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{{Infobox_gene}}
'''Stromelysin-3''' (SL-3) also known as '''matrix metalloproteinase-11''' (MMP-11) is an [[enzyme]] that in humans is encoded by the ''MMP11'' [[gene]].<ref name="pmid1639418">{{cite journal |vauthors=Levy A, Zucman J, Delattre O, Mattei MG, Rio MC, Basset P | 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 |date=Aug 1992 | pmid = 1639418 | pmc =  | doi =10.1016/0888-7543(92)90175-R  }}</ref><ref name="pmid7657606">{{cite journal |vauthors=Anglard P, Melot T, Guerin E, Thomas G, Basset P | title = Structure and promoter characterization of the human stromelysin-3 gene | journal = J Biol Chem | volume = 270 | issue = 35 | pages = 20337–44 |date=Oct 1995 | pmid = 7657606 | pmc =  | doi =10.1074/jbc.270.35.20337  }}</ref><ref name="pmid12006591">{{cite journal |vauthors=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 |date=Jul 2002 | pmid = 12006591 | pmc =  | doi = 10.1074/jbc.M202494200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4320| accessdate = }}</ref>
== Function ==
Proteins of the matrix metalloproteinase ([[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-antitrypsin|alpha 1-proteinase inhibitor]] but weakly degrades structural proteins of the extracellular matrix.<ref name="entrez"/>
== References ==
{{reflist}}
== Further reading ==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  |vauthors=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=10.1074/jbc.274.31.21491  }}
*{{cite journal  |vauthors=Basset P, Bellocq JP, Wolf C, etal |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  |vauthors=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  |vauthors=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 |url=https://deepblue.lib.umich.edu/bitstream/2027.42/62522/1/375244a0.pdf }}
*{{cite journal  |vauthors=Boulay A, Masson R, Chenard MP, etal |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  |vauthors=Perret AG, Duthel R, Fotso MJ, etal |title=Stromelysin-3 is expressed by aggressive meningiomas. |journal=Cancer |volume=94 |issue= 3 |pages= 765–72 |year= 2002 |pmid= 11857311 |doi=10.1002/cncr.10270  }}
*{{cite journal  |vauthors=Nakopoulou L, Panayotopoulou EG, Giannopoulou I, etal |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  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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  | pmc=139241 }}
*{{cite journal  |vauthors=Wasenius VM, Hemmer S, Kettunen E, etal |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  |vauthors=Fromigué O, Louis K, Wu E, etal |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  |vauthors=Skoglund J, Emterling A, Arbman G, etal |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  |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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  | pmc=528928 }}
*{{cite journal  |vauthors=Louis K, Guérineau N, Fromigué O, etal |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  |vauthors=Deng H, Guo RF, Li WM, etal |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  |vauthors=Arora S, Kaur J, Sharma C, etal |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  |vauthors=Vazquez-Ortiz G, Pina-Sanchez P, Vazquez K, etal |title=Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer. |journal=BMC Cancer |volume=5 |pages= 68 |year= 2006 |pmid= 15989693 |doi= 10.1186/1471-2407-5-68  | pmc=1175083 }}
}}
{{refend}}
{{PDB Gallery|geneid=4320}}
{{Metalloendopeptidases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Category:Matrix metalloproteinases]]
{{GNF_Protein_box
[[Category:EC 3.4.24]]
| image = PBB_Protein_MMP11_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hv5.
| PDB = {{PDB2|1hv5}}
| