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Porter, Sarah, Clark, Ian M., Kevorkian, Lara and Edwards, Dylan R. 
ORCID: https://orcid.org/0000-0002-3292-2064
(2005)
The ADAMTS metalloproteinases.
Biochemical Journal, 386 (1).
pp. 15-27.
ISSN 1470-8728
Abstract
The ADAMTSs (adisintegrin and metalloproteinase with thrombospondin motifs) are a group of proteases that are found both in mammals and invertebrates. Since the prototype ADAMTS-1 was first described in 1997, there has been a rapidly expanding body of literature describing this gene family and the proteins they encode. The complete human family has 19 ADAMTS genes, together with three members of a newly identified subgroup, the ADAMTSL (ADAMTS-like) proteins, which have several domains in common with the ADAMTSs. The ADAMTSs are extracellular, multidomain enzymes whose known functions include: (i) collagen processing as procollagen N-proteinase; (ii) cleavage of the matrix proteoglycans aggrecan, versican and brevican; (iii) inhibition of angiogenesis; and (iv) blood coagulation homoeostasis as the von Willebrand factor cleaving protease. Roles in organogenesis, inflammation and fertility are also apparent. Recently, some ADAMTS genes have been found to show altered expression in arthritis and various cancers. This review highlights progress in understanding the structural organization and functional roles of the ADAMTSs in normal and pathological conditions.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Medicine and Health Sciences > Research Groups > Nutrition and Preventive Medicine Faculty of Medicine and Health Sciences > Research Groups > Musculoskeletal Medicine Faculty of Medicine and Health Sciences > Research Groups > Cancer Studies |
| Depositing User: | EPrints Services |
| Date Deposited: | 01 Oct 2010 13:36 |
| Last Modified: | 24 Sep 2024 09:59 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/325 |
| DOI: | 10.1042/BJ20040424 |
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