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Gene Review

Mmp14  -  matrix metallopeptidase 14 (membrane...

Rattus norvegicus

Synonyms: MMP-14, MT-MMP, MT-MMP 1, MT1-MMP, MT1MMP, ...
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Disease relevance of Mmp14


High impact information on Mmp14


Chemical compound and disease context of Mmp14


Biological context of Mmp14


Anatomical context of Mmp14


Associations of Mmp14 with chemical compounds

  • RESULTS: Gelatinolytic activity of pro-and active MMP-2 and concentrations of MT1-MMP protein, as determined by zymography and Western blot analysis, respectively, increased significantly from 6 hours to day 42 after intraductal infusion of oleic acid [7].
  • Both membrane type-1 MMP (MT1-MMP) and the integrin alphaV subunit are fully activated upon cleavage at a furin recognition site [13].
  • Brefeldin A (BFA), a Golgi-disturbing agent, inhibited MT1-MMP activation, indicating that it occurs in the trans-Golgi network (TGN), where furin is concentrated and colocalized with MT1-MMP [14].
  • CONCLUSION: These findings indicate that cyclical stretch induces MMP-14 and -2 expression in neonatal rat cardiomyocytes and that the induction is mediated by the angiotensin II-JAK-STAT1 pathway [15].
  • The mechanical strain also increased the immunohistochemical labeling of MMP-14 and -2 that was attenuated by adding losartan [15].

Regulatory relationships of Mmp14


Other interactions of Mmp14

  • The IGF-1 receptor (IGF-1R) and MT1-MMP are synthesized as larger precursor proproteins, which require endoproteolytic activation by the proprotein convertases (PCs) furin/PC5 to gain full biological activity [12].
  • Gelatinase A, MT1-MMP, and TIMP-2 messenger RNA (mRNA) were all upregulated in HSCs activated on plastic over 5 to 14 days [16].
  • RESULTS: MMP-13 mRNA was detected in epithelial cells of wounded corneas, but not in normal controls; MMP-14 was found in both normal and wounded corneas [11].
  • CONCLUSION: Our data suggest that MT1-MMP may play a role in extracellular matrix degradation during periodontitis, in concert with MMP-2 and other proteinases [2].
  • RESULTS: MMP-9, MMP-13, and MMP-14 were expressed in discrete perichondrial cells that gave way to sites of intrachondral canal formation [21].

