THE PRIMARY STRUCTURE OF THE BETA-SUBUNIT OF THE CELL-SURFACE ADHESION GLYCOPROTEINS LFA-1, CR3 AND P150,95 AND ITS RELATIONSHIP TO THE FIBRONECTIN RECEPTOR
THE PRIMARY STRUCTURE OF THE BETA-SUBUNIT OF THE CELL-SURFACE ADHESION GLYCOPROTEINS LFA-1, CR3 AND P150,95 AND ITS RELATIONSHIP TO THE FIBRONECTIN RECEPTOR
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DOI：
10.1002/j.1460-2075.1987.tb04838.x
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发表时间：
1987-04-01
期刊：
影响因子：
11.4
通讯作者：
WONG, AJ
中科院分区：
文献类型：
--
作者：
LAW, SKA;GAGNON, J;WONG, AJ
淋巴细胞功能相关抗原-1 （LFA-1）、补体受体3型（R3）和抗原p150,95是细胞表面糖蛋白。它们是异二聚体复合物，每一个都含有一个独特的。-subunit与一个共同的。beta.-subunit非共价结合。我们提纯了。-亚基从人脾脏中获得有限的肽序列。这似乎是完全处理过的。beta的完整主要结构。从phorbol ester （PMA）刺激的U937 cDNA文库中对克隆进行cDNA测序，得到-亚基。有五个可能的糖基化位点和一个跨膜段。该序列含有高水平的半胱氨酸（7.6%），57个半胱氨酸残基中有24个存在于3个重复单元中，每个重复单元有8个残基。整个初级结构与来自鸡成纤维细胞的纤维连接蛋白的一个亚基有47%的同源性。LFA-1、CR3和p150,95抗原可能属于包括纤维连接蛋白结合蛋白在内的细胞表面分子的一个扩展家族。
The lymphocyte-function-associated antigen-1 (LFA-1), the complement receptor type 3 (R3) and the antigen p150,95 are cell-surfce glycoproteins. They are heterodimeric complexes, each containing a unique .alpha.-subunit noncovalently associated with a common .beta.-subunit. We have purified the .beta.-subunit from human spleen and obtained limited peptide sequences. What appears to be the complete primary structure for the fully processed .beta.-subunit was obtained by cDNA sequencing of clones from a phorbol ester (PMA) stimulated U937 cDNA library. There are five possible glycosylation sites and a transmembrane segment. The sequence contains a high level of cysteine (7.6%), with 24 of the 57 cysteine residues being found in three repeating units each with eight residues. The entire primary structure has 47% identity to a subunit of a fibronectin binding protein from chicken fibroblasts. It seems that LFA-1, CR3 and p150,95 antigens may belong to an extended family of cell surface molecules including the fibronectin binding protein.