The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology

被引：94

作者：

Bekhouche, Mourad ^{[1
]}

Colige, Alain ^{[1
]}

机构：

[1] Univ Liege, Lab Connect Tissues Biol, GIGA Res, B-4000 Sart Tilman Par Liege, Belgium

来源：

MATRIX BIOLOGY | 2015年 / 44-46卷

关键词：

Procollagen N-proteinases; ADAMTS; Fibrillar collagens; EHLERS-DANLOS-SYNDROME; GENE; COLLAGEN; METALLOPROTEINASES; DERMATOSPARAXIS; PROPEPTIDE; CLONING; FAMILY; PURIFICATION; DISINTEGRIN;

D O I：

10.1016/j.matbio.2015.04.001

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：

Collagen fibers are the main components of most of the extracellular matrices where they provide a structural support to cells, tissues and organs. Fibril-forming procollagens are synthetized as individual chains that associate to form homo- or hetero-trimers. They are characterized by the presence of a central triple helical domain flanked by amino and carboxy propeptides. Although there are some exceptions, these two propeptides have to be proteolytically removed to allow the almost spontaneous assembly of the trimers into collagen fibrils and fibers. While the carboxy-propeptide is mainly cleaved by proteinases from the tolloid family, the amino-propeptide is usually processed by procollagen N-proteinases: ADAMTS2, 3 and 14. This review summarizes the current knowledge concerning this subfamily of ADAMTS enzymes and discusses their potential involvement in physiopathological processes that are not directly linked to fibrillar procollagen processing. (C) 2015 Published by Elsevier B.V.

引用

页码：46 / 53

页数：8

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