Analytical, diagnostic and therapeutic context of Mmp14


  1. Enhanced expression of membrane type-1 matrix metalloproteinase in mesangial proliferative glomerulonephritis. Hayashi, K., Osada, S., Shofuda, K., Horikoshi, S., Shirato, I., Tomino, Y. J. Am. Soc. Nephrol. (1998) [Pubmed]
  2. Membrane type (MT) 1-matrix metalloproteinase (MMP) and MMP-2 expression in ligature-induced periodontitis in the rat. Achong, R., Nishimura, I., Ramachandran, H., Howell, T.H., Fiorellini, J.P., Karimbux, N.Y. J. Periodontol. (2003) [Pubmed]
  3. Gelatinase A (MMP-2) is necessary and sufficient for renal tubular cell epithelial-mesenchymal transformation. Cheng, S., Lovett, D.H. Am. J. Pathol. (2003) [Pubmed]
  4. Expression of matrix metalloproteinases during rat skin wound healing: evidence that membrane type-1 matrix metalloproteinase is a stromal activator of pro-gelatinase A. Okada, A., Tomasetto, C., Lutz, Y., Bellocq, J.P., Rio, M.C., Basset, P. J. Cell Biol. (1997) [Pubmed]
  5. Increased expression of membrane-type matrix metalloproteinase and preferential localization of matrix metalloproteinase-2 to the neointima of balloon-injured rat carotid arteries. Jenkins, G.M., Crow, M.T., Bilato, C., Gluzband, Y., Ryu, W.S., Li, Z., Stetler-Stevenson, W., Nater, C., Froehlich, J.P., Lakatta, E.G., Cheng, L. Circulation (1998) [Pubmed]
  6. Type I collagen-induced MMP-2 activation coincides with up-regulation of membrane type 1-matrix metalloproteinase and TIMP-2 in cardiac fibroblasts. Guo, C., Piacentini, L. J. Biol. Chem. (2003) [Pubmed]
  7. Long-term overexpression of membrane type-1 matrix metalloproteinase and matrix metalloproteinase-2 in oleic acid-induced pancreatitis in rats. Yamaguchi, T., Nakamura, H., Kihara, Y., Taguchi, M., Yoshikawa, H., Otsuki, M. Pancreas (2002) [Pubmed]
  8. Angiotensin type 1 receptor blockage improves ischemic injury following transient focal cerebral ischemia. Hosomi, N., Nishiyama, A., Ban, C.R., Naya, T., Takahashi, T., Kohno, M., Koziol, J.A. Neuroscience (2005) [Pubmed]
  9. Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation. Overall, C.M., Tam, E., McQuibban, G.A., Morrison, C., Wallon, U.M., Bigg, H.F., King, A.E., Roberts, C.R. J. Biol. Chem. (2000) [Pubmed]
  10. Coordinated elevation of membrane type 1-matrix metalloproteinase and matrix metalloproteinase-2 expression in rat uterus during postpartum involution. Manase, K., Endo, T., Chida, M., Nagasawa, K., Honnma, H., Yamazaki, K., Kitajima, Y., Goto, T., Kanaya, M., Hayashi, T., Mitaka, T., Saito, T. Reprod. Biol. Endocrinol. (2006) [Pubmed]
  11. Differential expression of MT1-MMP (MMP-14) and collagenase III (MMP-13) genes in normal and wounded rat corneas. Ye, H.Q., Maeda, M., Yu, F.S., Azar, D.T. Invest. Ophthalmol. Vis. Sci. (2000) [Pubmed]
  12. Proprotein convertases regulate insulin-like growth factor 1-induced membrane-type 1 matrix metalloproteinase in VSMCs via endoproteolytic activation of the insulin-like growth factor-1 receptor. Stawowy, P., Kallisch, H., Kilimnik, A., Margeta, C., Seidah, N.G., Chrétien, M., Fleck, E., Graf, K. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  13. Furin interacts with proMT1-MMP and integrin alphaV at specialized domains of renal cell plasma membrane. Mayer, G., Boileau, G., Bendayan, M. J. Cell. Sci. (2003) [Pubmed]
  14. Regulation of matrix metalloproteinase MT1-MMP/MMP-2 in cardiac fibroblasts by TGF-beta1 involves furin-convertase. Stawowy, P., Margeta, C., Kallisch, H., Seidah, N.G., Chrétien, M., Fleck, E., Graf, K. Cardiovasc. Res. (2004) [Pubmed]
  15. Angiotensin II signals mechanical stretch-induced cardiac matrix metalloproteinase expression via JAK-STAT pathway. Wang, T.L., Yang, Y.H., Chang, H., Hung, C.R. J. Mol. Cell. Cardiol. (2004) [Pubmed]
  16. Progelatinase A is produced and activated by rat hepatic stellate cells and promotes their proliferation. Benyon, R.C., Hovell, C.J., Da Gaça, M., Jones, E.H., Iredale, J.P., Arthur, M.J. Hepatology (1999) [Pubmed]
  17. MAPK signaling regulates endothelial cell assembly into networks and expression of MT1-MMP and MMP-2. Boyd, P.J., Doyle, J., Gee, E., Pallan, S., Haas, T.L. Am. J. Physiol., Cell Physiol. (2005) [Pubmed]
  18. Expression and activity of matrix metalloproteinase-2 and -9 in experimental granulation tissue. Inkinen, K., Turakainen, H., Wolff, H., Ravanti, L., Kähäri, V.M., Ahonen, J. APMIS (2000) [Pubmed]
  19. MT1-MMP in rat testicular development and the control of Sertoli cell proMMP-2 activation. Longin, J., Guillaumot, P., Chauvin, M.A., Morera, A.M., Le Magueresse-Battistoni, B. J. Cell. Sci. (2001) [Pubmed]
  20. Transcription factor Sp1 phosphorylation induced by shear stress inhibits membrane type 1-matrix metalloproteinase expression in endothelium. Yun, S., Dardik, A., Haga, M., Yamashita, A., Yamaguchi, S., Koh, Y., Madri, J.A., Sumpio, B.E. J. Biol. Chem. (2002) [Pubmed]
  21. Expression patterns of matrix metalloproteinases and vascular endothelial growth factor during epiphyseal ossification. Alvarez, J., Costales, L., Serra, R., Balbín, M., López, J.M. J. Bone Miner. Res. (2005) [Pubmed]
  22. The role of proteases in fibronectin matrix remodeling in thyroid epithelial cell monolayer cultures. Nezi, L., Greco, D., Nitsch, L., Garbi, C. Biol. Chem. (2002) [Pubmed]
  23. Increased matrix metalloproteinase-2 and membrane type 1 matrix metalloproteinase activity and expression in heterotopically transplanted murine tracheas. Inaki, N., Tsunezuka, Y., Kawakami, K., Sato, H., Takino, T., Oda, M., Watanabe, G. J. Heart Lung Transplant. (2004) [Pubmed]
  24. Activation of matrix metalloproteinase-2 from hepatic stellate cells requires interactions with hepatocytes. Théret, N., Musso, O., L'Helgoualc'h, A., Clément, B. Am. J. Pathol. (1997) [Pubmed]
  25. Macrophage-derived MT1-MMP and increased MMP-2 activity are associated with glomerular damage in crescentic glomerulonephritis. Hayashi, K., Horikoshi, S., Osada, S., Shofuda, K., Shirato, I., Tomino, Y. J. Pathol. (2000) [Pubmed]
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