Inhibition of fibrin-platelet interactions by fibrinogen-degradation fragment D.
Homogenized fibrin induced platelet aggregation and the release of serotonin from human platelets. Fragment D, purified from a plasmin digest of human fibrinogen, inhibited these platelet-fibrin interactions. Using a radiolabeled fragment D, it was possible to demonstrate saturable binding of fragment D to fibrin. Nonlabeled fragment D competed with the radiolabeled fragment D for binding to fibrin. Furthermore, the binding of fragment D to fibrin paralleled its ability to inhibit the fibrin-induced release of platelet serotonin. It is postulated that the inhibitory effect of fragment D on fibrin activation of platelets is due to the binding of fragment D to fibrin. The bound fragment D may cover up or block sites on fibrin that are involved in fibrin-platelet interactions. This would then result in inhibition of the fibrin-induced platelet aggregation and release of platelet serotonin.
D001792:Blood Platelets / Q000378:metabolism / Q000502:physiology*; D005337:Fibrin / Q000037:antagonists & inhibitors* / Q000502:physiology; D005338:Fibrin Fibrinogen Degradation Products; D006801:Humans; D010974:Platelet Aggregation; D012701:Serotonin / Q000378:metabolism
D005338:Fibrin Fibrinogen Degradation Products; D012701:Serotonin; D005337:Fibrin