PBB GE MMP9 203936 s at. MMP9 may play an important role in angiogenesis and neovascularization. Knock-out models of MMP9 result in delayed apoptosis, vascularization, and ossification of hypertrophic chondrocytes. Collagen induced arthritis in the mouse a MMP9 deficient mouse model, it was seen that MMP9 coordinated epithelial wound repair and deficient mice were unable to remove the fibrinogen matrix during wound healing.
When interacting with TGF-ß1, Gelatinase B also stimulates collagen contraction, aiding in wound closure. The propeptide domain is characterized by a conserved PRCGVPD sequence. MMP-9 catalytic domain in complex with a fluorogenic synthetic peptidic substrate. Plasmin generates active MMP-3 from its zymogen. The catalytic domain contains two zinc and three calcium atoms. The catalytic zinc is coordinated by three histidines from the conserved HEXXHXXGXXH binding motif.
The other zinc atom and the three calcium atoms are structural. Three type II fibronectin repeats are inserted in the catalytic domain, although these domains are omitted in most crystallographic structures of MMP9 in complex with inhibitors. The active form of MMP9 also contains a C-terminal hemopexin-like domain. The hemopexin domain is important to facilitate the cleavage of triple helical interstitial collagens. MMP9 has been found to be associated with numerous pathological processes, including cancer, placental malaria, immunologic and cardiovascular diseases. One of MMP9’s most widely associated pathologies is the relationship to cancer, due to its role in extracellular matrix remodeling and angiogenesis. For example, its increased expression was seen in a metastatic mammary cancer cell line.