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MMP11  -  matrix metallopeptidase 11 (stromelysin 3)

Homo sapiens

 
 
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Disease relevance of MMP11

 

High impact information on MMP11

 

Chemical compound and disease context of MMP11

 

Biological context of MMP11

  • These results provide new insights into the function of MMP11 and suggest that MMP11 may play an important role in the control of cell proliferation and tumor development in GC [10].
  • Stable transfection of recombinants into GC cell line BGC823 specifically depleted the mRNA and protein of MMP11 as demonstrated by RT-PCR and Western blotting analysis [10].
  • In order to reveal the correlation between expression of MMP11 and biological features of GC cell, we have constructed the recombinant plasmids producing hairpin small interfering RNA (siRNA) to target MMP11 mRNA using a vector-based RNA interference technology [10].
  • The levels of MMP-11 mRNA were twofold greater in leiomyoma compared with myometrium throughout the menstrual cycle, and the differences in the levels of MMP-11 were significantly different during the secretory phase [4].
  • These findings indicate that the human ST3 gene promoter is characterized by structural and functional features which differ from those previously described in other MMP promoters, and further supports the possibility that ST3 gene expression is controlled by specific factors during tissue remodeling [11].
 

Anatomical context of MMP11

  • MMP-11 was up-regulated in OA chondrocytes and, interestingly, also in the early-stage samples [12].
  • Hepatocyte growth factor receptor, matrix metalloproteinase-11, tissue inhibitor of metalloproteinase-1, and fibronectin are up-regulated in papillary thyroid carcinoma: a cDNA and tissue microarray study [13].
  • In this study, a significant correlation (p < 0.05, by Mann-Whitney U analysis) between TIMP-2 expression and lymph node involvement was identified, while MMP-11 and TIMP-1 expression patterning also significantly (p < 0.05) differed between those tumours showing calcification and those that did not [14].
  • However, the molecular mechanisms leading to ST3 expression in nonmalignant fibroblasts remain unknown [15].
  • Although the intracellular function of the beta-ST3 remains to be investigated, these data support the idea that the functions of MMPs are not restricted to the extracellular space [16].
 

Associations of MMP11 with chemical compounds

  • Transient transfection experiments demonstrated that a minimal promotor activity could be modulated by various sequences within the 3.4 kb of 5'-flanking region, and that the ST3 promoter was transactivated by retinoic acid receptors in the presence of retinoic acid [11].
  • The addition of batimastat, a broad spectrum MMP inhibitor, reversed the increased cell survival in ST3wt transfectants, confirming that ST3 enzymatic activity was required for this effect [17].
  • These reactions also showed that peptides with proline in position 3 were poor substrates for MMP-11 [18].
  • The Xenopus laevis ST3 is highly up-regulated by thyroid hormone (T3) during amphibian metamorphosis, and its expression is spatially and temporally correlated with apoptosis in different tissues [19].
  • The substrate with a S-para-methoxybenzyl cysteine residue in the P1' position displayed a kcat/Km value of 1.59 10(6) M-1 s-1 and 1.67 10(4) M-1 s-1, when assayed with MT1-MMP and ST3, respectively [20].
 

Regulatory relationships of MMP11

  • In a second approach, TIMP2 overproduction in MCF7 cells expressing hST3 was induced by retroviral infection [21].
  • Finally, a tetracycline-inducible expression model allowed us to confirm the central role of these PKC isoforms and the negative regulatory function of c-Src in the control of ST3 expression [15].
  • The MIB-1 proliferation index was significantly higher in the meningiomas expressing ST3 (Student t test: P < 0.001) [22].
  • Finally, we show that processing of the ST3 proform is inhibited by a furin inhibitor in human MCF7 breast cancer cells stably transfected to constitutively express a full-length human ST3 cDNA [23].
  • MEK inhibitor PD98059 and MMP11 antibody (Ab) significantly inhibited in vitro invasive and in vivo metastatic abilities induced by PrPc [24].
 

Other interactions of MMP11

  • This indicates that other degradation pathways might be more important in late stages of cartilage degeneration, involving other enzymes, such as MMP-2 and MMP-11, both of which were up-regulated in late-stage disease [12].
  • A cell line immortalized following myc expression was found to up-regulate MMP-7, MMP-11 and MMP-13 [25].
  • Kaplan-Meier survival analysis showed that patients with ST-3-positive and TIMP-2-negative carcinoma had a significantly shorter disease-free survival (median disease-free survival time of 4 months) as compared to patients in the other groups (median disease-free survival time of 20 months; p = 0.0016) [26].
  • Based on detection of either MMP-9 or MMP-11 mRNAs, we were able to distinguish between malignant and benign disease with a predictive accuracy of 90% with 94% sensitivity and 85% specificity [27].
  • The genes TIMP3 and PVALB were assigned to BTA5 and CRYbetaA4 and MMP11 to BTA17 [28].
 

