Role of Urokinase Receptor and Caveolin in Regulation of Integrin Signaling

作者：Ying Wei, Daniel I. Simon, David A. Waltz, Harold A. Chapman · 发表于：Thrombosis and Haemostasis · 年份：1999 · DOI：10.1055/s-0037-1615845 · 被引用次数：143 · 研究领域：Cell Adhesion Molecules Research、Caveolin-1 and cellular processes、Cellular transport and secretion

Introduction: Integrin-Associated Proteins Integrins are a group of heterodimeric adhesion receptors that mediate attachment of cells to extracellular matrices and other cells. These receptors serve as a major site of information flow from the immediate pericellular environment to the cellular interior and, in reverse, as effectors of the cellular responses to such information in biological processes as diverse as inflammation, tissue remodeling, growth, and tumorigenesis.1-3 The binding specificities of integrin receptors are determined by interactions of ligands with both the α and β chains that comprise integrins. Diversity of ligand binding is promoted by the fact that a single α chain may partner with numerous distinct β chains, and cells may express more than one and, sometimes, many α and β chains. Thus, as a family, integrins have the capacity to interact with a large set of cellular and extracellular matrix ligands. The structural features of integrin heterodimers that underlie their interactive potential and ligand specificity have been the subject of several recent reviews and will not be discussed here.4,5 A fundamental feature of integrins is that their function is determined not simply by their expression on the cell surface but by their dynamic regulation through activating events that amplify, sometimes only transiently, the adhesive capacity of integrins for their counter-ligands and the signals that follow.1-3,6,7 These dynamic aspects of integrin function a...