Matrix Metalloproteinase-9, total (MMP-9, total)
Matrix Metalloproteinase-9 (MMP-9), also known as 92 kd type IV collagenase or Gelatinase B, is a zinc-dependent endopeptidase, synthesized and secreted in monomeric form as a zymogen. The structure is similar to MMP-2, another member of matrixmetalloproteinase family. Its primary function is degradation of proteins in the extracellular matrix, digesting decorin, elastin, fibrillin, laminin, gelatin (denatured collagen), and types IV, V, XI and XVI collagen. MMP-9 also activates growth factors like proTGFb and proTNFa. Physiologically, MMP-9 in coordination with other MMPs, plays a role in normal tissue remodeling events such as neurite growth, embryonic development, angiogenesis, ovulation, mammary gland involution and wound healing. MMP-9, with other MMPs, is also involved in osteoblastic bone formation and/or inhibits osteoclastic bone resorption. Elevated expression of MMP-9, along with MMP-2, is usually seen in invasive and highly tumorigenic cancers such as colorectal tumors, gastric carcinoma, pancreatic carcinoma, breast cancer, oral cancer, melanoma, malignant gliomas, chondrosarcoma, and gastrointestinal adenocarcinoma. Levels are also increased in malignant astrocytomas, carcinomatous meningitis, and brain metastases.
Swiss-Prot Accession Number: P14780