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.