Matrix metallopeptidase 11 (stromelysin 3), also known as MMP11, is a human gene.cite web | title = Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)| url =| accessdate = ]

section_title =
summary_text = 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.cite web | title = Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)| url =| accessdate = ]


Further reading

citations =
*cite journal | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=
*cite journal | author=Levy A, Zucman J, Delattre O, "et al." |title=Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22. |journal=Genomics |volume=13 |issue= 3 |pages= 881–3 |year= 1992 |pmid= 1639418 |doi=
*cite journal | author=Basset P, Bellocq JP, Wolf C, "et al." |title=A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas. |journal=Nature |volume=348 |issue= 6303 |pages= 699–704 |year= 1991 |pmid= 1701851 |doi= 10.1038/348699a0
*cite journal | author=Pei D, Majmudar G, Weiss SJ |title=Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3. |journal=J. Biol. Chem. |volume=269 |issue= 41 |pages= 25849–55 |year= 1994 |pmid= 7523394 |doi=
*cite journal | author=Anglard P, Melot T, Guérin E, "et al." |title=Structure and promoter characterization of the human stromelysin-3 gene. |journal=J. Biol. Chem. |volume=270 |issue= 35 |pages= 20337–44 |year= 1995 |pmid= 7657606 |doi=
*cite journal | author=Pei D, Weiss SJ |title=Furin-dependent intracellular activation of the human stromelysin-3 zymogen. |journal=Nature |volume=375 |issue= 6528 |pages= 244–7 |year= 1995 |pmid= 7746327 |doi= 10.1038/375244a0
*cite journal | author=Boulay A, Masson R, Chenard MP, "et al." |title=High cancer cell death in syngeneic tumors developed in host mice deficient for the stromelysin-3 matrix metalloproteinase. |journal=Cancer Res. |volume=61 |issue= 5 |pages= 2189–93 |year= 2001 |pmid= 11280785 |doi=
*cite journal | author=Perret AG, Duthel R, Fotso MJ, "et al." |title=Stromelysin-3 is expressed by aggressive meningiomas. |journal=Cancer |volume=94 |issue= 3 |pages= 765–72 |year= 2002 |pmid= 11857311 |doi=
*cite journal | author=Luo D, Mari B, Stoll I, Anglard P |title=Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25527–36 |year= 2002 |pmid= 12006591 |doi= 10.1074/jbc.M202494200
*cite journal | author=Nakopoulou L, Panayotopoulou EG, Giannopoulou I, "et al." |title=Stromelysin-3 protein expression in invasive breast cancer: relation to proliferation, cell survival and patients' outcome. |journal=Mod. Pathol. |volume=15 |issue= 11 |pages= 1154–61 |year= 2003 |pmid= 12429794 |doi= 10.1097/01.MP.0000037317.84782.CD
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Wasenius VM, Hemmer S, Kettunen E, "et al." |title=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. |journal=Clin. Cancer Res. |volume=9 |issue= 1 |pages= 68–75 |year= 2003 |pmid= 12538453 |doi=
*cite journal | author=Fromigué O, Louis K, Wu E, "et al." |title=Active stromelysin-3 (MMP-11) increases MCF-7 survival in three-dimensional Matrigel culture via activation of p42/p44 MAP-kinase. |journal=Int. J. Cancer |volume=106 |issue= 3 |pages= 355–63 |year= 2003 |pmid= 12845673 |doi= 10.1002/ijc.11232
*cite journal | author=Skoglund J, Emterling A, Arbman G, "et al." |title=Clinicopathological significance of stromelysin-3 expression in colorectal cancer. |journal=Oncology |volume=67 |issue= 1 |pages= 67–72 |year= 2004 |pmid= 15459498 |doi= 10.1159/000080288
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Louis K, Guérineau N, Fromigué O, "et al." |title=Tumor cell-mediated induction of the stromal factor stromelysin-3 requires heterotypic cell contact-dependent activation of specific protein kinase C isoforms. |journal=J. Biol. Chem. |volume=280 |issue= 2 |pages= 1272–83 |year= 2005 |pmid= 15509588 |doi= 10.1074/jbc.M405482200
*cite journal | author=Deng H, Guo RF, Li WM, "et al." |title=Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells. |journal=Biochem. Biophys. Res. Commun. |volume=326 |issue= 2 |pages= 274–81 |year= 2005 |pmid= 15582574 |doi= 10.1016/j.bbrc.2004.11.027
*cite journal | author=Arora S, Kaur J, Sharma C, "et al." |title=Stromelysin 3, Ets-1, and vascular endothelial growth factor expression in oral precancerous and cancerous lesions: correlation with microvessel density, progression, and prognosis. |journal=Clin. Cancer Res. |volume=11 |issue= 6 |pages= 2272–84 |year= 2005 |pmid= 15788677 |doi= 10.1158/1078-0432.CCR-04-0572
*cite journal | author=Vazquez-Ortiz G, Pina-Sanchez P, Vazquez K, "et al." |title=Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer. |journal=BMC Cancer |volume=5 |issue= 1 |pages= 68 |year= 2006 |pmid= 15989693 |doi= 10.1186/1471-2407-5-68

update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes

Wikimedia Foundation. 2010.

Look at other dictionaries:

  • Matrix metalloproteinase — Cell surface associated MT1 MMP (MMP14), Green fluorescent protein (GFP) fused to the C term produces a signal on the surface of the cell[1] Matrix metalloproteinases (MMPs) are zinc dependent endopeptidases; other family members are adamalysins …   Wikipedia

  • Metalloendopeptidase — A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase. External links MeSH Metalloendopeptidase 3.4.21 24: Endopeptidase …   Wikipedia

  • Collagenase — matrix metallopeptidase 1 (interstitial collagenase) Identifiers Symbol MMP1 Entrez 4312 HUGO …   Wikipedia

  • ADAM17 — ADAM metallopeptidase domain 17 PDB rendering based on 1bkc …   Wikipedia

  • Neprilysin — Membrane metallo endopeptidase The structure of the neprilysin ectodomain in complex with a zinc chelating inhibitor. The zinc atom is shown as a gray sphere and the inhibitor is shown in green. Rendering based on 1r1h …   Wikipedia

  • Pregnancy-associated plasma protein A — Pregnancy associated plasma protein A, pappalysin 1 Identifiers Symbols PAPPA; ASBABP2; DIPLA1; IGFBP 4ase; PAPA; PAPP A; PAPPA1 External IDs …   Wikipedia

  • MMP14 — Matrix metallopeptidase 14 (membrane inserted) PDB rendering based on 1bqq …   Wikipedia

  • MMP1 — Matrix metallopeptidase 1 (interstitial collagenase) PDB rendering based on 1ayk …   Wikipedia

  • MMP3 — Matrix metallopeptidase 3 (stromelysin 1, progelatinase) PDB rendering based on 1b3d …   Wikipedia

  • MMP7 — Matrix metallopeptidase 7 (matrilysin, uterine) PDB rendering based on 1mmp …   Wikipedia