Matrix metallopeptidase 12

Matrix metalloproteinase-12 (MMP-12) also known as macrophage metalloelastase (MME) or macrophage elastase (ME) is an is_associated_with::enzyme that in humans is encoded by the MMP12 is_associated_with::gene.

Function
Proteins of the is_associated_with::matrix metalloproteinase (MMP) family are involved in the breakdown of is_associated_with::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. The prodomain is cleaved by extracellular proteinases when the enzyme is activated. The active enzyme is constituted by two domains, the catalytic domain resposnsible for its enzymatic activity and the hemopexin-like domain that in some MMPs plays a role in substrate recognition and can contribute to increasing catalytic efficiency. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble is_associated_with::elastin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.

Clinical significance
MMP12 may play a role in is_associated_with::aneurysm formation and studies in mice and humans suggest a role in the development of is_associated_with::emphysema.