Participation of ADP in the binding of fibrinogen to thrombin-stimulated platelets.
Thrombin and adenosine diphosphate (ADP) supported the binding of 125I-fibrinogen to washed human platelets with similar kinetics and affinity. Platelet secretion, as measured by 14C-serotonin release, and fibrinogen binding exhibited an identical dependence on thrombin concentration. Enzymatic removal of ADP with apyrase or creatine phosphate/creatine phosphokinase (CP/CPK) from thrombin-stimulated platelets markedly inhibited 125I-fibrinogen binding, but pretreatment of platelets with CP/CPK prior to thrombin stimulation was without effect. Thus, ADP, released from the platelet, participates in the binding of fibrinogen to thrombin-stimulated platelets.
D000244:Adenosine Diphosphate / Q000378:metabolism* / Q000494:pharmacology; D001792:Blood Platelets / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D012701:Serotonin / Q000378:metabolism; D013268:Stimulation, Chemical; D013917:Thrombin / Q000494:pharmacology; D013997:Time Factors
D012701:Serotonin; D000244:Adenosine Diphosphate; D005340:Fibrinogen; D013917:Thrombin