Background | Proteins of the matrix metalloproteinase (MMP) family are
involved in the breakdown of extracellular matrix in normal
physiological processes, such as embryonic development,
reproduction, and tissue remodeling, as well as in disease
processes, such as arthritis and metastasis. Most MMP's are
secreted as inactive proproteins which are activated when cleaved
by extracellular proteinases. The encoded protein degrades type IV
collagen, fibronectin, fibrinogen, casein, vitronectin, alpha
1-antitrypsin, alpha 2-macroglobulin, and insulin-like growth
factor-binding protein 1, and activates MMP9 by cleavage. The
protein differs from most MMP family members in that it lacks a
conserved C-terminal protein domain. |