Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1.
Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1.
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DOI：
10.1083/jcb.130.3.503
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发表时间：
1995-08
影响因子：
7.8
通讯作者：
BORNSTEIN, P
中科院分区：
文献类型：
--
作者：
BORNSTEIN, P
对hrombospondin 1（TSP 1）1参与多种生物过程的R电流评价（图1; 1，3，25）远远超出了最初归因于血小板聚集和凝血中蛋白质的作用。这种功能的多样性导致了文献中的相当大的混乱和科学家们的怀疑，即单一蛋白质可以支持这种多变的，有时是相互冲突的功能。在这篇评论中，我将试图表明，基质细胞蛋白的能力，如下文所定义的，与广泛的基质蛋白和细胞表面受体相互作用，可以解释TSP 1的复杂的生物学功能，并解决许多关于其作用方式的争议。这一分析的结论是，即使在实验和解释中出现一些错误，TSP 1的大多数功能报告，分歧，因为他们似乎是，很可能是正确的。在本分析中使用的术语”基质细胞”是指一组模块化的胞外蛋白，其功能通过结合基质蛋白以及细胞表面受体或其他分子如细胞因子和蛋白酶来实现，所述其他分子又与细胞表面相互作用。除了TSP 1之外，该组可能包括腱蛋白家族的成员、骨桥蛋白/骨连接素及其亲属和骨桥蛋白。虽然基质细胞蛋白质可以与结构元件如胶原纤维或基底膜相关联，但推测它们对这些元件的结构完整性没有贡献。然而，结合可以起到隔离基质细胞蛋白质的作用，并为随后募集到细胞表面提供蛋白质的来源。应该注意的是，结构基质和基质细胞蛋白之间的区别是不完全的，因为蛋白质如纤连蛋白和层粘连蛋白，它们确实作为结构元件的组成部分，也具有粘附功能，并发挥与基质细胞蛋白部分重叠的生物学作用。此外，在某些情况下，基质细胞蛋白可能参与结构复合物的形成。
R current appreciation of the involvement of hrombospondin 1 (TSP1) 1 in diverse biological processes (Fig. 1; 1, 3, 25) extends far beyond the role initially attributed to the protein in platelet aggregation and coagulation. This diversity of function has led to considerable confusion in the literature and skepticism among scientists that a single protein can subserve such protean, sometimes conflicting, functions. In this Commentary I will attempt to show that the ability of matricellular proteins, as defined below, to interact with a wide range of both matrix proteins and cell surface receptors can explain the complex biological functions of TSP1 and resolve many of the controversies regarding its mode of action. A conclusion of this analysis is that, even if allowances are made for some errors in experimentation and interpretation, the majority of the reported functions of TSP1, divergent as they appear to be, are likely to be correct. The term" matricellular" is used in this analysis to refer to a group of modular, extracellular proteins whose functions are achieved by binding to matrix proteins as well as to cell surface receptors, or to other molecules such as cytokines and proteases that interact, in turn, with the cell surface. In addition to TSP1, this group is likely to include members of the tenascin protein family, SPARC/osteonectin and its relatives, and osteopontin. Although matricellular proteins can be associated with structural elements such as collagen fibrils or basement membranes, it is presumed that they do not contribute to the structural integrity of these elements. An association could, nevertheless, serve to sequester matricellular proteins, and provide a source of the proteins for subsequent recruitment to the cell surface. It should be noted that the distinction between structural matrix and matricellular proteins is not complete, since proteins such as fibronectin and laminin, which do serve as integral components of structural elements, also have adhesive functions and play biological roles that partially overlap those of matricellular proteins. Furthermore, matricellular proteins may participate in the formation of structural complexes under some circum-
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影响因子：
4.1
作者：
PELLERIN, S;LAFEUILLADE, B;FEIGE, JJ
通讯作者：
FEIGE, JJ
影响因子：
2.5
作者：
IRUELAARISPE, ML;LISKA, DJ;BORNSTEIN, P
通讯作者：
BORNSTEIN, P
影响因子：
9.2
作者：
ADAMS, J;LAWLER, J
通讯作者：
LAWLER, J
影响因子：
2.5
作者：
CORLESS, CL;MENDOZA, A;LAWLER, J
通讯作者：
LAWLER, J
二硫化物调节血小板反应蛋白的 RGD 抑制细胞粘附活性。
影响因子：
7.8
作者：
Sun, X;Skorstengaard, K;Mosher, D F
通讯作者：
Mosher, D F