The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

MMP7  -  matrix metallopeptidase 7 (matrilysin,...

Homo sapiens

Synonyms: MMP-7, MPSL1, Matrilysin, Matrin, Matrix metalloproteinase-7, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of MMP7


Psychiatry related information on MMP7

  • CONCLUSION: We conclude that measurement of plasma MMP-7 or MMP-9 levels, as performed in our trial, was not a useful prognostic or predictive factor in patients with MBC or in patients treated with an MMPI [5].

High impact information on MMP7

  • Here we show that matrix metalloproteinase-7 (MMP-7) is expressed not only in the majority of human pancreatic ductal adenocarcinoma specimens, but also in human pancreatic intraepithelial neoplasia and metaplastic duct lesions in human and mouse [6].
  • Under identical conditions, mice either deficient in MMP-7 or carrying an inactive FasL gene are severely inhibited in development of progressive metaplasia and acinar cell apoptosis [6].
  • In a mouse model of pancreatic acinar-to-ductal metaplasia, MMP-7 progressively accumulates during the metaplastic transition, resulting in a concomitant increase in solubilization of Fas ligand (FasL) [6].
  • Proliferation of gastric epithelial cells also was stimulated by MMP-7-treated myofibroblasts via IGF-II [7].
  • We have studied the role of MMP-7 in signaling between epithelial cells and a key stromal cell type, the myofibroblast [7].

Chemical compound and disease context of MMP7


Biological context of MMP7


Anatomical context of MMP7


Associations of MMP7 with chemical compounds

  • Resistance to doxorubicin was also induced by expression in the tumor cells of constitutively active MMP-7 but not of a catalytically inactive mutant [14].
  • MMP-7 can also activate proMMP-9 up to approximately 50% of the full activity with a new NH2 terminus of Leu16-Arg-Thr-(Asn)-Leu [18].
  • Nitroglycerin 2,000 pmol also increased MMP-2 and MMP-7 mRNA levels to 187 +/- 8% and 183 +/- 21% of control values, respectively (p < 0.05) [19].
  • Active pump-1 is inhibited by EDTA, 1,10-phenanthroline, and the tissue inhibitor of metalloproteinases [20].
  • N-Acetyl-L-cysteine, superoxide (O2-) dismutase and catalase attenuated the EGCG-induced pro-MMP-7 production, suggesting an involvement of oxidative stress in these events [21].
  • On the other hand, estrogen acidification of the luminal solution would tend to alkalinize exocytotic vesicles and may lead to decreased activation of the MMP-7 [22].

Physical interactions of MMP7

  • Using EMSA analysis we also observed that the EGF stimulated increase in PEA3 transcription factors led to increased binding to specific ETS sites within the MMP-7 promoter [23].