Analytical, diagnostic and therapeutic context of MMP11

References

  1. Regulation of lung cancer cell growth and invasiveness by beta-TRCP. He, N., Li, C., Zhang, X., Sheng, T., Chi, S., Chen, K., Wang, Q., Vertrees, R., Logrono, R., Xie, J. Mol. Carcinog. (2005) [Pubmed]
  2. Substrate specificity of Xenopus matrix metalloproteinase stromelysin-3. Amano, T., Fu, L., Sahu, S., Markey, M., Shi, Y.B. Int. J. Mol. Med. (2004) [Pubmed]
  3. Expression and prognostic significance of metalloproteinases and their tissue inhibitors in patients with small-cell lung cancer. Michael, M., Babic, B., Khokha, R., Tsao, M., Ho, J., Pintilie, M., Leco, K., Chamberlain, D., Shepherd, F.A. J. Clin. Oncol. (1999) [Pubmed]
  4. Increased expression of stromelysin 3 mRNA in leiomyomas (uterine fibroids) compared with myometrium. Palmer, S.S., Haynes-Johnson, D., Diehl, T., Nowak, R.A. J. Soc. Gynecol. Investig. (1998) [Pubmed]
  5. Identification of matrix metalloproteinase 11 as a predictive tumor marker in serum based on gene expression profiling. Yang, Y.H., Deng, H., Li, W.M., Zhang, Q.Y., Hu, X.T., Xiao, B., Zhu, H.H., Geng, P.L., Lu, Y.Y. Clin. Cancer Res. (2008) [Pubmed]
  6. Requirement for matrix metalloproteinase stromelysin-3 in cell migration and apoptosis during tissue remodeling in Xenopus laevis. Ishizuya-Oka, A., Li, Q., Amano, T., Damjanovski, S., Ueda, S., Shi, Y.B. J. Cell Biol. (2000) [Pubmed]
  7. Stromelysin 3 belongs to a subgroup of proteinases expressed in breast carcinoma fibroblastic cells and possibly implicated in tumor progression. Wolf, C., Rouyer, N., Lutz, Y., Adida, C., Loriot, M., Bellocq, J.P., Chambon, P., Basset, P. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  8. Evaluation of P1'-diversified phosphinic peptides leads to the development of highly selective inhibitors of MMP-11. Matziari, M., Beau, F., Cuniasse, P., Dive, V., Yiotakis, A. J. Med. Chem. (2004) [Pubmed]
  9. The expression of matrix metalloproteinase-11 protein in various types of glomerulonephritis. Nakopoulou, L., Lazaris, A.C., Boletis, I., Michail, S., Iatrou, C., Papadakis, G., Athanassiadou, S., Stathakis, C. Nephrol. Dial. Transplant. (2007) [Pubmed]
  10. Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells. Deng, H., Guo, R.F., Li, W.M., Zhao, M., Lu, Y.Y. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  11. Structure and promoter characterization of the human stromelysin-3 gene. Anglard, P., Melot, T., Guérin, E., Thomas, G., Basset, P. J. Biol. Chem. (1995) [Pubmed]
  12. Anabolic and catabolic gene expression pattern analysis in normal versus osteoarthritic cartilage using complementary DNA-array technology. Aigner, T., Zien, A., Gehrsitz, A., Gebhard, P.M., McKenna, L. Arthritis Rheum. (2001) [Pubmed]
  13. Hepatocyte growth factor receptor, matrix metalloproteinase-11, tissue inhibitor of metalloproteinase-1, and fibronectin are up-regulated in papillary thyroid carcinoma: a cDNA and tissue microarray study. Wasenius, V.M., Hemmer, S., Kettunen, E., Knuutila, S., Franssila, K., Joensuu, H. Clin. Cancer Res. (2003) [Pubmed]
  14. An assessment of MMP and TIMP gene expression in cell lines and stroma - tumour differences in microdissected breast cancer biopsies. Mellick, A.S., Blackmore, D., Weinstein, S.R., Griffiths, L.R. Tumour Biol. (2003) [Pubmed]
  15. Tumor cell-mediated induction of the stromal factor stromelysin-3 requires heterotypic cell contact-dependent activation of specific protein kinase C isoforms. Louis, K., Guérineau, N., Fromigué, O., Defamie, V., Collazos, A., Anglard, P., Shipp, M.A., Auberger, P., Joubert, D., Mari, B. J. Biol. Chem. (2005) [Pubmed]
