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Gene Review

MMP10  -  matrix metallopeptidase 10 (stromelysin 2)

Homo sapiens

Synonyms: MMP-10, Matrix metalloproteinase-10, SL-2, STMY2, Stromelysin-2, ...
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Disease relevance of MMP10

  • The catalytic domain of matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 A resolution [1].
  • MMP-10 was expressed widely in the epithelium of all SCC specimens. alphavbeta6 integrin expression was also detected in some cases of epithelial hyperplasia but was significantly more abundant in cancers at the invasive front [2].
  • In this study, specific cDNA probes for three members of the stromelysin subfamily of MMPs--stromelysin (MMP-3), stromelysin-2 (MMP-10), and pump-1 (MMP-7)--were used to examine the expression of these three different MMPs in human gastric and colonic carcinomas and in adjacent normal mucosa [3].
  • Overexpression of MMP 10 and MMP 11 correlated with higher grade for NSCLC (p = 0.029 and p = 0.016, respectively), and also in a subset of adenocarcinomas (AC) (p = 0.015 and p = 0.009, respectively) [4].
  • Our approach revealed that MMP-10 plays an important role in the recurrence in stage IB lung cancer, irrespective of the histologic type [5].

Psychiatry related information on MMP10


High impact information on MMP10


Biological context of MMP10


Anatomical context of MMP10


Associations of MMP10 with chemical compounds

  • In summary, our work demonstrates that MMP-1 zymogen activation is mediated by multiple serine proteases and MMP-10, and that these events are central to EC-mediated collagen degradation and capillary tube regression in 3D collagen matrices [17].
  • Beta-carotene dose-dependently quenched (1)O(2)-mediated induction of MMP-1 and MMP-10 [18].
  • Multiple alignment analysis of the amino acid sequence revealed that HcSP-1 is most similar to SL-1 from S. litura (73.8% identity) and other methionine-rich hexamers, whereas HcSP-2 is most similar to the SL-2 alpha subunit from S. litura (74.8% identity) and other moderately methionine-rich hexamers [19].
  • The spin labeled acetylcholine analog, SL-2, which is a potent, non-stimulating muscarinic antagonist on the isolated frog heart, is a potent agonist a low concentrations (3x10-5 M) and an antagonist at slightly higher concentrations (4.5x10-5 M) on the mixed cholinergic receptors of the leech [20].
  • The serum concentration of lipid hydroperoxides (LH) increased markedly at rest and after maximal exercise at BC (p < 0.05 vs. SL1/SL2) whereas no changes were observed for plasma malondialdehyde (MDA) [7].

Regulatory relationships of MMP10

  • ECs expressing increased levels of MMP-10 activated MMP-1 to a greater degree than control ECs [17].
  • We also found that 6/8 MM cell lines expressed MMP-7 (matrilysin) and 3/8 MM cell lines expressed MMP-10 (stromelysin-2) [21].
  • The latent SL-2 proenzyme was isolated from 12-O-tetradecanoylphorbol-13-acetate-induced keratinocytes by immunoaffinity chromatography using a cross-reactive antibody raised against human SL-1 [22].

Other interactions of MMP10

  • Comparative studies using zymography and PCR analysis demonstrated differences in MMP-2 and MMP-10 expression between the 3 cultures [23].
  • Invasive properties of fibroblast-like synoviocytes: correlation with growth characteristics and expression of MMP-1, MMP-3, and MMP-10 [24].
  • CXCL12 also significantly increased stromelysin-2 (MMP-10) expression by LNCaP cells [25].
  • In conclusion, our results suggest that ZNF267 as a negative transcriptional regulator of MMP-10 might promote liver fibrogenesis through alteration of matrix degradation in vivo [13].
  • Also, MMP 10 and MMP 11 correlated with lymph node involvement in NSCLC (p = 0.025 and p = 0.027 respectively) [4].

