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Integrins.

机译：整联蛋白。

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摘要

Integrins are cell adhesion receptors that are evolutionary old and that play important roles during developmental and pathological processes. The integrin family is composed of 24 alphabeta heterodimeric members that mediate the attachment of cells to the extracellular matrix (ECM) but that also take part in specialized cell-cell interactions. Only a subset of integrins (8 out of 24) recognizes the RGD sequence in the native ligands. In some ECM molecules, such as collagen and certain laminin isoforms, the RGD sequences are exposed upon denaturation or proteolytic cleavage, allowing cells to bind these ligands by using RGD-binding receptors. Proteolytic cleavage of ECM proteins might also generate fragments with novel biological activity such as endostatin, tumstatin, and endorepellin. Nine integrin chains contain an alphaI domain, including the collagen-binding integrins alpha1beta1, alpha2beta1, alpha10beta1, and alpha11beta1. The collagen-binding integrins recognize the triple-helical GFOGER sequence in the major collagens, but their ability to recognize these sequences in vivo is dependent on the fibrillar status and accessibility of the interactive domains in the fibrillar collagens. The current review summarizes some basic facts about the integrin family including a historical perspective, their structure, and their ligand-binding properties.
机译：整联蛋白是细胞粘附受体，其在进化上是古老的，并且在发育和病理过程中起重要作用。整联蛋白家族由24个字母a异二聚体成员组成，其介导细胞与细胞外基质（ECM）的附着，但也参与专门的细胞-细胞相互作用。整联蛋白中只有一个子集（24个中的8个）识别天然配体中的RGD序列。在某些ECM分子（例如胶原蛋白和某些层粘连蛋白同工型）中，RGD序列在变性或蛋白水解切割后暴露，从而使细胞可以通过使用RGD结合受体结合这些配体。 ECM蛋白的蛋白水解切割也可能产生具有新的生物学活性的片段，例如内皮抑素，肿瘤抑素和内驱素。九个整联蛋白链包含一个alphaI域，包括胶原结合整联蛋白alpha1beta1，alpha2beta1，alpha10beta1和alpha11beta1。胶原结合整联蛋白可识别主要胶原中的三螺旋GFOGER序列，但它们在体内识别这些序列的能力取决于原纤维状态和原纤维胶原中相互作用域的可及性。本篇综述总结了有关整联蛋白家族的一些基本事实，包括历史观点，结构及其配体结合特性。

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