Human 92 kDa type IV collagenase: functional analysis of fibronectin and carboxyl-end domains.

Human 92 kDa type IV collagenase: functional analysis of fibronectin and carboxyl-end domains.
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人 92 kDa IV 型胶原酶:纤连蛋白和羧基末端结构域的功能分析。

DOI:
10.1038/ki.1993.26
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发表时间:
1993
影响因子:
19.6
通讯作者:
Goldberg,GI
Goldberg,GI
中科院分区:
医学1区
文献类型:
--
作者:
Strongin,AY;Collier,IE;Krasnov,PA;Genrich,LT;Marmer,BL;Goldberg,GI

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人类 92 kDa IV 型胶原酶:纤连蛋白和羧基末端结构域的功能分析。两种密切相关的分泌型金属蛋白酶 72 和 92 kDa IV 型胶原酶(72- 和 92T4C1)由多个结构域组成,但其功能知之甚少。两种金属蛋白酶都可以与明胶结合,并与酶原形式的特定抑制剂形成复合物。酶原-抑制剂复合物形成的生物学作用仍不清楚。在这里,我们总结了结果,证明 92T4C1 的纤连蛋白样结构域介导酶原的明胶结合,而血红素结合蛋白样羧基末端结构域对于酶原与 TIMP 的复合物形成至关重要。与 TIMP 形成的 92T4C1 酶原复合物可防止二聚化、与 ClI 酶原形成新型复合物以及溶基质素对 92T4Cl 的激活。相反,共价 92T4Cl 同二聚体的形成排除了酶原-TIMP 复合物的形成,从而允许这种形式的酶进入激活的蛋白水解级联。 92T4Cl-ClI 复合物的两种成分都可以以类似于游离酶的方式被激活,产生针对明胶和纤维状胶原蛋白均具有活性的复合物。
Human 92 kDa type IV collagenase: Functional analysis of fibronectin and carboxyl-end domains. Two closely related secreted metallopro-teases 72 and 92 kDa type IV collagenases (72- and 92T4C1) consist of several structural domains, the functions of which are poorly understood. Both metalloproteases can bind to gelatin as well as form complexes with specific inhibitors in the proenzyme form. The biologic role of the proenzyme-inhibitor complex formation remained unclear. Here we summarize results demonstrating that the fibronectin-like domain of 92T4C1 mediates gelatin binding of the proenzyme, while the hemopexin like carboxy-terminal domain is essential for the complex formation of the proenzyme with TIMP. The formation of a 92T4C1 proenzyme complex with TIMP prevents dimerization, formation of the novel complex with ClI proenzyme, and activation of the 92T4Cl by stromelysin. Conversely, formation of the covalent 92T4Cl homodimer excludes the formation of a proenzyme-TIMP complex, thus allowing this form of enzyme to enter into the proteolytic cascade of activation. Both components of the 92T4Cl-ClI complex can be activated in a fashion similar to that of free enzymes, yielding a complex active against both gelatin and fibrillar collagen.
细胞外基质金属蛋白酶在肿瘤侵袭和转移中的作用。
DOI: 10.1007/978-1-4615-3940-7_20
发表时间: 1991
影响因子: --
作者:
Goldberg,GI;Eisen,AZ
通讯作者: Eisen,AZ
DOI: 10.1016/s0021-9258(18)42873-6
发表时间: 1992-03
期刊: The Journal of biological chemistry
影响因子: --
作者:
G. Goldberg;A. Strongin;I. Collier;L. T. Genrich;B. Marmer
通讯作者: G. Goldberg;A. Strongin;I. Collier;L. T. Genrich;B. Marmer
人皮肤成纤维细胞溶基质素:结构、糖基化、底物特异性以及正常细胞和致瘤细胞中的差异表达。
DOI: 10.1073/pnas.84.19.6725
发表时间: 1987
影响因子: 11.1
作者:
Wilhelm,SM;Collier,IE;Kronberger,A;Eisen,AZ;Marmer,BL;Grant,GA;Bauer,EA;Goldberg,GI
通讯作者: Goldberg,GI
DOI: --
发表时间: 1986-05
期刊: The Journal of biological chemistry
影响因子: --
作者:
G. Goldberg;S. Wilhelm;A. Kronberger;E. Bauer;G. A. Grant;A. Eisen
通讯作者: G. Goldberg;S. Wilhelm;A. Kronberger;E. Bauer;G. A. Grant;A. Eisen
DOI: 10.1016/s0021-9258(18)45657-8
发表时间: 1987-04
期刊: The Journal of biological chemistry
影响因子: --
作者:
G. A. Grant;A. Eisen;B. Marmer;W. Roswit;G. Goldberg
通讯作者: G. A. Grant;A. Eisen;B. Marmer;W. Roswit;G. Goldberg