Enzymatic interactions of MMP7


Regulatory relationships of MMP7


Other interactions of MMP7


Analytical, diagnostic and therapeutic context of MMP7


  1. Specific matrix metalloproteinase expression in focal myositis: an immunopathological study. Rodolico, C., Mazzeo, A., Toscano, A., Messina, S., Aguennouz, M., Gaeta, M., Messina, C., Vita, G. Acta neurologica Scandinavica. (2005) [Pubmed]
  2. Comprehensive analysis of matrix metalloproteinase and tissue inhibitor expression in pancreatic cancer: increased expression of matrix metalloproteinase-7 predicts poor survival. Jones, L.E., Humphreys, M.J., Campbell, F., Neoptolemos, J.P., Boyd, M.T. Clin. Cancer Res. (2004) [Pubmed]
  3. Differential expression of matrilysin-1 (MMP-7), 92 kD gelatinase (MMP-9), and metalloelastase (MMP-12) in oral verrucous and squamous cell cancer. Impola, U., Uitto, V.J., Hietanen, J., Hakkinen, L., Zhang, L., Larjava, H., Isaka, K., Saarialho-Kere, U. J. Pathol. (2004) [Pubmed]
  4. Identification of amino acid residues of matrix metalloproteinase-7 essential for binding to cholesterol sulfate. Higashi, S., Oeda, M., Yamamoto, K., Miyazaki, K. J. Biol. Chem. (2008) [Pubmed]
  5. Plasma matrix metalloproteinases 7 and 9 in patients with metastatic breast cancer treated with marimastat or placebo: Eastern Cooperative Oncology Group trial E2196. Zucker, S., Wang, M., Sparano, J.A., Gradishar, W.J., Ingle, J.N., Davidson, N.E. Clin. Breast Cancer (2006) [Pubmed]
  6. Matrix metalloproteinase-7 is expressed by pancreatic cancer precursors and regulates acinar-to-ductal metaplasia in exocrine pancreas. Crawford, H.C., Scoggins, C.R., Washington, M.K., Matrisian, L.M., Leach, S.D. J. Clin. Invest. (2002) [Pubmed]
  7. The role of matrix metalloproteinase-7 in redefining the gastric microenvironment in response to Helicobacter pylori. McCaig, C., Duval, C., Hemers, E., Steele, I., Pritchard, D.M., Przemeck, S., Dimaline, R., Ahmed, S., Bodger, K., Kerrigan, D.D., Wang, T.C., Dockray, G.J., Varro, A. Gastroenterology (2006) [Pubmed]
  8. Mycobacterium tuberculosis, but not vaccine BCG, specifically upregulates matrix metalloproteinase-1. Elkington, P.T., Nuttall, R.K., Boyle, J.J., O'Kane, C.M., Horncastle, D.E., Edwards, D.R., Friedland, J.S. Am. J. Respir. Crit. Care Med. (2005) [Pubmed]
  9. Clinicopathologic and prognostic significance of matrix metalloproteinases in rectal cancer. Schwandner, O., Schlamp, A., Broll, R., Bruch, H.P. International journal of colorectal disease (2007) [Pubmed]
  10. Effect of an Efflux Pump Inhibitor on the Function of the Multidrug Efflux Pump CmeABC and Antimicrobial Resistance in Campylobacter. Martinez, A., Lin, J. Foodborne Pathog. Dis. (2006) [Pubmed]
  11. Nobiletin, a citrus flavonoid, down-regulates matrix metalloproteinase-7 (matrilysin) expression in HT-29 human colorectal cancer cells. Kawabata, K., Murakami, A., Ohigashi, H. Biosci. Biotechnol. Biochem. (2005) [Pubmed]
  12. Regulation of matrilysin expression in endothelium by fibroblast growth factor-2. Holnthoner, W., Kerenyi, M., Gröger, M., Kratochvill, F., Petzelbauer, P. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  13. Mapping of the metalloproteinase gene matrilysin (MMP7) to human chromosome 11q21-->q22. Knox, J.D., Boreham, D.R., Walker, J.A., Morrison, D.P., Matrisian, L.M., Nagle, R.B., Bowden, G.T. Cytogenet. Cell Genet. (1996) [Pubmed]
  14. Matrix metalloproteinase-7-mediated cleavage of Fas ligand protects tumor cells from chemotherapeutic drug cytotoxicity. Mitsiades, N., Yu, W.H., Poulaki, V., Tsokos, M., Stamenkovic, I. Cancer Res. (2001) [Pubmed]
  15. Imbalance of expression of matrix metalloproteinases (MMPs) and tissue inhibitors of the matrix metalloproteinases (TIMPs) in human pancreatic carcinoma. Bramhall, S.R., Neoptolemos, J.P., Stamp, G.W., Lemoine, N.R. J. Pathol. (1997) [Pubmed]
  16. Insulin-like growth factor binding protein-5 is a target of matrix metalloproteinase-7: implications for epithelial-mesenchymal signaling. Hemers, E., Duval, C., McCaig, C., Handley, M., Dockray, G.J., Varro, A. Cancer Res. (2005) [Pubmed]
  17. Concanavalin A produces a matrix-degradative phenotype in human fibroblasts. Induction and endogenous activation of collagenase, 72-kDa gelatinase, and Pump-1 is accompanied by the suppression of the tissue inhibitor of matrix metalloproteinases. Overall, C.M., Sodek, J. J. Biol. Chem. (1990) [Pubmed]
