Evrosimovska, Biljana and Velickovski, Boris and Dimova, Cena and Veleska-Stefkovska, Daniela (2011) Matrix metalloproteinases (with accent to collagenases). Journal of Cell and Animal Biology, 5 (7). pp. 113-120. ISSN 1996-0867
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Abstract
Matrix metalloproteinases (MMPs) are a major group of enzymes that regulate cell–matrix composition.
The MMPs are zinc-dependent endopeptidases known for their ability to cleave one or several
extracellular matrix (ECM) constituents, as well as nonmatrix proteins. This review focuses on structural
and functional elements of MMPs, and their roles in physiological and pathological processes, in which
it is believed the MMPs play an important, or even indispensable role. According to their structural and
functional characteristics, MMP family members have been classified into six different but closely
related subgroups with fairly characteristic but often overlapping substrate specificities. MMP
synthesis and functions are regulated by transcriptional activation, post-transcriptional processing
(release of pro-domain, cell surface shedding), and control of activity by a family of endogenous
inhibitors collectively known as tissue inhibitors of metalloproteinases (TIMPs). The balance of MMPs
to TIMPs therefore determines matrix turnover, where either an excess of MMPs or a deficit of TIMPs
may result in excess ECM degradation. Moreover, the recent development of selective and nonselective
inhibitors of MMPs would also provide new insights in the knowledge of the relationship
between activation of inflammatory cells and tissue remodeling and propose new therapeutic
possibilities to the treatment of inflammatory disease.
Key words: Extracellular matrix, matrix metalloproteinases, inflammation.
Item Type: | Article |
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Subjects: | Medical and Health Sciences > Basic medicine Medical and Health Sciences > Clinical medicine Medical and Health Sciences > Other medical sciences |
Divisions: | Faculty of Medical Science |
Depositing User: | Cena Dimova |
Date Deposited: | 26 Nov 2012 08:26 |
Last Modified: | 30 Sep 2013 10:58 |
URI: | https://eprints.ugd.edu.mk/id/eprint/2012 |
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