This preclinical study demonstrates that the glycoprotein IIb-IIIa complex on activated platelets mediates adhesion to vitronectin via an Arg-Gly-Asp-dependent mechanism, providing mechanistic insight into platelet-vessel wall interactions.
Animal data on glycoprotein IIb-IIIa inhibition leave open any role in human thrombosis; further studies required before clinical consideration.
Platelets adhere to vitronectin substrate following activation with physiological concentrations of thrombin. Adhesion of activated platelets to vitronectin substrate is dependent upon the presence of divalent cations, the amount of vitronectin, and the duration of adhesion assay. The adhesion of platelets is inhibited by synthetic peptides containing the sequence of Arg-Gly-Asp. In addition, monoclonal antibodies to glycoprotein IIb-IIIa complex inhibit the adhesion of activated platelets to vitronectin substrate in a dose-dependent manner. These studies suggest that the glycoprotein IIb-IIIa complex on activated platelets may interact with vitronectin substrate through the Arg-Gly-Asp mechanism. Since vitronectin is present in the subendothelial matrix, it might be involved in platelet-vessel wall interactions.
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Thiagarajan et al. (1988) studied this question.
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