期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
卷 1812, 期 12, 页码 1616-1629出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbadis.2011.08.009
关键词
Aggrecan; Brevican; Versican; SLRP; Neoepitope
资金
- University of Melbourne
- Murdoch Children's Research Institute
- Victorian Government
- University of Sydney
- New South Wales Office of Science and Medical Research through the Kolling Institute of Medical Research and Arthritis Australia
- National Health and Medical Research Council Australia (NHMRC) [352562]
- NHMRC
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据