MMP-2, also known as gelatinase A, is a member the of matrix metalloproteinase family of proteins (MMPs). MMPs are structurally-related calcium-dependent, zinc-containing enzymes that degrade extracellular matrix and connective tissue proteins in normal physiological processes such as embryonic development, reproduction, and tissue remodeling. MMPs are also active in disease processes such as arthritis and metastasis. ? MMP-2 consists of a pro-domain (cleaved upon activation), a catalytic domain containing the zinc binding site, a fibronectin-like domain (that plays a role in the substrate targeting), and a carboxyl-terminal hemopexin-like domain. The activated form of MMP-2 is produced by a 2-step proteolytic processing. First, a complex comprised of membrane type 1 MMP (MT1-MMP) and tissue inhibitor of metalloproteinase 2 (TIMP-2) recruits pro-MMP-2 from the extracellular milieu to the cell surface. The second step requires an active molecule of MT1-MMP, which itself activates MMP-2, leading to subsequent autocatalytic cleavage. Substrates of activated MMP-2 include several components of the articular cartilaginous matrix including: type IV collagen, aggrecan, link protein, decorin, fibronectin, and type X and XI collagens. ? Elevated MMP-2 secretion is associated with poor prognosis in several types of human cancers. Mutations in the gene encoding MMP-2 gene are associated with Torg-Winchester syndrome, multicentric osteolysis, arthritis syndrome, and possibly keloids. MMP-2 deficient mice exhibit slightly delayed growth, reduced neovascularization, retarded tumor progression, an exaggerated asthma response to allergens, and impaired branching morphogenesis of the mammary glands.
Size
4 pack
Concentration
n/a
Applications
ELISA
Other Names
Matrix metallopeptidase 2, Gelatinase A, MMP2, GelA, Clg4a