CLONING OF GMP-140, A GRANULE MEMBRANE-PROTEIN OF PLATELETS AND ENDOTHELIUM - SEQUENCE SIMILARITY TO PROTEINS INVOLVED IN CELL-ADHESION AND INFLAMMATION
CLONING OF GMP-140, A GRANULE MEMBRANE-PROTEIN OF PLATELETS AND ENDOTHELIUM - SEQUENCE SIMILARITY TO PROTEINS INVOLVED IN CELL-ADHESION AND INFLAMMATION
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DOI：
10.1016/0092-8674(89)90636-3
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发表时间：
1989-03-24
期刊：
影响因子：
64.5
通讯作者：
MCEVER, RP
中科院分区：
文献类型：
--
作者：
JOHNSTON, GI;COOK, RG;MCEVER, RP
GMP-140 是一种存在于血小板和内皮细胞分泌颗粒中的整合膜糖蛋白。细胞激活后，它迅速重新分布到质膜上。源自 cDNA 的 GMP-140 一级结构预测其是一种富含半胱氨酸的蛋白质，具有多个结构域，包括“凝集素”区域、“EGF”结构域、与补体结合蛋白相关的 9 个串联共有重复序列、一个跨膜结构域和一个短胞质尾。一些 cDNA 还预测出具有缺失跨膜片段的可溶性蛋白质。 GMP-140 的结构域组织与 ELAM-1 相似，ELAM-1 是一种细胞因子诱导的内皮细胞受体，可结合中性粒细胞。这种相似性表明 GMP-140 属于一个新的诱导型受体家族，在血管细胞上具有相关的结构和功能。
GMP-140 is an integral membrane glycoprotein found in secretory granules of platelets and endothelial cells. After cellular activation, it is rapidly redistributed to the plasma membrane. The cDNA-derived primary structure of GMP-140 predicts a cysteine-rich protein with multiple domains, including a "lectin" region, an "EGF" domain, nine tandem consensus repeats related to those in complement-binding proteins, a transmembrane domain, and a short cytoplasmic tail. Some cDNAs also predict a soluble protein with a deleted transmembrane segment. The domain organization of GMP-140 is similar to that of ELAM-1, a cytokine-inducible endothelial cell receptor that binds neutrophils. This similarity suggests that GMP-140 belongs to a new family of inducible receptors with related structure and function on vascular cells.