Institute of Pathology Rikshospitalet, N-0027, Oslo, Norway.
Platelets. 1993;4(4):225-9. doi: 10.3109/09537109309013222.
The effect of vitronectin on platelet aggregation has been investigated. Vitronectin inhibited both thrombin- and ADP-induced platelet aggregation in a dose-dependent manner. A monoclonal antibody (MoAb) to vitronectin increased thrombin-induced platelet aggregation. This effect of the MoAb was not mediated via the platelet Fc-receptor, suggesting that the antibody directly counteracted the inhibitory effect of vitronectin on platelet aggregation. Like some other adhesive proteins such as fibrinogen, fibronectin, and von Willebrand factor, vitronectin contains the amino-acid sequence Arg-Gly-Asp (RGD) which enables binding to the platelet membrane glycoprotein complex IIb/IIIa (GPIIb/IIIa). The results of this study indicate that vitronectin can modulate the function of fibrinogen on platelet aggregation by interfering with the binding of fibrinogen to GPIIb/IIIa in activated platelets.
已研究了 vitronectin 对血小板聚集的影响。vitronectin 以剂量依赖的方式抑制凝血酶和 ADP 诱导的血小板聚集。抗 vitronectin 的单克隆抗体 (MoAb) 增强了凝血酶诱导的血小板聚集。该 MoAb 的这种作用不是通过血小板 Fc 受体介导的，这表明抗体直接拮抗了 vitronectin 对血小板聚集的抑制作用。像纤维蛋白原、纤维连接蛋白和 von Willebrand 因子等其他一些黏附蛋白一样，vitronectin 含有氨基酸序列 Arg-Gly-Asp (RGD)，能够与血小板膜糖蛋白复合物 IIb/IIIa (GPIIb/IIIa) 结合。本研究结果表明，vitronectin 可通过干扰纤维蛋白原与活化血小板中 GPIIb/IIIa 的结合来调节纤维蛋白原对血小板聚集的功能。
