MMP-9 Antikörper

Enzyme>>Protease & Regulator>>Metalloprotease & Regulator>>Matrix Metalloproteinase>>MMP-9/MMP9

Cancer>>Angiogenesis>>Matrix Metalloproteinase>>MMP-9/MMP9

Cancer>>Cancer Biomarkers>>MMP-9/MMP9

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. MMPs are synthesized as enzymogen and converted to active form by other MMPs or extracellular proteinases. MMP-9/MMP9, also known as 92-kDa gelatinase B/type IV collagenase, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. It contains a fibronectin-like domain, which functions in the binding of gelatin, a unique serine/proline/threonine-rich collagen type V-like domain probably serving as attachment sites of multiple O-linked oligosaccharides and a carboxyl terminal hemopexin-like domain. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. Studies have shown that MMP-9/MMP9 play control roles in IL8-induced leukocytosis and stem cell mobilization, and additionally in release of biologically active VEGF and consequently in the formation of ascites. MMP-9/MMP9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.

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