CDNA AND AMINO-ACID-SEQUENCES OF THE CELL-ADHESION PROTEIN-RECEPTOR RECOGNIZING VITRONECTIN REVEAL A TRANSMEMBRANE DOMAIN AND HOMOLOGIES WITH OTHER ADHESION PROTEIN RECEPTORS
CDNA AND AMINO-ACID-SEQUENCES OF THE CELL-ADHESION PROTEIN-RECEPTOR RECOGNIZING VITRONECTIN REVEAL A TRANSMEMBRANE DOMAIN AND HOMOLOGIES WITH OTHER ADHESION PROTEIN RECEPTORS
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DOI：
10.1073/pnas.83.22.8614
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发表时间：
1986-11-01
影响因子：
11.1
通讯作者：
RUOSLAHTI, E
中科院分区：
文献类型：
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作者：
SUZUKI, S;ARGRAVES, WS;RUOSLAHTI, E
细胞通过一个细胞表面受体附着在玻璃体连接蛋白底物上，该受体可识别玻璃体连接蛋白中的ag .cntdot. gly .cntdot. asp序列。受体是一种由150 kda . α组成的糖蛋白。和115kda的β。亚基。.alpha。亚基由两个125 kDa和25 kDa的二硫键链组成。分离到cDNA克隆。来自噬菌体的玻璃体连接蛋白受体的亚基。用人成纤维细胞系RNA构建g11表达文库。imr - 90。根据免疫学标准从文库中选择的克隆通过DNA和蛋白质序列的比较来验证其身份。得到了每个。alpha序列的nh2末端序列。亚基链。.alpha.的25kda链的序列。在cDNA克隆中发现亚基，推导出的氨基酸序列建立了25kda链的完整氨基酸序列。该链包含一个跨膜结构域以及一个假定的胞质内区域，该区域长32个氨基酸，主要由极性氨基酸组成。cDNA与蛋白序列的比较表明，该25 kda链是由α α蛋白水解裂解产生的。-亚基前体，其部分序列包含在cDNA克隆中。这些克隆包含1910个碱基对的开放阅读框和一个3”的未翻译序列。RNA印迹杂交在成纤维细胞和上皮细胞的RNA中检测到一个约7千碱基的转录本。cDNA克隆总共覆盖了该RNA的4442个碱基。.alpha。-亚基序列与。α序列具有较强的同源性。纤维连接蛋白受体亚基。此外，125-kDa链的nh2末端蛋白序列与另外两种细胞表面蛋白的nh2末端序列同源，即淋巴细胞功能相关抗原1 （LFA-1）和巨噬细胞抗原1 (Mac-1)，这两种蛋白被认为是白细胞粘附蛋白的受体。这些结果确定了玻璃体粘连蛋白受体的几个结构特征，并表明存在一个细胞粘附蛋白受体超家族。
Cells adhere to vitronectin substrates through a cell surface receptor that recognizes an Arg.cntdot.Gly.cntdot.Asp sequence in vitronectin. The receptor is a glycoprotein composed of a 150-kDa .alpha. and a 115-kDa .beta. subunit. The .alpha. subunit consists of two disulfide-bonded chains of 125 kDa and 25 kDa. cDNA clones were isolated for the .alpha. subunit of the vitronectin receptor from a phage .lambda.g11 expression library made with RNA from a human fibroblast cell line. IMR-90. The identity of the clones that had been selected from the library based on immunological criteria was verified by comparison of DNA and protein sequences. NH2-terminal sequences were obtained for each of the .alpha.-subunit chains. The sequence of the 25-kDa chain of the .alpha. subunit was found in a cDNA clone, and the amino acid sequence deduced from the cDNA establishes the complete amino acid sequence of the 25-kDa chain. The chain contains a membrane-spanning domain as well as a putative intracytoplasmic region that is 32 amino acids long and consists mostly of polar amino acids. Comparison of the cDNA and protein sequences shows that the 25-kDa chain is generated by proteolytic cleavage of an .alpha.-subunit precursor, the partial sequence of which is contained in the cDNA clones. These clones contain 1910 base pairs of open reading frame and a 3'' untranslated sequence. RNA blot hybridization detected one transcript of about 7 kilobases in RNA from fibroblasts and epithelial cells. Together, the cDNA clones cover 4442 bases of this RNA. The .alpha.-subunit sequence showed strong homology with the sequence of the .alpha. subunit of fibronectin receptor. Moreover, the NH2-terminal protein sequence of the 125-kDa chain was homologous with the NH2-terminal sequences of two other cell surface proteins, lymphocyte function-associated antigen 1 (LFA-1) and macrophage antigen 1 (Mac-1), which have been implicated as receptors for adhesion proteins of leukocytes. These results establish several of the structural features in the vitronectin receptor and suggest the existence of a superfamily of receptors for cell adhesion proteins.