New Perspectives in Cell Adhesion: RGD and Integrins

IF 44.7 1区综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES

Science Pub Date : 1987-10-23 DOI:10.1126/science.2821619

Erkki Ruoslahti, Michael D. Pierschbacher

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引用次数: 4537

Abstract

Rapid progress has been made in the understanding of the molecular interactions that result in cell adhesion. Many adhesive proteins present in extracellular matrices and in the blood contain the tripeptide arginine-glycine-aspartic acid (RGD) as their cell recognition site. These proteins include fibronectin, vitronectin, osteopontin, collagens, thrombospondin, fibrinogen, and von Willebrand factor. The RGD sequences of each of the adhesive proteins are recognized by at least one member of a family of structurally related receptors, integrins, which are heterodimeric proteins with two membrane-spanning subunits. Some of these receptors bind to the RGD sequence of a single adhesion protein only, whereas others recognize groups of them. The conformation of the RGD sequence in the individual proteins may be critical to this recognition specificity. On the cytoplasmic side of the plasma membrane, the receptors connect the extracellular matrix to the cytoskeleton. More than ten proved or suspected RGD-containing adhesion-promoting proteins have already been identified, and the integrin family includes at least as many receptors recognizing these proteins. Together, the adhesion proteins and their receptors constitute a versatile recognition system providing cells with anchorage, traction for migration, and signals for polarity, position, differentiation, and possibly growth.

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细胞粘附的新视角：RGD 和整合素

人们对导致细胞粘附的分子相互作用的认识取得了快速进展。细胞外基质和血液中的许多粘附蛋白都含有精氨酸-甘氨酸-天冬氨酸（RGD）三肽作为细胞识别位点。这些蛋白质包括纤维粘连蛋白、玻璃粘连蛋白、骨粘连蛋白、胶原、血栓软骨素、纤维蛋白原和冯-维勒布兰德因子。每种粘附蛋白的 RGD 序列都能被结构相关的受体整合素家族中的至少一种成员识别，整合素是具有两个跨膜亚基的异源二聚体蛋白。其中一些受体只与单个粘附蛋白的 RGD 序列结合，而另一些则能识别粘附蛋白群。单个蛋白质中 RGD 序列的构象可能是这种识别特异性的关键。在质膜的细胞质一侧，受体将细胞外基质与细胞骨架连接起来。目前已发现十多种证明或怀疑含有 RGD 的粘附促进蛋白，整合素家族中至少有同样多的受体可识别这些蛋白。粘附蛋白及其受体共同构成了一个多功能识别系统，为细胞提供锚定、迁移牵引以及极性、位置、分化和可能的生长信号。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Science 综合性期刊-综合性期刊

CiteScore

61.10

自引率

0.90%

发文量

审稿时长

2.1 months

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