Isolation and characterization of a platelet surface collagen binding complex related to VLA-2.
Isolation and characterization of a platelet surface collagen binding complex related to VLA-2.
复制标题
与 VLA-2 相关的血小板表面胶原蛋白结合复合物的分离和表征。
DOI：
10.1016/s0006-291x(88)81211-7
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发表时间：
1988
影响因子：
3.1
通讯作者：
WoodsJr,VL
中科院分区：
文献类型：
--
作者：
Santoro,SA;Rajpara,SM;Staatz,WD;WoodsJr,VL
已从血小板膜中分离出一种异二聚体、Mg++ 依赖性胶原结合蛋白。电泳特性和单克隆抗体反应性表明复合物的重链是血小板膜糖蛋白Ia，轻链是糖蛋白IIa。此外，该受体似乎与最近在活化的 T 淋巴细胞、血小板和其他细胞上发现的 VLA-2 复合物相同。当掺入脂质体时，纯化的复合物介导脂质体与胶原基质的 Mg++ 依赖性粘附。这些观察结果表明，VLA-2 复合物介导血小板和其他细胞中胶原蛋白的细胞粘附。
A heterodimeric, Mg++-dependent, collagen binding protein has been isolated from platelet membranes. Electrophoretic properties and monoclonal antibody reactivity indicate that the heavy chain of the complex is platelet membrane glycoprotein Ia and that the light chain is glycoprotein IIa. Furthermore, the receptor appears to be identical with the recently defined VLA-2 complex found on activated T-lymphocytes, platelets and other cells. When incorporated into liposomes, the purified complex mediates the Mg++-dependent adhesion of the liposomes to collagen substrates. These observations suggest that the VLA-2 complex mediates cellular adhesion to collagen in platelets and possibly in other cells.