MMP11

Matrix metallopeptidase 11 (stromelysin 3)

PDB rendering based on 1hv5.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsMMP11 ; SL-3; ST3; STMY3
External IDsOMIM: 185261 MGI: 97008 HomoloGene: 38116 IUPHAR: 1635 ChEMBL: 2867 GeneCards: MMP11 Gene
EC number3.4.24.-
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez432017385
EnsemblENSG00000099953ENSMUSG00000000901
UniProtP24347Q02853
RefSeq (mRNA)NM_005940NM_008606
RefSeq (protein)NP_005931NP_032632
Location (UCSC)Chr 22:
24.11 – 24.13 Mb		Chr 10:
75.92 – 75.93 Mb
PubMed search

Stromelysin-3 (SL-3) also known as matrix metalloproteinase-11 (MMP-11) is an enzyme that in humans is encoded by the MMP11 gene.[1][2][3][4]

Function

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.[4]

References

  1. ↑ Levy A, Zucman J, Delattre O, Mattei MG, Rio MC, Basset P (Aug 1992). "Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22". Genomics 13 (3): 881–3. doi:10.1016/0888-7543(92)90175-R. PMID 1639418.
  2. ↑ Anglard P, Melot T, Guerin E, Thomas G, Basset P (Oct 1995). "Structure and promoter characterization of the human stromelysin-3 gene". J Biol Chem 270 (35): 20337–44. doi:10.1074/jbc.270.35.20337. PMID 7657606.
  3. ↑ Luo D, Mari B, Stoll I, Anglard P (Jul 2002). "Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase". J Biol Chem 277 (28): 25527–36. doi:10.1074/jbc.M202494200. PMID 12006591.
  4. ↑ 4.0 4.1 "Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)".

Further reading

  • Nagase H, Woessner JF (1999). "Matrix metalloproteinases.". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
  • Basset P, Bellocq JP, Wolf C et al. (1991). "A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas.". Nature 348 (6303): 699–704. doi:10.1038/348699a0. PMID 1701851.
  • Pei D, Majmudar G, Weiss SJ (1994). "Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3.". J. Biol. Chem. 269 (41): 25849–55. PMID 7523394.
  • Pei D, Weiss SJ (1995). "Furin-dependent intracellular activation of the human stromelysin-3 zymogen.". Nature 375 (6528): 244–7. doi:10.1038/375244a0. PMID 7746327.
  • Boulay A, Masson R, Chenard MP et al. (2001). "High cancer cell death in syngeneic tumors developed in host mice deficient for the stromelysin-3 matrix metalloproteinase.". Cancer Res. 61 (5): 2189–93. PMID 11280785.
  • Perret AG, Duthel R, Fotso MJ et al. (2002). "Stromelysin-3 is expressed by aggressive meningiomas.". Cancer 94 (3): 765–72. doi:10.1002/cncr.10270. PMID 11857311.
  • Nakopoulou L, Panayotopoulou EG, Giannopoulou I et al. (2003). "Stromelysin-3 protein expression in invasive breast cancer: relation to proliferation, cell survival and patients' outcome.". Mod. Pathol. 15 (11): 1154–61. doi:10.1097/01.MP.0000037317.84782.CD. PMID 12429794.
  • Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Wasenius VM, Hemmer S, Kettunen E et al. (2003). "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.". Clin. Cancer Res. 9 (1): 68–75. PMID 12538453.
  • Fromigué O, Louis K, Wu E et al. (2003). "Active stromelysin-3 (MMP-11) increases MCF-7 survival in three-dimensional Matrigel culture via activation of p42/p44 MAP-kinase.". Int. J. Cancer 106 (3): 355–63. doi:10.1002/ijc.11232. PMID 12845673.
  • Skoglund J, Emterling A, Arbman G et al. (2004). "Clinicopathological significance of stromelysin-3 expression in colorectal cancer.". Oncology 67 (1): 67–72. doi:10.1159/000080288. PMID 15459498.
  • Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Louis K, Guérineau N, Fromigué O et al. (2005). "Tumor cell-mediated induction of the stromal factor stromelysin-3 requires heterotypic cell contact-dependent activation of specific protein kinase C isoforms.". J. Biol. Chem. 280 (2): 1272–83. doi:10.1074/jbc.M405482200. PMID 15509588.
  • Deng H, Guo RF, Li WM et al. (2005). "Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells.". Biochem. Biophys. Res. Commun. 326 (2): 274–81. doi:10.1016/j.bbrc.2004.11.027. PMID 15582574.
  • Arora S, Kaur J, Sharma C et al. (2005). "Stromelysin 3, Ets-1, and vascular endothelial growth factor expression in oral precancerous and cancerous lesions: correlation with microvessel density, progression, and prognosis.". Clin. Cancer Res. 11 (6): 2272–84. doi:10.1158/1078-0432.CCR-04-0572. PMID 15788677.
  • Vazquez-Ortiz G, Pina-Sanchez P, Vazquez K et al. (2006). "Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer.". BMC Cancer 5: 68. doi:10.1186/1471-2407-5-68. PMC 1175083. PMID 15989693.