血小板膜糖蛋白IIb和IIIa与纤维蛋白原的复合物形成。
Complex formation of platelet membrane glycoproteins IIb and IIIa with fibrinogen.
作者信息
Nachman R L, Leung L L
出版信息
J Clin Invest. 1982 Feb;69(2):263-9. doi: 10.1172/jci110448.
Abstract
We have recently reported the isolation of purified platelet membrane glycoproteins IIb and IIIa and the generation of monospecific antisera to these membrane proteins. Using these monospecific antisera in an enzyme-linked immunosorbent assay system, it is no demonstrated that glycoprotein IIb (GPIIb) and glycoprotein IIIa (GPIIIa) form a complex with purified human fibrinogen. The formation of this GPIIb-GPIIIa fibrinogen complex is calcium dependent, fibrinogen specific, saturable, and inhibited by specific amino sugars and amino acids. These observations suggest that the GPIIb-GPIIIa macromolecular complex on the platelet surface acts under the proper physiologic circumstances as the fibrinogen binding site required for normal platelet aggregation.
摘要
我们最近报道了纯化的血小板膜糖蛋白IIb和IIIa的分离以及针对这些膜蛋白的单特异性抗血清的产生。在酶联免疫吸附测定系统中使用这些单特异性抗血清，现已证明糖蛋白IIb（GPIIb）和糖蛋白IIIa（GPIIIa）与纯化的人纤维蛋白原形成复合物。这种GPIIb - GPIIIa纤维蛋白原复合物的形成是钙依赖性的、纤维蛋白原特异性的、可饱和的，并被特定的氨基糖和氨基酸所抑制。这些观察结果表明，血小板表面的GPIIb - GPIIIa大分子复合物在适当的生理情况下作为正常血小板聚集所需的纤维蛋白原结合位点发挥作用。
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