Key result
Monoclonal antibodies against the platelet type I collagen receptor inhibit collagen-induced platelet aggregation and adhesion.
Monoclonal antibodies against the platelet type I collagen receptor demonstrate that collagen-induced platelet aggregation is mediated through direct interaction with this specific receptor.
Antibody blockade of the type I collagen receptor inhibits platelet aggregation in animal models; leaves open translation to human antithrombotic strategies.
Monoclonal antibodies to the purified platelet type I collagen receptor were produced to study platelet receptor function. The antibody specifically reacted with the platelet receptor in immunoblot experiments. The IgG purified from the monoclonal antibodies and isolated Fab' fragments inhibited the binding of radiolabeled alpha 1(I) chain to washed platelets competitively. Soluble and fibrillar type I collagen-induced platelet aggregations were inhibited by purified IgG suggesting that soluble and fibrillar collagens shared a common receptor. The adhesion of platelets to an artificial collagen matrix was also inhibited by the monoclonal antibody. However, adenosine diphosphate-induced platelet aggregation was not inhibited by the same amount of IgG that inhibited collagen-induced platelet aggregation. The results suggest that collagen-induced platelet aggregation is mediated through the interaction of collagen with the platelet receptor.
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Chiang et al. (1987) studied this question. Monoclonal antibodies to the purified platelet type I collagen receptor was evaluated on Platelet aggregation and adhesion to collagen matrix. Monoclonal antibodies against the platelet type I collagen receptor inhibited collagen-induced platelet aggregation and adhesion, suggesting aggregation is mediated through this receptor.
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