3.4.24.80 CCN3 + H2O - 3.4.24.80 CCN5 + H2O UniProt ID O76076, CCN5 lacks the CTCK domain 3.4.24.80 CD44 + H2O - 3.4.24.80 Collagen + H2O - 3.4.24.80 collagen I + H2O - 3.4.24.80 collagen I + H2O degradation 3.4.24.80 fibroblast growth factor receptor-1 + H2O - 3.4.24.80 fibroblast growth factor receptor-4 + H2O - 3.4.24.80 Fibronectin + H2O - 3.4.24.80 Gelatin + H2O - 3.4.24.80 growth differentiation factor-1 + H2O - 3.4.24.80 hepatocyte growth factor activator inhibitor-1 + H2O - 3.4.24.80 hepatocyte growth factor activator inhibitor-1 + H2O the 66 kDa protein is cleaved to 58, 42, and 16 kDa fragments 3.4.24.80 kidney injury molecule-1 + H2O the enzyme cleaves and sheds the substrate's ectodomain 3.4.24.80 Laminin + H2O - 3.4.24.80 Laminin-1 + H2O - 3.4.24.80 laminin-5 + H2O - 3.4.24.80 additional information membrane type 1 matrix metalloproteinase activates progelatinase A, a type IV collagenase, on the cell surface of tumors. Membrane type 1-matrix metalloproteinase may play an important role in the invasive growth and spread of breast cancer cells by specifically activating pro-MMP-2 to cleave the connective-tissue barrier 3.4.24.80 additional information healing process 3.4.24.80 additional information breakdown of extracellular matrix 3.4.24.80 additional information involved in cell migration 3.4.24.80 additional information enzyme activates gelatinase 3.4.24.80 additional information role in extracellular matrix remodelling under physiological and pathological conditions 3.4.24.80 additional information degrades components of tissue barriers, regulates cell-extracellular matrix interaction by processing cell adhesion molecules such as CD44 and integrin alpha v chain 3.4.24.80 additional information remodeling of the extracellular matrix 3.4.24.80 additional information central role in tumor cell invasion 3.4.24.80 additional information key protease in tumor cell invasion 3.4.24.80 additional information the enzyme regulates extracellular matrix remodeling and is capable of cleaving a wide variety of transmembrane proteins. The enzymatic activity of MT1-MMP is regulated by endogenous inhibitors, TIMP, the tissue inhibitor of metalloproteinases 3.4.24.80 additional information enzyme regulation, transcription factor EGR1 is involved, overview 3.4.24.80 additional information in vivo growth of FaDu cells co-injected with murine fibroblasts is increased, while their progression is reduced in MT1-MMP-deficient fibroblasts, overview 3.4.24.80 additional information MT1-MMP activates MMP-2 3.4.24.80 additional information MT1-MMP is increased in myocardial ischemia and reperfusion, and contributes to myocardial dysfunction, upstream induction mechanism by release of endothelin and protein kinase C activation, microdialysis analysis, overview 3.4.24.80 additional information membrane-type MMPs are membrane spanning binding sites that play an important role in the cell surface activation of MMPs such as MMP-2 3.4.24.80 additional information MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview. Tetraspanins are attracting attention as binding proteins of MT1-MMP, which regulate subcellular localization and compartmentalization of MT1-MMP and consequent MT1-MMP activities 3.4.24.80 additional information overview of MT1-MMP-associating proteins by localization and MT1-MMP-associating membrane proteins by function. Some proteins, such as MT1-SP, EGFR, 5T4, DCP, and CD36L1, preferentially precipitate pro-MT1-MMP, other proteins, e.g. GA733-1, HAI-1, HAI-2, TF, THBD, and CD9, precipitate preferentially the active form of MT1-MMP indicating that these proteins may form a complex on the cell surface 3.4.24.80 additional information the enzyme does not degrade fibroblast growth factor-2 or fibroblast growth factor receptor-2 3.4.24.80 additional information interaction analysis of MMP14 with proteins in HeLa cells identified by inactive catalytic domain capture yeast 2-hybrid analysis, overview. Detection of CCN5 as a MMP14 substrate by yeast 2-hybrid screening 3.4.24.80 neuronal glial antigen 2 + H2O three (210, 160, and 51-52 kDa) major cleavage products are formed 3.4.24.80 Notch1 + H2O - 3.4.24.80 pro-MMP-2 + H2O MT-MMP1 activates MMP-2, EC 3.4.24.24 3.4.24.80 pro-MMP-2 + H2O activation of MMP-2 3.4.24.80 pro-MMP-2 + H2O - 3.4.24.80 pro-MMP-2 + H2O MMP14 is essential for proMMP-2 activation: pro-MMP-2 activation by MMP14/TIMP complex is realized in an environment of low TIMP concentration 3.4.24.80 pro-MMP-2 + H2O the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP (TIMP)-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP 3.4.24.80 pro-MMP-2 + H2O the TIMP-2-dependent pathway of MMP-2 activation involves tissue inhibitor of MMP-2 as a bridging molecule between MT1-MMP and pro-MMP-2. Thus, net activity of MT1-MMP and MMP-2 is regulated in a complex manner depending on TIMP-2 concentration. For the TIMP-2-independent pathway, claudin recruits MT-MMP and MMP-2 at a tight junction to achieve elevated focal concentrations, and consequently enhances activation of pro-MMP-2. Pro-MMP-2 associates with TIMP-2-deficient cells through the hemopexin domain, and is processed by MT2-MMP 3.4.24.80 proMMP-2 + H2O - 3.4.24.80 proMMP-2 + H2O activation 3.4.24.80 stromal cell-derived factor 1 + H2O - 3.4.24.80 syndecan-1 + H2O - 3.4.24.80 transforming growth factor-beta + H2O - 3.4.24.80 Type I collagen + H2O - 3.4.24.80 Type I collagen + H2O cleavage of collagen by MT1-MMP regulates cell growth and invasion in a collagen-rich environment 3.4.24.80 Vitronectin + H2O -