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Yamamoto, Kazuhiro, Murphy, Gillian and Troeberg, Linda 
ORCID: https://orcid.org/0000-0003-0939-4651
(2015)
Extracellular regulation of metalloproteinases.
Matrix Biology, 44-46.
pp. 255-263.
ISSN 0945-053X
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Abstract
Matrix metalloproteinases (MMPs) and adamalysin-like metalloproteinase with thrombospondin motifs (ADAMTSs) belong to the metzincin superfamily of metalloproteinases and they play key roles in extracellular matrix catabolism, activation and inactivation of cytokines, chemokines, growth factors, and other proteinases at the cell surface and within the extracellular matrix. Their activities are tightly regulated in a number of ways, such as transcriptional regulation, proteolytic activation and interaction with tissue inhibitors of metalloproteinases (TIMPs). Here, we highlight recent studies that have illustrated novel mechanisms regulating the extracellular activity of these enzymes. These include allosteric activation of metalloproteinases by molecules that bind outside the active site, modulation of location and activity by interaction with cell surface and extracellular matrix molecules, and endocytic clearance from the extracellular milieu by low-density lipoprotein receptor-related protein 1 (LRP1).
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright © 2015. Published by Elsevier B.V. |
| Uncontrolled Keywords: | chemistry,allosteric regulation,binding sites,enzymology,enzyme activation,gene expression regulation, enzymologic,humans,chemistry |
| Faculty \ School: | Faculty of Medicine and Health Sciences > Norwich Medical School |
| UEA Research Groups: | Faculty of Medicine and Health Sciences > Research Groups > Musculoskeletal Medicine Faculty of Medicine and Health Sciences > Research Centres > Metabolic Health |
| Depositing User: | LivePure Connector |
| Date Deposited: | 08 Jan 2019 12:30 |
| Last Modified: | 19 Oct 2023 02:20 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/69485 |
| DOI: | 10.1016/j.matbio.2015.02.007 |
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