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Gene Review

MMP15  -  matrix metallopeptidase 15 (membrane...

Homo sapiens

Synonyms: MMP-15, MT-MMP 2, MT2-MMP, MT2MMP, MTMMP2, ...
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Disease relevance of MMP15


High impact information on MMP15

  • Additional targets of these inhibitors include MT2-MMP and ADAM-15, which also regulate EC invasion [6].
  • Northern blot analysis demonstrated the predominant expression of MT1-MMP mRNA in carcinoma tissues (20 of 20 cases), whereas MT2-MMP was detected in only 25% of the cases (5 of 20 cases), and no detectable expression of MT3-MMP was observed [2].
  • Similarly, TIMP-3 did not promote MT2-MMP-mediated MMP-2 activation but inhibited activation at higher concentrations [7].
  • The in vivo relevance of these findings is supported by the overexpression of MMP-15 in human lung adenocarcinoma compared with normal lung [8].
  • The quantitative reverse transcription polymerase chain reaction analyses demonstrate that MT1-MMP and MT2-MMP are expressed predominantly in glioblastoma tissues (17/17 and 12/17 cases, respectively), and their expression levels increase significantly as tumor grade increases [3].

Biological context of MMP15


Anatomical context of MMP15


Associations of MMP15 with chemical compounds

  • These residues are located in the insertion sequence-2 (IS-2), which was conserved in six clones of the human MT2-MMP gene from different sources, except that of proline-183 which was substituted with serine from HT1080 cells [16].

Physical interactions of MMP15


Regulatory relationships of MMP15


Other interactions of MMP15

  • Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization [17].
  • In addition, the MMP15 and MX2 genes were identified, for the first time, as being commonly overexpressed in lung AdC cells [18].
  • RESULTS: MMP-1, -2, -3, and -9; MT2-MMP; and TIMP-1 were expressed in cultured RPE cells [19].
  • Results showed that incubation of MCF-7 cells with 30 microM of the synthetic GnRH analogues for 48 h in serum-containing medium resulted in a decrease of MMP-9 expression and increase in MT1- and MT2-MMP mRNA levels [20].
  • Expression of MMP-7, MT2-MMP and TIMP-1 was found at a low frequency and a low amount in both the cells and the tissues [21].

Analytical, diagnostic and therapeutic context of MMP15

  • An increase in the activation ratio of proMMP-2 correlated directly with the expression of MT1-MMP but not MT2-MMP, as measured by either Northern blot analysis or immunostaining [2].
  • Furthermore, the finding of a preferential expression of MT2-MMP in hepatocytes, together with our previous demonstration that the activation of stellate cell-derived MMP2 in co-culture requires interactions with hepatocytes (Am J Pathol 1997, 150:51-58), suggests that parenchymal cells might play a pivotal role in the MMP2 activation process [14].
  • Furthermore, data suggest that, independently of cell culture conditions, the expression of MT2-MMP may be associated with malignant transformation of mammary cells and the overexpression of MMP-1 and -7 with the highly metastatic potential of epithelial breast cancer cells [22].


