MMP-1: the elder of the family

被引:212
作者
Pardo, A
Selman, M
机构
[1] Univ Nacl Autonoma Mexico, Fac Ciencias, Mexico City 04000, DF, Mexico
[2] Inst Nacl Enfermedades Resp, Mexico City 04000, DF, Mexico
关键词
fibrosis; collagenase; matrix metalloproteinases; cancer;
D O I
10.1016/j.biocel.2004.06.017
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The matrix metalloproteinases (MMPs) area family of zinc-containing endopeptidases that play a key role in both physiological and pathological tissue remodeling. Human fibroblast collagenase (MMP-1) was the first vertebrate collagenase purified as a protein and cloned as a cDNA, and is considered the prototype for all the interstitial collagenases. It is synthesized as a zymogen where N-terminal residues are removed by proteolysis and shares with other MMPs a catalytic domain and a carboxy terminal domain with sequence similarity to hemopexin. Importantly, MMP-1 should be considered a multifunctional molecule since it participates not only in the turnover of collagen fibrils in the extracellular space but also in the cleavage of a number of non-matrix substrates and cell surface molecules suggesting a role in the regulation of cellular behaviour. Furthermore, an extensive body of evidence indicates that MMP-1 plays an important role in diverse physiologic processes such as development, tissue morphogenesis, and wound repair. Likewise, it seems to be implicated in a variety of human diseases including cancer, rheumatoid arthritis, pulmonary emphysema and fibrotic disorders, suggesting that its inhibition or stimulation may open therapeutic avenues. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:283 / 288
页数:6
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