PARTICIPATION OF ADP IN THE BINDING OF FIBRINOGEN TO THROMBIN-STIMULATED PLATELETS

  • 1 January 1980
    • journal article
    • research article
    • Vol. 56  (3) , 553-555
Abstract
Thrombin and 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. ADP released from the platelet apparently participates in the binding of fibrinogen to thrombin-stimulated platelets.