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Matrix metalloproteinases in inflammation

Authors :
Veli-Matti Kähäri
Liisa Nissinen
Source :
Biochimica et biophysica acta. 1840(8)
Publication Year :
2013

Abstract

Background Matrix metalloproteinases (MMPs) are a family of ubiquitously expressed zinc-dependent endopeptidases with broad substrate specificity and strictly regulated tissue specific expression. They are expressed in physiological situations and pathological conditions involving inflammation. MMPs regulate several functions related to inflammation including bioavailability and activity of inflammatory cytokines and chemokines. There is also evidence that MMPs regulate inflammation in tumor microenvironment, which plays an important role in cancer progression. Scope of review Here, we discuss the current view on the role of MMPs in the regulation of inflammation. Major conclusions MMPs modulate inflammation by regulating bioavailability and activity of cytokines, chemokines, and growth factors, as well as integrity of physical tissue barriers. MMPs are also involved in immune evasion of tumor cells and in regulation of inflammation in tumor microenvironment. General significance There is increasing evidence for non-matrix substrates of MMPs that are related to regulation of inflammatory processes. New methods have been employed for identification of the substrates of MMPs in inflammatory processes in vivo. Detailed information on the substrates of MMPs may offer more specific and effective ways of inhibiting MMP function by blocking the cleavage site in substrate or by inhibition of the bioactivity of the substrate. It is expected, that more precise information on the MMP–substrate interaction may offer novel strategies for therapeutic intervention in inflammatory diseases and cancer without blocking beneficial actions of MMPs. This article is part of a Special Issue entitled Matrix-mediated cell behaviour and properties.

Details

ISSN :
00063002
Volume :
1840
Issue :
8
Database :
OpenAIRE
Journal :
Biochimica et biophysica acta
Accession number :
edsair.doi.dedup.....a34bcb2370c1997feb6917376c3358a5