Satoh T, Kouns W C, Yamashita Y, Kamiyama T, Steiner B
Nippon Roche Research Center, Kanagawa, Japan.
Biochem Biophys Res Commun. 1994 Oct 14;204(1):325-32. doi: 10.1006/bbrc.1994.2463.
The specificity of tetrafibricin was examined by comparing its activities on GPIIb/IIIa and on the vitronectin receptor (alpha v beta 3) with those of Arg-Gly-Asp-Ser (RGDS) on the same receptors. Tetrafibricin, which inhibited fibrinogen-GPIIb/IIIa binding 10 times more potently than RGDS, was three orders of magnitude less potent compared to RGDS on the inhibition of fibrinogen binding to alpha v beta 3. Furthermore, tetrafibricin potently inhibited platelet adhesion to both fibrinogen and von Willebrand factor. Whereas, there was no significant inhibition observed in the GPIIb/IIIa-independent cellular adhesions. These results suggest that tetrafibricin is highly selective for GPIIb/IIIa.
通过比较四纤维蛋白对糖蛋白IIb/IIIa和玻连蛋白受体（αvβ3）的活性与精氨酸-甘氨酸-天冬氨酸-丝氨酸（RGDS）对相同受体的活性，来检测四纤维蛋白的特异性。四纤维蛋白抑制纤维蛋白原与糖蛋白IIb/IIIa结合的效力比RGDS强10倍，但与RGDS相比，其抑制纤维蛋白原与αvβ3结合的效力低三个数量级。此外，四纤维蛋白能有效抑制血小板与纤维蛋白原和血管性血友病因子的黏附。然而，在不依赖糖蛋白IIb/IIIa的细胞黏附中未观察到明显抑制作用。这些结果表明，四纤维蛋白对糖蛋白IIb/IIIa具有高度选择性。
