MMP-2, also named gelatinase A, is a member of matrix metalloproteinase family proteins (MMPs). MMPs are structurally related, zinc-containing enzymes that degrade the extracellular matrix and connective tissue proteins in normal physiological processes such as embryonic development, reproduction, and tissue remodeling as well as in disease processes such as arthritis and metastasis. MMP-2 consists of a prodomain, which is 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 repeats) domain. Activation of MMP-2 requires proteolytic processing: first, a complex of membrane type 1 MMP (MT1-MMP) and tissue inhibitor of metalloproteinase 2 recruits pro-MMP-2 from the extracellular milieu to the cell surface; second, MMP-2 is activated by active MT1-MMP and subsequent autocatalytic cleavage. Substrates of MMP-2 include type IV collagen, aggrecan, link protein, decorin, fibronectin, and type X and XI collagens, all of which are components of the articular cartilaginous matrix. Importantly, MMP-2 secretion is elevated in several types of human cancers and its elevated expression has been associated with a poor prognosis. Mutations in the 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 gland.
Size
25 μg
Concentration
n/a
Applications
BA
Other Names
Matrix metallopeptidase 2, Gelatinase A, MMP2, GelA, Clg4a