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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP12 may be involved in tissue injury and remodeling. This protein has significant elastolytic activity. MMP12 can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, wtih small hydrophobic residues (prefereably alanine) occupying P3. The protein is found in alveolar macrophages but not in peripheral blood monocytes. MMP12 can be induced by exposure to lypopolysaccharide, and is inhibited by dexamethasone.
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