HUMAN-ENDOTHELIAL CELLS SYNTHESIZE AND EXPRESS AN ARG-GLY-ASP-DIRECTED ADHESION RECEPTOR INVOLVED IN ATTACHMENT TO FIBRINOGEN AND VONWILLEBRAND-FACTOR
HUMAN-ENDOTHELIAL CELLS SYNTHESIZE AND EXPRESS AN ARG-GLY-ASP-DIRECTED ADHESION RECEPTOR INVOLVED IN ATTACHMENT TO FIBRINOGEN AND VONWILLEBRAND-FACTOR
复制标题
DOI：
10.1073/pnas.84.18.6471
复制
发表时间：
1987-09-01
影响因子：
11.1
通讯作者：
CHERESH, DA
中科院分区：
文献类型：
--
作者：
CHERESH, DA
人脐静脉内皮细胞表达了由非共价相关的.alpha组成的异二聚体粘附受体复合物。和.beta。在还原条件下的亚基的分子质量分别为135 kDa和115 kDa。该复合物可以从由含有ARG-AP-APP的肝肽组成的亲和力基质中分离出来，并通过针对针对人类黑色素瘤细胞的玻璃体受体的单克隆抗体（MAB）特异性免疫沉淀。这些数据表明，该复合物是大型细胞粘附受体家族的成员之一。其中一种mABS是LM609，抑制了人内皮细胞与纤维蛋白原，von Willebrand因子和玻璃纤维素的附着，但对这些细胞与纤连蛋白，胶原蛋白或层粘连蛋白的附着没有影响。此外，MAB LM609抑制内皮细胞附着在含有arg-gly-Asp序列的固定合成肽上。这种粘附受体在结构上与在血小板上表达的IIB/IIIA糖蛋白络合物结构相似，但在抗原上是抗原截然不同的，因为MAB LM609无法识别IIB/IIIA糖蛋白。该受体在内皮细胞上的簇中在簇上组织von Willebrand因子，玻璃体蛋白或含Arg-Gly-App的七肽。本报告中提供的数据表明，Arg-Gly-Asp识别可能在与血管增殖相关的生物学事件中起重要作用。
Human umbilical vein endothelial cells express a heterodimeric adhesion receptor complex consisting of noncovalently associated .alpha. and .beta. subunits that under reducing conditions have molecular masses of 135 kDa and 115 kDa, respectively. This complex can be isolated in pure form from an affinity matrix consisting of an Arg-Asp-containing hepatapeptide and is specifically immunoprecipitated with monoclonal antibodies (mAbs) directed against the vitronectin receptor of human melanoma cells. These data suggest that this complex is one member of a large family of cell adhesion receptors. One of the mAbs, LM609, inhibits the attachment of human endothelial cells to fibrinogen, von Willebrand factor, and vitronectin yet has no effect on the attachment of these cells to fibronectin, collagen, or laminin. In addition, mAb LM609 inhibits attachment of endothelial cells to an immobilized synthetic peptide containing the Arg-Gly-Asp sequence. This adhesion receptor appears structurally similar to the IIb/IIIa glycoprotein complex expressed on platelets yet is antigenically distinct, since mAb LM609 fails to recognize IIb/IIIa glycoproteins. This receptor organizes in clusters on endothelial cells during their attachment to von Willebrand factor, vitronectin, or the Arg-Gly-Asp-containing heptapeptide. The data presented in this report suggest that Arg-Gly-Asp recognition may play a significant role in biological events associated with vascular proliferation.