Proteoglycan degradation by the ADAMTS family of proteinases

被引：159

作者：

Stanton, Heather ^{[1
,2
]}

Melrose, James ^{[3
]}

Little, Christopher B. ^{[3
]}

Fosang, Amanda J. ^{[1
,2
]}

机构：

[1] Univ Melbourne, Dept Paediat, Parkville, Vic 3052, Australia

[2] Royal Childrens Hosp, Murdoch Childrens Res Inst, Parkville, Vic 3052, Australia

[3] Univ Sydney, Royal N Shore Hosp, Raymond Purves Bone & Joint Res Labs, Kolling Inst Med Res,Inst Bone & Joint Res, St Leonards, NSW 2065, Australia

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE | 2011年 / 1812卷 / 12期

基金：

澳大利亚国家健康与医学研究理事会; 英国医学研究理事会;

关键词：

Aggrecan; Brevican; Versican; SLRP; Neoepitope; HUMAN ARTICULAR-CARTILAGE; CHONDROITIN SULFATE PROTEOGLYCAN; SMOOTH-MUSCLE-CELLS; TRANSLUMINAL CORONARY ANGIOPLASTY; MATRIX-METALLOPROTEINASE CLEAVAGE; LEUCINE-RICH PROTEOGLYCANS; HYALURONAN-BINDING REGION; LINKED KERATAN SULFATE; EXTRACELLULAR-MATRIX; PROTEOLYTIC CLEAVAGE;

D O I：

10.1016/j.bbadis.2011.08.009

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：

Proteoglycans are key components of extracellular matrices, providing structural support as well as influencing cellular behaviour in physiological and pathological processes. The diversity of proteoglycan function reported in the literature is equally matched by diversity in proteoglycan structure. Members of the ADAMTS (A Disintegrin And Metalloproteinase with ThromboSpondin motifs) family of enzymes degrade proteoglycans and thereby have the potential to alter tissue architecture and regulate cellular function. In this review, we focus on ADAMTS enzymes that degrade the lectican and small leucine-rich repeat families of proteoglycans. We discuss the known ADAMTS cleavage sites and the consequences of cleavage at these sites. We illustrate our discussion with examples from the literature in which ADAMTS proteolysis of proteoglycans makes profound changes to tissue function. (C) 2011 Elsevier B.V. All rights reserved.

引用

页码：1616 / 1629

页数：14

共 187 条

[1] Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family [J].