  16. Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase. Luo, D., Mari, B., Stoll, I., Anglard, P. J. Biol. Chem. (2002) [Pubmed]
  17. Active stromelysin-3 (MMP-11) increases MCF-7 survival in three-dimensional Matrigel culture via activation of p42/p44 MAP-kinase. Fromigué, O., Louis, K., Wu, E., Belhacène, N., Loubat, A., Shipp, M., Auberger, P., Mari, B. Int. J. Cancer (2003) [Pubmed]
  18. Identification of peptide substrates for human MMP-11 (stromelysin-3) using phage display. Pan, W., Arnone, M., Kendall, M., Grafstrom, R.H., Seitz, S.P., Wasserman, Z.R., Albright, C.F. J. Biol. Chem. (2003) [Pubmed]
  19. Transcriptional regulation of the Xenopus laevis Stromelysin-3 gene by thyroid hormone is mediated by a DNA element in the first intron. Fu, L., Tomita, A., Wang, H., Buchholz, D.R., Shi, Y.B. J. Biol. Chem. (2006) [Pubmed]
  20. Membrane type-1 matrix metalloprotease and stromelysin-3 cleave more efficiently synthetic substrates containing unusual amino acids in their P1' positions. Mucha, A., Cuniasse, P., Kannan, R., Beau, F., Yiotakis, A., Basset, P., Dive, V. J. Biol. Chem. (1998) [Pubmed]
  21. Demonstration in vivo that stromelysin-3 functions through its proteolytic activity. Noël, A., Boulay, A., Kebers, F., Kannan, R., Hajitou, A., Calberg-Bacq, C.M., Basset, P., Rio, M.C., Foidart, J.M. Oncogene (2000) [Pubmed]
  22. Stromelysin-3 is expressed by aggressive meningiomas. Perret, A.G., Duthel, R., Fotso, M.J., Brunon, J., Mosnier, J.F. Cancer (2002) [Pubmed]
  23. Characterization of structural determinants and molecular mechanisms involved in pro-stromelysin-3 activation by 4-aminophenylmercuric acetate and furin-type convertases. Santavicca, M., Noel, A., Angliker, H., Stoll, I., Segain, J.P., Anglard, P., Chretien, M., Seidah, N., Basset, P. Biochem. J. (1996) [Pubmed]
  24. Cellular prion protein promotes invasion and metastasis of gastric cancer. Pan, Y., Zhao, L., Liang, J., Liu, J., Shi, Y., Liu, N., Zhang, G., Jin, H., Gao, J., Xie, H., Wang, J., Liu, Z., Fan, D. FASEB J. (2006) [Pubmed]
  25. Overview of matrix metalloproteinase expression in cultured human cells. Giambernardi, T.A., Grant, G.M., Taylor, G.P., Hay, R.J., Maher, V.M., McCormick, J.J., Klebe, R.J. Matrix Biol. (1998) [Pubmed]
  26. Prognostic significance of stromelysin-3 and tissue inhibitor of matrix metalloproteinase-2 in esophageal cancer. Sharma, R., Chattopadhyay, T.K., Mathur, M., Ralhan, R. Oncology (2004) [Pubmed]
  27. Comparative analysis of the expression patterns of metalloproteinases and their inhibitors in breast neoplasia, sporadic colorectal neoplasia, pulmonary carcinomas and malignant non-Hodgkin's lymphomas in humans. Kossakowska, A.E., Huchcroft, S.A., Urbanski, S.J., Edwards, D.R. Br. J. Cancer (1996) [Pubmed]
  28. The assignment by linkage mapping of four genes from human chromosome 22 to bovine chromosome 5 and 17. Ariza, F., Harrison, B., Drinkwater, R.D. Anim. Genet. (2001) [Pubmed]
  29. Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer. Vazquez-Ortiz, G., Pina-Sanchez, P., Vazquez, K., Duenas, A., Taja, L., Mendoza, P., Garcia, J.A., Salcedo, M. BMC Cancer (2005) [Pubmed]
  30. Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22. Levy, A., Zucman, J., Delattre, O., Mattei, M.G., Rio, M.C., Basset, P. Genomics (1992) [Pubmed]
  31. Stimulation of MMP-11 (stromelysin-3) expression in mouse fibroblasts by cytokines, collagen and co-culture with human breast cancer cell lines. Selvey, S., Haupt, L.M., Thompson, E.W., Matthaei, K.I., Irving, M.G., Griffiths, L.R. BMC Cancer (2004) [Pubmed]
 
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