Collagen derived octapeptide inhibits platelet procoagulant activity induced by the combined action of collagen and thrombin.

Platelet prothrombin converting activity was measured in a system using washed human platelets and purified coagulation factors Xa, Va and prothrombin. Exposure of platelet prothrombin converting activity evoked by collagen or the combined action of collagen and thrombin was effectively inhibited when a collagen derived octapeptide was added prior to platelet activation. Half maximal inhibition of prothrombinase activity of platelets stimulated by collagen plus thrombin- or collagen alone was obtained at 0.9 mM and 0.5 mM octapeptide, respectively. This suggests a modifying effect of thrombin on the platelet-collagen interaction. Octapeptide either alone or in combination with thrombin was unable to enhance platelet procoagulant activity. The increased prothrombin converting activity seen upon treatment of platelets with ionophore A23187 was not affected by octapeptide, added either before or after treatment with ionophore. It is concluded that octapeptide specifically interferes with the platelet-collagen interaction required to generate a procoagulant surface which enhances the rate of thrombin formation.