ADP stimulates IP3 formation in human platelets

FEBS Letters

Daniel, James L.¹  Selak, Mary¹  Smith, J.Bryan¹  Dangelmaier, Carol A.¹ 

[1] Temple University, Pharmacology Department and Thrombosis Research Center, 3400 N Broad Street, Philadephia, PA 19140, USA

关键词: (Platelet);    Polyphosphoinositide;    Inositol triphosphate;    Myosin phosphorylation;    Ca2+ Phosphatidic acid;    PI;    phosphatidylinositol;    PIP;    phosphatidylinositol 4-phosphate;    PIP2;    phosphatidylinositol 4;    5-phosphate;    IP3;    inositol 1;    4;    5-triphosphate;    PAF;    platelet activating factor;   

DOI  :  10.1016/0014-5793(86)81000-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Aspirinated human platelets labeled with ³²PO₄ showed a 1.7-fold increase in [³²P]IP₃ when stimulated with ADP. ADP-stimulated mobilization of internal Ca²⁺ and phosphorylation of myosin were enhanced in the presence of extracellular Ca²⁺ but the increase in IP₃ was not significantly affected by external Ca²⁺. The Ca²⁺ ionophore, ionomycin, elevated internal Ca²⁺ and induced myosin phosphorylation without a detectable change in IP₃. These results indicate that the mechanism of ADP stimulation of human platelets is similar to that of other platelet agonists and supports the theory that IP₃ functions to liberate internal Ca²⁺.

【 授权许可】

Unknown