Participation of ADP in the binding of fibrinogen to thrombin- stimulated
platelets
EF Plow and GA Marguerie
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.
Volume 56,
Issue 3,
pp. 553-555,
09/01/1980
Copyright © 1980 by The American Society of Hematology