Analytical, diagnostic and therapeutic context of MMP10


  1. Crystal structure of the catalytic domain of human matrix metalloproteinase 10. Bertini, I., Calderone, V., Fragai, M., Luchinat, C., Mangani, S., Terni, B. J. Mol. Biol. (2004) [Pubmed]
  2. 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]
  3. Expression and localization of the matrix metalloproteinase pump-1 (MMP-7) in human gastric and colon carcinomas. McDonnell, S., Navre, M., Coffey, R.J., Matrisian, L.M. Mol. Carcinog. (1991) [Pubmed]
  4. Expression of matrix metalloproteinases 3, 10 and 11 (stromelysins 1, 2 and 3) and matrix metalloproteinase 7 (matrilysin) by cancer cells in non-small cell lung neoplasms. Clinicopathologic studies. Kren, L., Goncharuk, V.N., Krenová, Z., Stratil, D., Hermanová, M., Skricková, J., Sheehan, C.E., Ross, J.S. Ceskoslovenská patologie. (2006) [Pubmed]
  5. MMP expression profiling in recurred stage IB lung cancer. Cho, N.H., Hong, K.P., Hong, S.H., Kang, S., Chung, K.Y., Cho, S.H. Oncogene (2004) [Pubmed]
  6. Redox regulation of matrix metalloproteinase gene family in small cell lung cancer cells. Savaraj, N., Wei, Y., Unate, H., Liu, P.M., Wu, C.J., Wangpaichitr, M., Xia, D., Xu, H.J., Hu, S.X., Tien Kuo, M. Free Radic. Res. (2005) [Pubmed]
  7. A potential role for free radical-mediated skeletal muscle soreness in the pathophysiology of acute mountain sickness. Bailey, D.M., Davies, B., Young, I.S., Hullin, D.A., Seddon, P.S. Aviation, space, and environmental medicine. (2001) [Pubmed]
  8. Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10. Chang, S., Young, B.D., Li, S., Qi, X., Richardson, J.A., Olson, E.N. Cell (2006) [Pubmed]
  9. Muscle-specific expression of SRF-related genes in the early embryo of Xenopus laevis. Chambers, A.E., Kotecha, S., Towers, N., Mohun, T.J. EMBO J. (1992) [Pubmed]
  10. Downstream target genes of the neuropeptide S-NPSR1 pathway. Vendelin, J., Bruce, S., Holopainen, P., Pulkkinen, V., Rytilä, P., Pirskanen, A., Rehn, M., Laitinen, T., Laitinen, L.A., Haahtela, T., Saarialho-Kere, U., Laitinen, A., Kere, J. Hum. Mol. Genet. (2006) [Pubmed]
  11. Matrix metalloproteinases 9 and 10 inhibit protein kinase C-potentiated, p53-mediated apoptosis. Meyer, E., Vollmer, J.Y., Bovey, R., Stamenkovic, I. Cancer Res. (2005) [Pubmed]
  12. Stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) expression in developing human bone: potential roles in skeletal development. Bord, S., Horner, A., Hembry, R.M., Compston, J.E. Bone (1998) [Pubmed]
  13. Zinc finger protein 267 is up-regulated during the activation process of human hepatic stellate cells and functions as a negative transcriptional regulator of MMP-10. Schnabl, B., Hu, K., Mühlbauer, M., Hellerbrand, C., Stefanovic, B., Brenner, D.A., Schölmerich, J. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  14. The SL1-SL2 (Stem-Loop) Domain Is the Primary Determinant for Stability of the Gamma Retroviral Genomic RNA Dimer. Gherghe, C., Weeks, K.M. J. Biol. Chem. (2006) [Pubmed]
  15. Overexpression of matrix metalloproteinase-10 and matrix metalloproteinase-3 in human diabetic corneas: a possible mechanism of basement membrane and integrin alterations. Saghizadeh, M., Brown, D.J., Castellon, R., Chwa, M., Huang, G.H., Ljubimova, J.Y., Rosenberg, S., Spirin, K.S., Stolitenko, R.B., Adachi, W., Kinoshita, S., Murphy, G., Windsor, L.J., Kenney, M.C., Ljubimov, A.V. Am. J. Pathol. (2001) [Pubmed]
