Matrix metalloproteinase

Matrix metalloproteases ( MMPs) are a group of related enzymes, which catalyze the cleavage of peptide bonds in proteins ( so-called peptidases ). They come in all living things before except protozoa. In eukaryotes they are located outside of the cells in the extracellular matrix, they can degrade in the activated state. This is part of the tissue remodeling that occurs in a variety of biological processes such as morphogenesis, wound healing, angiogenesis or tumor growth. In addition, MMPs have additional functions in the processing of signaling molecules that control cell behavior, this function is often performed by a whole network of MMPs and is braked at the same time of endogenous protease inhibitors.

While bacteria and archaea have only a few MMP homologs in the genome, are found in mammals up to two dozen. In humans, 23 matrix metalloproteinases known ( gene MMP1 to MMP28 ). Mutations in three genes MMP can be the cause of rare inherited disorders: Torg - Winchester syndrome, a special form of osteolysis ( MMP2 ); two forms of dysplasia ( MMP13 ); and enamel formation defect ( MMP20 ').

MMPs include the addition Peptidasedomäne which a metal (usually zinc, Zn ) binds, one or more vitronectin or hemopexin domains to help the enzyme at the anchorage in the extracellular matrix or cell membrane. In addition, they always have a calcium-binding domain, which is necessary for activation. They belong to the subfamily M10A in the MEROPS classification of peptidases.