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MMP19  -  matrix metallopeptidase 19

Homo sapiens

Synonyms: MMP-18, MMP-19, MMP18, Matrix metalloproteinase RASI, Matrix metalloproteinase-18, ...
 
 
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Disease relevance of MMP19

  • The cDNA encoding a full-length MMP-19 was expressed in Escherichia coli, and after purification and refolding, the recombinant protein was able to degrade synthetic substrates for MMPs [1].
  • MMP-19 was expressed by epithelial keratinocytes in hyperproliferative areas of verrucous hyperplasia, VC, and SCC, but was absent in the invasive cancer cell nests of SCC [2].
  • Our aim was to study the putative role of MMP-19 in skin cancer [3].
  • MMP-19 (also designated RASI) is a recently discovered member of a large family of zinc-dependent proteolytic enzymes, most of which have been implicated in cancer growth and metastasis [3].
  • No MMP-19 mRNA was detected by Northern analysis in cultured HaCaT or A5 cells or in an SCC cell line established from head-and-neck cancer [3].
 

High impact information on MMP19

  • In an attempt to give new insights into MMP-19 in vivo functions, angiogenic response of mutant mice lacking MMP-19 was analyzed after transplantation of murine malignant PDVA keratinocytes and after injection of Matrigel supplemented with basic fibroblast growth factor [4].
  • Among matrix metalloproteinases (MMP), MMP-19 displays unique structural features and tissue distribution [4].
  • Conversely, these effects were not observed in cells transfected with MMP-2 or a catalytically inactive MMP-19 mutant [5].
  • Calcium-regulation occurred through E-cadherin mediated cell-cell contacts because neutralizing anti-E-cadherin antibodies restored MMP-19 expression in high calcium [5].
  • This was due to proteolysis of the insulin-like growth factor (IGF) binding protein-3 by MMP-19, which augmented signaling through the IGF-I receptor, as evidenced by its increased autophosphorylation [5].
 

Biological context of MMP19

 

Anatomical context of MMP19

  • Unlike most other matrix metalloproteinases (MMPs) MMP-19 is expressed in undifferentiated basal keratinocytes of healthy human skin [5].
  • The human keratinocyte cell line HaCaT, which like basal keratinocytes constitutively expresses MMP-19, down-regulated the expression of MMP-19 at high calcium concentrations [5].
  • Whereas MMP-19 mRNA is found widely expressed in body tissues, including the synovium of normal and rheumatoid arthritic patients, MMP-20 expression is restricted to the enamel organ [8].
  • We have shown that MMP-19 associates with the cell surface of myeloid cells [9].
  • Northern blot analysis of polyadenylated RNAs isolated from a variety of human tissues revealed that MMP-19 is mainly expressed in placenta, lung, pancreas, ovary, spleen, and intestine, suggesting that it may play a specialized role in these tissues [1].
 

Associations of MMP19 with chemical compounds

  • Strikingly, a homologously inserted cysteine is also found in Xenopus XMMP and human MMP19, two recently cloned novel members of the MMP family [6].
  • MMP-19 proteolytic activity was abolished by TIMP-2 and EDTA, thus providing additional evidence that the isolated cDNA codes for an authentic MMP [1].
  • We have recently cloned MMP-19, a novel matrix metalloproteinase, which, due to unique structural features, was proposed to represent the first member of a new MMP subfamily (Pendás, A. M., Knäuper, V. , Puente, X. S., Llano, E., Mattei, M. G., Apte, S., Murphy, G., and López-Otin, C. (1997) J. Biol. Chem. 272, 4281-4286) [7].
  • These data suggest that the MMP-19-dependent processing of the gamma2 chains leads to the integrin switch favoring epithelial migration and that MMP-19 actively participates in the early stages of SCC invasion [10].
  • The constitutive expression of MMP-19 was upregulated with phorbol myristate acetate and downregulated with retinoic acid and dexamethasone [11].
 

Physical interactions of MMP19

 

Enzymatic interactions of MMP19

 

Regulatory relationships of MMP19

 

Other interactions of MMP19

  • Matrilysins-1 and -2 (MMP-7 and -26) and metalloelastase (MMP-12), unlike MMP-19, are up-regulated in necrotizing enterocolitis [16].
  • RASI-1, although its function and substrates are unknown, could be involved in processes such as neovascularization and angiogenesis or lymphocyte extravasation and thus may participate in joint tissue destruction during RA [14].
  • The tissue inhibitor of metalloproteinases (TIMP-1), although also widely expressed in the synovium, exhibits strong colocalization with RASI-1 in blood vessel walls [14].
  • The matrixmetalloproteinase-19 (MMP-19) belongs to the superfamily of the zinc-dependent endopeptidases, which are secreted by cells and are involved in the remodeling of the extracellular matrix [17].
  • We show that the hemopexin-like domain of MMP-19 is able to bind calcium and this binding induces a conformational change and an increase in the thermal stability of the domain [17].
 

