MATRIX METALLOPROTEINASES (MMP) - STRUCTU RE AND ACTIVITY

Citation
A. Cuvelier et al., MATRIX METALLOPROTEINASES (MMP) - STRUCTU RE AND ACTIVITY, Revue des maladies respiratoires, 14(1), 1997, pp. 1-10
Citations number
42
Categorie Soggetti
Respiratory System
ISSN journal
07618425
Volume
14
Issue
1
Year of publication
1997
Pages
1 - 10
Database
ISI
SICI code
0761-8425(1997)14:1<1:MM(-SR>2.0.ZU;2-W
Abstract
The matrix metalloproteinases (MMP) are a multigenic family involving 14 enzymes which can cleave most, if not all, the components of the ex tracellular matrix (interstitium and basement membranes). The present work reports on the main structural characteristics, the substrate pre ference and the site synthesis of these proteinases and their inhibito rs (TIMP). Human MMPs are produced by various cell types and are invol ved in the remodelling of the extracellular matrix in many physiologic al and pathophysiological circumstances. Elastolytic MMPs produced by monocytes and/or macrophages (matrilysin, gelatinases, macrophage elas tase) are likely to be implicated in the development of acquired pulmo nary emphysema.