CDNA CLONING AND COMPLETE PRIMARY STRUCTURE OF THE ALPHA-SUBUNIT OF A LEUKOCYTE ADHESION GLYCOPROTEIN, P150,95
CDNA CLONING AND COMPLETE PRIMARY STRUCTURE OF THE ALPHA-SUBUNIT OF A LEUKOCYTE ADHESION GLYCOPROTEIN, P150,95
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DOI：
10.1002/j.1460-2075.1987.tb02746.x
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发表时间：
1987-12-01
期刊：
影响因子：
11.4
通讯作者：
SPRINGER, TA
中科院分区：
文献类型：
--
作者：
CORBI, AL;MILLER, LJ;SPRINGER, TA
白细胞粘附受体p150、p95、Mac-1和LFA-1是含有不同α的完整膜糖蛋白。18万到15万Mr的亚基与相同的β相关。95000 Mr的亚单位，在…复合物，p150,95。利用亚基色氨酸肽指定寡核苷酸探针，从大小选择的骨髓细胞cDNA文库中分离出包含完整编码序列的4.7 kb cDNA克隆。这个4.7 kb的cDNA克隆编码一个信号序列、一个由1081个氨基酸组成的胞外结构域（含10个潜在糖基化位点）、一个由26个氨基酸组成的跨膜结构域和一个由29个残基组成的胞质c端尾部。胞外结构域包含。apprx的三个串联同源重复序列。60个氨基酸与假定的二价阳离子结合位点和4个弱重复序列缺乏这种结合位点。该cDNA克隆与髓系体外分化过程中诱导的4.7 kb mRNA杂交。p150 95。亚基与。α同源。识别细胞外基质成分中RGD序列的受体亚基，如先前在。β。亚单位，支持参与细胞-细胞和细胞-基质相互作用的受体属于称为整合素的单一基因超家族的概念。p150,95 .alpha的独特特点。亚基包括126个残基n端插入到假定的金属结合区域，以及在加工过程中基质受体被蛋白水解切割的区域的缺失。
The leukocyte adhesion receptors, p150,95, Mac-1 and LFA-1 are integral membrane glycoproteins which contain distinct .alpha. subunits of 180,000-150,000 Mr associated with identical .beta. subunits of 95,000 Mr in .alpha..beta. complexes, p150,95 .alpha. subunit tryptic peptides were used to specify oligonucleotide probes and a cDNA clone of 4.7 kb containing the entire coding sequence was isolated from a size-selected myeloid cell cDNA library. The 4.7-kb cDNA clone encodes a signal sequence, an extracellular domain of 1081 amino acids containing 10 potential glycosylation sites, a transmembrane domain of 26 amino acids, and a C-terminal cytoplasmic tail of 29 residues. The extracellular domain contains three tandem homologous repeats of .apprx. 60 amino acids with putative divalent cationbinding sites, and four weaker repeats which lack such binding sites. The cDNA clone hybridizes with a mRNA of 4.7 kb which is induced during in vitro differentiation of myeloid cell lines. The p150,95 .alpha. subunit is homologous to the .alpha. subunits of receptors which recognize the RGD sequence in extracellular matrix components, as has previously been shown for the .beta. subunits, supporting the concept that receptors involved in both cell-cell and cell-matrix interactions belong to a single gene superfamily termed the integrins. Distinctive features of the p150,95 .alpha. subunit include an insertion of 126 residues N-terminal to the putative metal binding region and a deletion of the region in which the matrix receptors are proteolytically cleaved during processing.