. From these observations it was concluded that PI kinase is activated by elevation of cAMP or chelation of Ca/sup 2 +/ in intact platelets.

Research Organization:
Osaka Univ. Medical School, Japan
OSTI ID:
6937303
Journal Information:
Thromb. Res.; (United States), Journal Name: Thromb. Res.; (United States) Vol. 2; ISSN THBRA
Country of Publication:
United States
Language:
English