Analytical, diagnostic and therapeutic context of MMP19

References

  1. Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution. Pendás, A.M., Knäuper, V., Puente, X.S., Llano, E., Mattei, M.G., Apte, S., Murphy, G., López-Otín, C. J. Biol. Chem. (1997) [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. Matrix metalloproteinase-19 is expressed by proliferating epithelium but disappears with neoplastic dedifferentiation. Impola, U., Toriseva, M., Suomela, S., Jeskanen, L., Hieta, N., Jahkola, T., Grenman, R., Kähäri, V.M., Saarialho-Kere, U. Int. J. Cancer (2003) [Pubmed]
  4. Earlier onset of tumoral angiogenesis in matrix metalloproteinase-19-deficient mice. Jost, M., Folgueras, A.R., Frérart, F., Pendas, A.M., Blacher, S., Houard, X., Berndt, S., Munaut, C., Cataldo, D., Alvarez, J., Melen-Lamalle, L., Foidart, J.M., López-Otín, C., Noël, A. Cancer Res. (2006) [Pubmed]
  5. Matrix metalloproteinase 19 regulates insulin-like growth factor-mediated proliferation, migration, and adhesion in human keratinocytes through proteolysis of insulin-like growth factor binding protein-3. Sadowski, T., Dietrich, S., Koschinsky, F., Sedlacek, R. Mol. Biol. Cell (2003) [Pubmed]
  6. Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain. Yang, M., Kurkinen, M. J. Biol. Chem. (1998) [Pubmed]
  7. Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme. Stracke, J.O., Hutton, M., Stewart, M., Pendás, A.M., Smith, B., López-Otin, C., Murphy, G., Knäuper, V. J. Biol. Chem. (2000) [Pubmed]
  8. Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP). Stracke, J.O., Fosang, A.J., Last, K., Mercuri, F.A., Pendás, A.M., Llano, E., Perris, R., Di Cesare, P.E., Murphy, G., Knäuper, V. FEBS Lett. (2000) [Pubmed]
  9. Matrix metalloproteinase-19 is expressed in myeloid cells in an adhesion-dependent manner and associates with the cell surface. Mauch, S., Kolb, C., Kolb, B., Sadowski, T., Sedlacek, R. J. Immunol. (2002) [Pubmed]
  10. Matrix metalloproteinase 19 processes the laminin 5 gamma 2 chain and induces epithelial cell migration. Sadowski, T., Dietrich, S., Koschinsky, F., Ludwig, A., Proksch, E., Titz, B., Sedlacek, R. Cell. Mol. Life Sci. (2005) [Pubmed]
  11. Matrix metalloproteinase-19 expression in normal and diseased skin: dysregulation by epidermal proliferation. Sadowski, T., Dietrich, S., Müller, M., Havlickova, B., Schunck, M., Proksch, E., Müller, M.S., Sedlacek, R. J. Invest. Dermatol. (2003) [Pubmed]
  12. Matrix metalloproteinase MMP-19 (RASI-1) is expressed on the surface of activated peripheral blood mononuclear cells and is detected as an autoantigen in rheumatoid arthritis. Sedlacek, R., Mauch, S., Kolb, B., Schätzlein, C., Eibel, H., Peter, H.H., Schmitt, J., Krawinkel, U. Immunobiology (1998) [Pubmed]
  13. Activity of MMP-19 inhibits capillary-like formation due to processing of nidogen-1. Titz, B., Dietrich, S., Sadowski, T., Beck, C., Petersen, A., Sedlacek, R. Cell. Mol. Life Sci. (2004) [Pubmed]
  14. The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient. Kolb, C., Mauch, S., Peter, H.H., Krawinkel, U., Sedlacek, R. Immunol. Lett. (1997) [Pubmed]
  15. MMP-19: cellular localization of a novel metalloproteinase within normal breast tissue and mammary gland tumours. Djonov, V., Högger, K., Sedlacek, R., Laissue, J., Draeger, A. J. Pathol. (2001) [Pubmed]
  16. Matrilysins-1 and -2 (MMP-7 and -26) and metalloelastase (MMP-12), unlike MMP-19, are up-regulated in necrotizing enterocolitis. Bister, V., Salmela, M.T., Heikkilä, P., Anttila, A., Rintala, R., Isaka, K., Andersson, S., Saarialho-Kere, U. J. Pediatr. Gastroenterol. Nutr. (2005) [Pubmed]
  17. Structural characterization and binding properties of the hemopexin-like domain of the matrixmetalloproteinase-19. Mysliwy, J., Dingley, A.J., Sedlacek, R., Grötzinger, J. Protein Expr. Purif. (2006) [Pubmed]
  18. Transformation-specific matrix metalloproteinases, MMP-7 and MMP-13, are present in epithelial cells of keratoacanthomas. Kuivanen, T.T., Jeskanen, L., Kyllönen, L., Impola, U., Saarialho-Kere, U.K. Mod. Pathol. (2006) [Pubmed]
  19. Matrix metalloproteinase-19 in capillary endothelial cells: expression in acutely, but not in chronically, inflamed synovium. Kolb, C., Mauch, S., Krawinkel, U., Sedlacek, R. Exp. Cell Res. (1999) [Pubmed]
  20. Matrix metalloproteinase-19 expression in dermal wounds and by fibroblasts in culture. Hieta, N., Impola, U., López-Otín, C., Saarialho-Kere, U., Kähäri, V.M. J. Invest. Dermatol. (2003) [Pubmed]
 
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