The regulation of matrix metalloproteinases and their inhibitors

Clark, Ian M., Swingler, Tracey E., Sampieri, Clara L. and Edwards, Dylan R. (2008) The regulation of matrix metalloproteinases and their inhibitors. International Journal of Biochemistry & Cell Biology, 40 (6-7). pp. 1362-1378. ISSN 1878-5875

[img]
Preview
PDF (Clark_et_al_2008.pdf)
Download (897kB) | Preview

Abstract

The matrix metalloproteinases (MMP) are a family of 23 enzymes in man. These enzymes were originally described as cleaving extracellular matrix (ECM) substrates with a predominant role in ECM homeostasis, but it is now clear that they have much wider functionality. Control over MMP and/or tissue inhibitor of metalloproteinases (TIMP) activity in vivo occurs at different levels and involves factors such as regulation of gene expression, activation of zymogens and inhibition of active enzymes by specific inhibitors. Whilst these enzymes and inhibitors have clear roles in physiological tissue turnover and homeostasis, if control of their expression or activity is lost, they contribute to a number of pathologies including e.g. cancer, arthritis and cardiovascular disease. The expression of many MMPs and TIMPs is regulated at the level of transcription by a variety of growth factors, cytokines and chemokines, though post-transcriptional pathways may contribute to this regulation in specific cases. The contribution of epigenetic modifications has also been uncovered in recent years. The promoter regions of many of these genes have been, at least partly, characterised including the role of identified single nucleotide polymorphisms. This article aims to review current knowledge across these gene families and use a bioinformatic approach to fill the gaps where no functional data are available.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Depositing User: Users 2731 not found.
Date Deposited: 13 May 2011 10:40
Last Modified: 04 Sep 2020 23:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/30531
DOI: 10.1016/j.biocel.2007.12.006

Actions (login required)

View Item View Item