PLATELET MEMBRANE GLYCOPROTEIN IIB/IIIA - MEMBER OF A FAMILY OF ARG-GLY-ASP SPECIFIC ADHESION RECEPTORS
PLATELET MEMBRANE GLYCOPROTEIN IIB/IIIA - MEMBER OF A FAMILY OF ARG-GLY-ASP SPECIFIC ADHESION RECEPTORS
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DOI：
10.1126/science.2420006
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发表时间：
1986-03-28
期刊：
影响因子：
56.9
通讯作者：
RUOSLAHTI, E
中科院分区：
文献类型：
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作者：
PYTELA, R;PIERSCHBACHER, MD;RUOSLAHTI, E
血小板表面与血浆蛋白（如纤维蛋白原和纤维连接蛋白）的粘附相互作用在血栓形成和止血中起重要作用。含有Arg-Gly-Asp序列的合成肽抑制了这两种蛋白与血小板的结合，该序列与纤维连接蛋白中的细胞粘附位点相对应，也存在于。α中。纤维蛋白原链。由含有Arg-Gly-Asp序列的不溶七肽组成的亲和基质选择性地结合血小板洗涤剂提取物中的血小板膜糖蛋白IIb/IIIa。当与脂质体膜结合时，分离的蛋白赋予脂质体与纤维蛋白原、纤维连接蛋白和玻璃体连接蛋白包被的表面结合的能力，但不能与血栓反应蛋白或白蛋白包被的表面结合。这种血小板受体与先前鉴定的纤维连接蛋白和玻璃体连接蛋白受体相关，因为它识别Arg-Gly-Asp序列，但与其他受体不同的是，它对各种粘附蛋白具有更广泛的特异性。这些结果确定了一个粘附受体家族的存在，该家族识别序列Arg-Gly-Asp。
Adhesive interactions of the platelet surface with plasma proteins such as fibrinogen and fibronectin play an important role in thrombosis and hemostasis. The binding of both of these proteins to platelets is inhibited by synthetic peptides containing the sequence Arg-Gly-Asp, which corresponds to the cell adhesion site in fibronectin and is also present in the .alpha. chain of fibrinogen. An affinity matrix made of an insolubilized heptapeptide containing the Arg-Gly-Asp sequence selectively binds the platelet membrane glycoprotein IIb/IIIa from detergent extracts of platelets. When incorporated into liposome membranes, the isolated protein confers to the liposomes the ability to bind to surfaces coated with fibrinogen, fibronectin, and vitronectin but not to surfaces coated with thrombospondin or albumin. This platelet receptor is related to the previously identified fibronectin and vitronectin receptors in that it recognizes an Arg-Gly-Asp sequence but differs from the other receptors in its wider specificity towards various adhesive proteins. These results establish the existence of a family of adhesion receptors that recognize the sequence Arg-Gly-Asp.