New Perspectives in Cell Adhesion: RGD and Integrins

整合素 纤维连接蛋白 细胞粘附 细胞生物学 RGD基序 化学 受体 细胞粘附分子 维生素连接蛋白 细胞外基质 生物 细胞 生物化学
作者
Erkki Ruoslahti,Michael D. Pierschbacher
出处
期刊:Science [American Association for the Advancement of Science (AAAS)]
卷期号:238 (4826): 491-497 被引量:4814
标识
DOI:10.1126/science.2821619
摘要

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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