The ADAMTS metalloproteinases
Open accessAbstract
The ADAMTSs (a disintegrin 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.
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ADAMTS proteases cleave several PNN CSPGs, including aggrecan, brevican, neurocan, versican, and phosphacan.
“For instance, ADAMTSs are known to cleave multiple PNN components including the CSPGs aggrecan, brevican, neurocan, versican, and phosphacan (Fig. 2) (Porter et al., 2005; Tauchi et al., 2012).”
From Losing the sugar coating: Potential impact of perineuronal net abnormalities on interneurons in schizophrenia (2015) · cites this paper as Porter et al., 2005
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Extracellular Matrix Assembly: A Multiscale Deconstruction
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- Authors
- PORTER, S., CLARK, I. M., KEVORKIAN, L., & EDWARDS, D. R.
- Affiliations
- University of East Anglia (GB)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2005-02-08
- Volume
- 386
- Issue
- 1
- Pages
- 15-27
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1134762
- OpenAlex
- W2030246164
- Cited by
- 779
- References
- 126
- Citations by year
- 2026: 7 · 2025: 18 · 2024: 10 · 2023: 27 · 2022: 22 · 2021: 26 · 2020: 43 · 2019: 32 · 2018: 27 · 2017: 33 · 2016: 39 · 2015: 49 · 2014: 36 · 2013: 37 · 2012: 44
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UEA Digital Repository (University of East Anglia) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- collagen processing, aggrecan cleavage, versican, brevican, proteoglycan degradation, angiogenesis inhibition, von Willebrand factor cleavage, coagulation, organogenesis, inflammation, fertility, arthritis, cancer
- MeSH terms
- Animals, Cloning, Molecular, Forecasting, Multigene Family, Humans, Metalloendopeptidases, Neoplasm Proteins, Terminology as Topic, Protease Inhibitors, Substrate Specificity, Gene Expression Regulation, Enzymologic, Extracellular Matrix Proteins, Protein Structure, Tertiary, Angiogenesis Inhibitors, Rats
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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