COMPARISON OF CDNA-DERIVED PROTEIN SEQUENCES OF THE HUMAN FIBRONECTIN AND VITRONECTIN RECEPTOR ALPHA-SUBUNITS AND PLATELET GLYCOPROTEIN-IIB
COMPARISON OF CDNA-DERIVED PROTEIN SEQUENCES OF THE HUMAN FIBRONECTIN AND VITRONECTIN RECEPTOR ALPHA-SUBUNITS AND PLATELET GLYCOPROTEIN-IIB
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DOI：
10.1021/bi00399a021
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发表时间：
1987-12-15
期刊：
影响因子：
2.9
通讯作者：
PHILLIPS, DR
中科院分区：
文献类型：
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作者：
FITZGERALD, LA;PONCZ, M;PHILLIPS, DR
纤连蛋白受体（FnR）、玻连蛋白受体（VnR）和血小板膜糖蛋白（GP）IIb-IIIa复合物是细胞粘附受体家族的成员，其由非共价结合的α-和β-亚单位。本研究设计为比较α-Lactobacillus的cDNA衍生的蛋白质序列。人FnR、VnR和血小板GP IIb亚基。α-β-CD的cDNA克隆FnR的亚基（FnR α）从人脐静脉内皮（HUVE）细胞库中获得，通过使用由血小板GP IIb的肽序列设计的寡核苷酸探针。用抗体从人红白血病细胞cDNA表达文库中分离血小板GP Ⅱ b的cDNA克隆。VnR α的cDNA克隆-亚基（VnR α）通过使用来自VnR α的部分cDNA序列的寡核苷酸探针从HUVE细胞库获得。这些序列的翻译显示FNR α，VnR α，和GP IIb由二硫键连接的大链（858-871个氨基酸）和小链（137-158个氨基酸）组成，所述大链和小链由单个mRNA后加工而成。位于每个小链的羧基末端附近的单个疏水片段似乎是跨膜结构域。大链似乎完全是细胞外的，每个包含4个重复的推定的Ca 2+结合结构域的约30个氨基酸，具有序列相似性的其他Ca 2+结合蛋白。这三种受体α-β的蛋白质序列之间的同一性亚基的同源性为36.1%~ 44.5%，其中Ca ~（2+）结合结构域的同源性最高。这些蛋白质显然是通过基因复制过程进化而来的。
The fibronectin receptor (FnR), the vitronectin receptor (VnR), and the platelet membrane glycoprotein (GP) IIb-IIIa complex are members of a family of cell adhesion receptors, which consist of noncovalently associated .alpha.- and .beta.-subunits. The present study was designed to compare the cDNA-derived protein sequences of the .alpha.-subunits of human FnR, VnR, and platelet GP IIb. cDNA clones for the .alpha.-subunit of the FnR (FnR.alpha.) were obtained from a human umbilical vein endothelial (HUVE) cell library by using an oligonucleotide probe designed from a peptide sequence of platelet GP IIb. cDNA clones for platelet GP IIb were isolated from a cDNA expression library of human erythroleukemia cells by using antibodies. cDNA clones of the VnR .alpha.-subunit (VnR.alpha.) were obtained from the HUVE cell library by using an oligonucleotide probe from the partial cDNA sequence for the VnR.alpha.. Translation of these sequences showed that the FNR.alpha., the VnR.alpha., and GP IIb are composed of disulfide-linked large (858-871 amino acids) and small (137-158 amino acids) chains that are posttranslationally processed from a single mRNA. A single hydrophobic segment located near the carboxyl terminus of each small chain appears to be a transmembrane domain. The large chains appear to be entirely extracellular, and each contains four repeated putative Ca2+-binding domains of about 30 amino acids that have sequence similarities to other Ca2+-binding proteins. The identity among the protein sequences of the three receptor .alpha.-subunits ranges from 36.1% to 44.5%, with the Ca2+-binding domains having the greatest homology. These proteins apparently evolved by a process of gene duplication.