Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases.
Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases.
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通过构象变化和基质金属蛋白酶的有限蛋白水解，从静止纤连蛋白中释放生物活性。
作者：
F. Fukai;M. Ohtaki;N. Fujii;H. Yajima;T. Ishii;Y. Nishizawa;K. Miyazaki;T. Katayama
We reported that specific biological activities are confined to three domains of the fibronectin (Fn) molecule [Fukai et al. (1991) J. Biol. Chem. 266, 8807; Fukai et al. (1993) Biochemistry 32, 5746]: the potent ability to stimulate the adipocyte differentiation of ST-13 cells is in the amino-terminal fibrin-binding (Fib 1) domain (referred to as Fib 1 domain activity); the RGD-dependent activities that stimulate NIH-L13 cell migration and inhibit adipocyte differentiation are in the central cell-binding (Cell) domain (Cell domain activity); and the activity that stimulates cell migration in a RGD-independent manner is in the carboxyl-terminal fibrin-binding (Fib 2) domain (Fib 2 domain activity). Human plasma Fn which was purified without exposure to a denaturant, such as urea, exhibited no Fib 1, Fib 2, or Cell domain activity. By exposure to urea or surface adsorption, Fn showed Cell domain activity but not those of the Fib 1 and Fib 2 domains. Whether the cryptic domain activities are disclosed or not depended on whether or not the responsible domains were irreversibly exposed from confined environments of Fn structure as confirmed by light-scattering measurement and enzyme immunoassay using domain-specific monoclonal antibodies. We then investigated the action of matrix metalloproteinases (MMPs) in liberating the Fib 1, Cell, and Fib 2 domain activities. Matrilysin released only the Cell domain activity. In contrast, stromelysin, collagenase, and especially gelatinase A additionally liberated the Fib 1 and Fib 2 domain activities. The Fib 1, Fib 2, and Cell domains acquired much higher activities when they were freed from linkage with adjacent domains.(ABSTRACT TRUNCATED AT 250 WORDS)
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从正常成纤维细胞和转化成纤维细胞的血浆和培养上清液中分离的人纤连蛋白之间的结构域差异。
DOI：
--
发表时间：
1985
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Sekiguchi,K;Siri,A;Zardi,L;Hakomori,S
通讯作者：
Hakomori,S
纤连蛋白片段引起培养物中牛关节软骨切片的软骨溶解。
DOI：
--
发表时间：
1992
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Homandberg,GA;Meyers,R;Xie,DL
通讯作者：
Xie,DL
血浆纤连蛋白和纤连蛋白片段的近紫外圆二色光谱。
DOI：
10.1016/0006-291x(82)92111-8
发表时间：
1982
影响因子：
3.1
作者：
Tooney,NM;Amrani,DL;Homandberg,GA;McDonald,JA;Mosesson,MW
通讯作者：
Mosesson,MW
DOI：
10.1016/s0021-9258(17)43896-8
发表时间：
1983-12
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
H. Erickson;N. Carrell
通讯作者：
H. Erickson;N. Carrell
纤连蛋白的细胞粘附结构域和氨基末端基质组装结构域参与其组装成成纤维细胞细胞周基质。
DOI：
--
发表时间：
1987
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
McDonald,JA;Quade,BJ;Broekelmann,TJ;LaChance,R;Forsman,K;Hasegawa,E;Akiyama,S
通讯作者：
Akiyama,S