  16. Expression of matrix metalloproteinases and their specific inhibitors in normal and different human thyroid tumor cell lines. Baldini, E., Toller, M., Graziano, F.M., Russo, F.P., Pepe, M., Biordi, L., Marchioni, E., Curcio, F., Ulisse, S., Ambesi-Impiombato, F.S., D'Armiento, M. Thyroid (2004) [Pubmed]
  17. MMP-1 activation by serine proteases and MMP-10 induces human capillary tubular network collapse and regression in 3D collagen matrices. Saunders, W.B., Bayless, K.J., Davis, G.E. J. Cell. Sci. (2005) [Pubmed]
  18. Beta-carotene inhibits UVA-induced matrix metalloprotease 1 and 10 expression in keratinocytes by a singlet oxygen-dependent mechanism. Wertz, K., Seifert, N., Hunziker, P.B., Riss, G., Wyss, A., Lankin, C., Goralczyk, R. Free Radic. Biol. Med. (2004) [Pubmed]
  19. Two juvenile hormone suppressible storage proteins may play different roles in Hyphantria cunea Drury. Cheon, H.M., Hwang, S.J., Kim, H.J., Jin, B.R., Chae, K.S., Yun, C.Y., Seo, S.J. Arch. Insect Biochem. Physiol. (2002) [Pubmed]
  20. Effects of spin labeled acetylcholine analogs on cholinergic receptors of the leech. Goldner, M.M., Rosen, G.M. Res. Commun. Chem. Pathol. Pharmacol. (1977) [Pubmed]
  21. Expression and activity of matrix metalloproteases in human malignant mesothelioma cell lines. Liu, Z., Ivanoff, A., Klominek, J. Int. J. Cancer (2001) [Pubmed]
  22. Cell type-specific regulation of SL-1 and SL-2 genes. Induction of the SL-2 gene but not the SL-1 gene by human keratinocytes in response to cytokines and phorbolesters. Windsor, L.J., Grenett, H., Birkedal-Hansen, B., Bodden, M.K., Engler, J.A., Birkedal-Hansen, H. J. Biol. Chem. (1993) [Pubmed]
  23. Metalloproteinase and TIMP expression by the human breast carcinoma cell line 8701-BC. Alessandro, R., Minafra, S., Pucci-Minafra, I., Onisto, M., Garbisa, S., Melchiori, A., Tetlow, L., Woolley, D.E. Int. J. Cancer (1993) [Pubmed]
  24. Invasive properties of fibroblast-like synoviocytes: correlation with growth characteristics and expression of MMP-1, MMP-3, and MMP-10. Tolboom, T.C., Pieterman, E., van der Laan, W.H., Toes, R.E., Huidekoper, A.L., Nelissen, R.G., Breedveld, F.C., Huizinga, T.W. Ann. Rheum. Dis. (2002) [Pubmed]
  25. CXCL12-CXCR4 interactions modulate prostate cancer cell migration, metalloproteinase expression and invasion. Singh, S., Singh, U.P., Grizzle, W.E., Lillard, J.W. Lab. Invest. (2004) [Pubmed]
  26. C-reactive protein induces matrix metalloproteinase-1 and -10 in human endothelial cells: implications for clinical and subclinical atherosclerosis. Montero, I., Orbe, J., Varo, N., Beloqui, O., Monreal, J.I., Rodríguez, J.A., Díez, J., Libby, P., Páramo, J.A. J. Am. Coll. Cardiol. (2006) [Pubmed]
  27. Matrix metalloproteinase 10 promotion of collagenolysis via procollagenase activation: Implications for cartilage degradation in arthritis. Barksby, H.E., Milner, J.M., Patterson, A.M., Peake, N.J., Hui, W., Robson, T., Lakey, R., Middleton, J., Cawston, T.E., Richards, C.D., Rowan, A.D. Arthritis Rheum. (2006) [Pubmed]
  28. Proteinase and growth factor alterations revealed by gene microarray analysis of human diabetic corneas. Saghizadeh, M., Kramerov, A.A., Tajbakhsh, J., Aoki, A.M., Wang, C., Chai, N.N., Ljubimova, J.Y., Sasaki, T., Sosne, G., Carlson, M.R., Nelson, S.F., Ljubimov, A.V. Invest. Ophthalmol. Vis. Sci. (2005) [Pubmed]
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