  1. Activation of progelatinase A and progelatinase A/TIMP-2 complex by membrane type 2-matrix metalloproteinase. Kolkenbrock, H., Hecker-Kia, A., Orgel, D., Ulbrich, N., Will, H. Biol. Chem. (1997) [Pubmed]
  2. Expression and tissue localization of membrane-types 1, 2, and 3 matrix metalloproteinases in human invasive breast carcinomas. Ueno, H., Nakamura, H., Inoue, M., Imai, K., Noguchi, M., Sato, H., Seiki, M., Okada, Y. Cancer Res. (1997) [Pubmed]
  3. Expression and tissue localization of membrane-type 1, 2, and 3 matrix metalloproteinases in human astrocytic tumors. Nakada, M., Nakamura, H., Ikeda, E., Fujimoto, N., Yamashita, J., Sato, H., Seiki, M., Okada, Y. Am. J. Pathol. (1999) [Pubmed]
  4. Targeting the cytotoxicity of fusogenic membrane glycoproteins in gliomas through protease-substrate interaction. Johnson, K.J., Peng, K.W., Allen, C., Russell, S.J., Galanis, E. Gene Ther. (2003) [Pubmed]
  5. The chemokine stromal cell derived factor-1 (CXCL12) promotes glioma invasiveness through MT2-matrix metalloproteinase. Zhang, J., Sarkar, S., Yong, V.W. Carcinogenesis (2005) [Pubmed]
  6. Coregulation of vascular tube stabilization by endothelial cell TIMP-2 and pericyte TIMP-3. Saunders, W.B., Bohnsack, B.L., Faske, J.B., Anthis, N.J., Bayless, K.J., Hirschi, K.K., Davis, G.E. J. Cell Biol. (2006) [Pubmed]
  7. TIMP independence of matrix metalloproteinase (MMP)-2 activation by membrane type 2 (MT2)-MMP is determined by contributions of both the MT2-MMP catalytic and hemopexin C domains. Morrison, C.J., Overall, C.M. J. Biol. Chem. (2006) [Pubmed]
  8. Identification of MMP-15 as an anti-apoptotic factor in cancer cells. Abraham, R., Schäfer, J., Rothe, M., Bange, J., Knyazev, P., Ullrich, A. J. Biol. Chem. (2005) [Pubmed]
  9. Genes of the membrane-type matrix metalloproteinase (MT-MMP) gene family, MMP14, MMP15, and MMP16, localize to human chromosomes 14, 16, and 8, respectively. Mattei, M.G., Roeckel, N., Olsen, B.R., Apte, S.S. Genomics (1997) [Pubmed]
  10. Messenger RNA for membrane-type 2 matrix metalloproteinase, MT2-MMP, is expressed in human placenta of first trimester. Bjørn, S.F., Hastrup, N., Larsen, J.F., Lund, L.R., Pyke, C. Placenta (2000) [Pubmed]
  11. Progesterone inhibits activation of latent matrix metalloproteinase (MMP)-2 by membrane-type 1 MMP: enzymes coordinately expressed in human endometrium. Zhang, J., Hampton, A.L., Nie, G., Salamonsen, L.A. Biol. Reprod. (2000) [Pubmed]
  12. Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family. Takino, T., Sato, H., Shinagawa, A., Seiki, M. J. Biol. Chem. (1995) [Pubmed]
  13. Implication of collagen type I-induced membrane-type 1-matrix metalloproteinase expression and matrix metalloproteinase-2 activation in the metastatic progression of breast carcinoma. Gilles, C., Polette, M., Seiki, M., Birembaut, P., Thompson, E.W. Lab. Invest. (1997) [Pubmed]
  14. Differential expression and origin of membrane-type 1 and 2 matrix metalloproteinases (MT-MMPs) in association with MMP2 activation in injured human livers. Théret, N., Musso, O., L'Helgoualc'h, A., Campion, J.P., Clément, B. Am. J. Pathol. (1998) [Pubmed]
  15. Role of MT-MMPs and MMP-2 in pancreatic cancer progression. Ellenrieder, V., Alber, B., Lacher, U., Hendler, S.F., Menke, A., Boeck, W., Wagner, M., Wilda, M., Friess, H., Büchler, M., Adler, G., Gress, T.M. Int. J. Cancer (2000) [Pubmed]
  16. Human membrane type-2 matrix metalloproteinase is defective in cell-associated activation of progelatinase A. Miyamori, H., Takino, T., Seiki, M., Sato, H. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  17. Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization. Sato, H., Tanaka, M., Takino, T., Inoue, M., Seiki, M. Genomics (1997) [Pubmed]
  18. Identification of genes whose expression is upregulated in lung adenocarcinoma cells in comparison with type II alveolar cells and bronchiolar epithelial cells in vivo. Kobayashi, K., Nishioka, M., Kohno, T., Nakamoto, M., Maeshima, A., Aoyagi, K., Sasaki, H., Takenoshita, S., Sugimura, H., Yokota, J. Oncogene (2004) [Pubmed]
  19. Modulation of matrix metalloproteinase and TIMP-1 expression by cytokines in human RPE cells. Eichler, W., Friedrichs, U., Thies, A., Tratz, C., Wiedemann, P. Invest. Ophthalmol. Vis. Sci. (2002) [Pubmed]
  20. Gonadotropin-releasing hormone analogues alter gene expression of metalloproteinases and their tissue inhibitors in human breast cancer epithelial cells. Lamari, F.N., Zompra, A.A., Pateraki, E., Kousidou, O.C., Magafa, V., Karamanos, N.K., Cordopatis, P. Anticancer Res. (2006) [Pubmed]
  21. Expression of matrix metalloproteinases (MMPs) in cultured hepatocellular carcinoma (HCC) cells and surgically resected HCC tissues. Ogasawara, S., Yano, H., Momosaki, S., Nishida, N., Takemoto, Y., Kojiro, S., Kojiro, M. Oncol. Rep. (2005) [Pubmed]
  22. Expression of MMPs and TIMPs genes in human breast cancer epithelial cells depends on cell culture conditions and is associated with their invasive potential. Kousidou, O.C., Roussidis, A.E., Theocharis, A.D., Karamanos, N.K. Anticancer Res. (2004) [Pubmed]
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