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Gene Review

MMP26  -  matrix metallopeptidase 26

Homo sapiens

Synonyms: Endometase, MGC126590, MGC126592, MMP-26, Matrilysin-2, ...
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Disease relevance of MMP26


High impact information on MMP26


Chemical compound and disease context of MMP26


Biological context of MMP26

  • The mRNA and protein level of MMP26 in chorionic villi was highest at Weeks 6-7, and decreased thereafter, reaching its lowest level at the second trimester [6].
  • The expression patterns of MMP26 in human placenta suggests complicated roles for MMP26 during the processes of placentation and hematopoiesis, perhaps working in concert with other members of the MMP family, such as MMP9 [6].
  • Interestingly, inhibitor titration studies revealed that only approximately 5% of the total MMP-26 molecules was catalytically active, indicating that the thiol groups of Cys(82) in the active molecules may be dissociated or removed from the active site zinc ions [7].
  • Peptide libraries were used to profile the substrate specificity of MMP-26 from the P4-P4' sites [7].
  • By using a novel cloning strategy, we identified three previously unknown human MMPs, i.e. MMP-21, MMP-26 and MMP-28, in comprehensive gene libraries [8].

Anatomical context of MMP26

  • MMP26 was widely localized to villous cytotrophoblast cells, syncytiotrophoblast cells, and to column trophoblasts during early pregnancy [6].
  • Notably, intense expression of MMP26 was found in fetal nucleated red cells inside the villous capillaries during gestational Weeks 6-9 [6].
  • Strong expression of MMP26 mRNA was also demonstrated in fetal red cells isolated from the whole blood of fetuses at midpregnancy [6].
  • We have previously reported that matrix metalloproteinase-26 (MMP-26) promotes the invasion of human prostate cancer cells via the cleavage of basement membrane proteins and by activating the zymogen form of MMP-9 [9].
  • A pair of stereoisomers had only a 40-fold difference in K(i)(app) values against MMP-26 compared with a 250-fold difference against neutrophil collagenase, indicating that MMP-26 is less stereoselective for its inhibitors [7].

Associations of MMP26 with chemical compounds

  • To explore MMP-26 active site structure-activity, a series of new potent mercaptosulfide MMP inhibitors (MMPIs) with Leu or homophenylalanine (Homophe) side chains at the P1' site were selected [10].
  • Several unique structural and regulatory features, including an unusual 'cysteine-switch' motif, discriminate broad-spectrum MMP-26 from most other MMPs [8].
  • RESULT(S): Endometrium from women with a normal menstrual cycle and users of levonorgestrel implants expresses MMP-26, TIMP-3, and TIMP-4 [5].
  • An expression of MMP-26 in the estrogen-dependent neoplasms is likely to contribute to the inactivation of AAT, to the follow-up liberation of the Ser protease activity, and because of these biochemical events, to promote matrix destruction and malignant progression [11].
  • We recently discovered that AAT is efficiently cleaved by a novel metalloproteinase, MMP-26, which exhibits an unconventional PH(81)CGVPD Cys switch motif and is autocatalytically activated in cells and tissues [11].

Enzymatic interactions of MMP26


Co-localisations of MMP26


Regulatory relationships of MMP26


Other interactions of MMP26


Analytical, diagnostic and therapeutic context of MMP26


  1. Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion. Zhao, Y.G., Xiao, A.Z., Park, H.I., Newcomer, R.G., Yan, M., Man, Y.G., Heffelfinger, S.C., Sang, Q.X. Cancer Res. (2004) [Pubmed]
  2. 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]
  3. Association of matrilysin-2 (MMP-26) expression with tumor progression and activation of MMP-9 in esophageal squamous cell carcinoma. Yamamoto, H., Vinitketkumnuen, A., Adachi, Y., Taniguchi, H., Hirata, T., Miyamoto, N., Nosho, K., Imsumran, A., Fujita, M., Hosokawa, M., Hinoda, Y., Imai, K. Carcinogenesis (2004) [Pubmed]
  4. Matrix metalloproteinase 26 proteolysis of the NH2-terminal domain of the estrogen receptor beta correlates with the survival of breast cancer patients. Savinov, A.Y., Remacle, A.G., Golubkov, V.S., Krajewska, M., Kennedy, S., Duffy, M.J., Rozanov, D.V., Krajewski, S., Strongin, A.Y. Cancer Res. (2006) [Pubmed]
  5. Expression of matrix metalloproteinase-26 and tissue inhibitor of matrix metalloproteinase-3 and -4 in endometrium throughout the normal menstrual cycle and alteration in users of levonorgestrel implants who experience irregular uterine bleeding. Chegini, N., Rhoton-Vlasak, A., Williams, R.S. Fertil. Steril. (2003) [Pubmed]
  6. Spatio-temporal expression of matrix metalloproteinase-26 in human placental trophoblasts and fetal red cells during normal placentation. Qiu, W., Bai, S.X., Zhao, M.R., Wu, X.Q., Zhao, Y.G., Sang, Q.X., Wang, Y.L. Biol. Reprod. (2005) [Pubmed]
  7. Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26. Park, H.I., Turk, B.E., Gerkema, F.E., Cantley, L.C., Sang, Q.X. J. Biol. Chem. (2002) [Pubmed]
  8. Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin. Marchenko, G.N., Ratnikov, B.I., Rozanov, D.V., Godzik, A., Deryugina, E.I., Strongin, A.Y. Biochem. J. (2001) [Pubmed]
  9. Coordinated peak expression of MMP-26 and TIMP-4 in preinvasive human prostate tumor. Lee, S., Desai, K.K., Iczkowski, K.A., Newcomer, R.G., Wu, K.J., Zhao, Y.G., Tan, W.W., Roycik, M.D., Sang, Q.X. Cell Res. (2006) [Pubmed]
  10. The intermediate S1' pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling. Park, H.I., Jin, Y., Hurst, D.R., Monroe, C.A., Lee, S., Schwartz, M.A., Sang, Q.X. J. Biol. Chem. (2003) [Pubmed]
  11. Matrix metalloproteinase-26 is associated with estrogen-dependent malignancies and targets alpha1-antitrypsin serpin. Li, W., Savinov, A.Y., Rozanov, D.V., Golubkov, V.S., Hedayat, H., Postnova, T.I., Golubkova, N.V., Linli, Y., Krajewski, S., Strongin, A.Y. Cancer Res. (2004) [Pubmed]
  12. Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor. Park, H.I., Ni, J., Gerkema, F.E., Liu, D., Belozerov, V.E., Sang, Q.X. J. Biol. Chem. (2000) [Pubmed]
  13. Matrilysin-2 (matrix metalloproteinase-26) is upregulated in keratinocytes during wound repair and early skin carcinogenesis. Ahokas, K., Skoog, T., Suomela, S., Jeskanen, L., Impola, U., Isaka, K., Saarialho-Kere, U. J. Invest. Dermatol. (2005) [Pubmed]
  14. Beta-catenin regulates the gene of MMP-26, a novel metalloproteinase expressed both in carcinomas and normal epithelial cells. Marchenko, N.D., Marchenko, G.N., Weinreb, R.N., Lindsey, J.D., Kyshtoobayeva, A., Crawford, H.C., Strongin, A.Y. Int. J. Biochem. Cell Biol. (2004) [Pubmed]
  15. Promoter characterization of the novel human matrix metalloproteinase-26 gene: regulation by the T-cell factor-4 implies specific expression of the gene in cancer cells of epithelial origin. Marchenko, G.N., Marchenko, N.D., Leng, J., Strongin, A.Y. Biochem. J. (2002) [Pubmed]
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