  18. Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties. Imai, K., Yokohama, Y., Nakanishi, I., Ohuchi, E., Fujii, Y., Nakai, N., Okada, Y. J. Biol. Chem. (1995) [Pubmed]
  19. Nitroglycerin upregulates matrix metalloproteinase expression by human macrophages. Death, A.K., Nakhla, S., McGrath, K.C., Martell, S., Yue, D.K., Jessup, W., Celermajer, D.S. J. Am. Coll. Cardiol. (2002) [Pubmed]
  20. Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Quantin, B., Murphy, G., Breathnach, R. Biochemistry (1989) [Pubmed]
  21. (-)-Epigallocatechin-3-gallate promotes pro-matrix metalloproteinase-7 production via activation of the JNK1/2 pathway in HT-29 human colorectal cancer cells. Kim, M., Murakami, A., Kawabata, K., Ohigashi, H. Carcinogenesis (2005) [Pubmed]
  22. Estrogen decrease in tight junctional resistance involves matrix-metalloproteinase-7-mediated remodeling of occludin. Gorodeski, G.I. Endocrinology (2007) [Pubmed]
  23. Epidermal growth factor upregulates matrix metalloproteinase-7 expression through activation of PEA3 transcription factors. Lynch, C.C., Crawford, H.C., Matrisian, L.M., McDonnell, S. Int. J. Oncol. (2004) [Pubmed]
  24. Matrix metalloproteinases cleave tissue factor pathway inhibitor. Effects on coagulation. Belaaouaj, A.A., Li, A., Wun, T.C., Welgus, H.G., Shapiro, S.D. J. Biol. Chem. (2000) [Pubmed]
  25. Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. Imai, K., Hiramatsu, A., Fukushima, D., Pierschbacher, M.D., Okada, Y. Biochem. J. (1997) [Pubmed]
  26. Activation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cells. Zhao, Y.G., Xiao, A.Z., Newcomer, R.G., Park, H.I., Kang, T., Chung, L.W., Swanson, M.G., Zhau, H.E., Kurhanewicz, J., Sang, Q.X. J. Biol. Chem. (2003) [Pubmed]
  27. ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3. Mochizuki, S., Shimoda, M., Shiomi, T., Fujii, Y., Okada, Y. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  28. beta-Catenin and p53 analyses of a breast carcinoma tissue microarray. Chung, G.G., Zerkowski, M.P., Ocal, I.T., Dolled-Filhart, M., Kang, J.Y., Psyrri, A., Camp, R.L., Rimm, D.L. Cancer (2004) [Pubmed]
  29. Expression and activity of matrix metalloproteases in human malignant mesothelioma cell lines. Liu, Z., Ivanoff, A., Klominek, J. Int. J. Cancer (2001) [Pubmed]
  30. Differential expression of matrix metalloproteinases and their tissue inhibitors in human primary cultured prostatic cells and malignant prostate cell lines. Zhang, J., Jung, K., Lein, M., Kristiansen, G., Rudolph, B., Hauptmann, S., Schnorr, D., Loening, S.A., Lichtinghagen, R. Prostate (2002) [Pubmed]
  31. Role of PTEN and MMP-7 expression in growth, invasion, metastasis and angiogenesis of gastric carcinoma. Zheng, H.C., Sun, J.M., Li, X.H., Yang, X.F., Zhang, Y.C., Xin, Y. Pathol. Int. (2003) [Pubmed]
  32. beta-catenin regulates the expression of the matrix metalloproteinase-7 in human colorectal cancer. Brabletz, T., Jung, A., Dag, S., Hlubek, F., Kirchner, T. Am. J. Pathol. (1999) [Pubmed]
  33. Matrix metalloproteinase-7 increases resistance to Fas-mediated apoptosis and is a poor prognostic factor of patients with colorectal carcinoma. Wang, W.S., Chen, P.M., Wang, H.S., Liang, W.Y., Su, Y. Carcinogenesis (2006) [Pubmed]
  34. Design, synthesis, and characterization of potent, slow-binding inhibitors that are selective for gelatinases. Bernardo, M.M., Brown, S., Li, Z.H., Fridman, R., Mobashery, S. J. Biol. Chem. (2002) [Pubmed]
  35. Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin). Agnihotri, R., Crawford, H.C., Haro, H., Matrisian, L.M., Havrda, M.C., Liaw, L. J. Biol. Chem. (2001) [Pubmed]
  36. Enhanced production and activation of matrix metalloproteinase-7 (matrilysin) in human endometrial carcinomas. Ueno, H., Yamashita, K., Azumano, I., Inoue, M., Okada, Y. Int. J. Cancer (1999) [Pubmed]
  37. Matrilysin (MMP-7) is a major matrix metalloproteinase upregulated in biliary atresia-associated liver fibrosis. Huang, C.C., Chuang, J.H., Chou, M.H., Wu, C.L., Chen, C.M., Wang, C.C., Chen, Y.S., Chen, C.L., Tai, M.H. Mod. Pathol. (2005) [Pubmed]
  38. Effects of norepinephrine, HIV type 1 infection, and leukocyte interactions with endothelial cells on the expression of matrix metalloproteinases. Sundstrom, J.B., Mosunjac, M., Martinson, D.E., Bostik, P., Donahoe, R.M., Gravanis, M.B., Ansari, A.A. AIDS Res. Hum. Retroviruses (2001) [Pubmed]
WikiGenes - Universities