Assembly of fibronectin fibrils occurs at the surface of substrate-attached cells and is mediated by the first to the fifth type I modules in the N-terminal 70 kDa portion of the molecule. The first type III module (III1) of fibronectin, not present in the 70 kDa portion, contains a conformation-dependent binding site for the 70 kDa N-terminal region of fibronectin, suggesting that the III1 module on cell-surface fibronectin may serve as a binding site for fibronectin's N-terminus on substrate-attached cells. To explore this possiblility, we compared the ability of mutant recombinant 70 kDa proteins containing deletions of one or several of the first five type I modules to bind to fibroblasts and to III1. Proteins containing the fourth and fiftBiomolecular Chemistry and Medicine, University of Wisconsin, Madison, WI 53706U.S.A. Assembly of fibronectin fibrils occurs at the surface of substrate-attached cells and is mediated by the first to the fifth type I modules in the N-terminal 70 kDa portion of the molecule. The first type III module (III1) of fibronectin, not present in the 70 kDa portion, contains a conh as 70 kDa deletion mutants lacking I4 and I5 also bound to the cell surface, and deletion mutants lacking I1-3 and I4-5 both competed only partially for binding of 125I-labelled fibronectin or 70 kDa protein. These data indicate that the N-terminal part of fibronectin binds to III1 via I4 and I5 and that interactions in addition to that of I4 and I5 with III1 are important for cell-surface-mediated fibronectin polymerization.

译文

纤连蛋白原纤维的组装发生在附着于底物的细胞的表面,并由分子的N末端70 kDa部分中的第一至第五种I型模块介导。纤连蛋白的第一个III型模块 (III1) 不存在于70 kDa部分中,包含纤连蛋白70 kDa N末端区域的构象依赖性结合位点,提示细胞表面纤连蛋白上的III1模块可以用作底物附着细胞上纤连蛋白N末端的结合位点。为了探索这种可能性,我们比较了含有前五个I型模块中一个或几个缺失的突变重组70 kDa蛋白与成纤维细胞和iii1结合的能力。含有第四和第五生物分子化学和医学的蛋白质,威斯康星大学麦迪逊分校,WI 53706u.S.A.纤连蛋白原纤维的组装发生在附着于底物的细胞的表面,并由分子的N末端70 kDa部分中的第一至第五种I型模块介导。纤连蛋白的第一个III型模块 (III1) 不存在于70 kda部分中,包含也与细胞表面结合的缺乏I4和I5的conh as 70 kda缺失突变体,并且缺乏I1-3和I4-5的缺失突变体都仅部分竞争125i标记的纤连蛋白或70 kda蛋白的结合。这些数据表明,纤连蛋白的N端部分通过I4和I5与III1结合,并且除了I4和I5与III1的相互作用外,还对细胞表面介导的纤连蛋白聚合很重要。

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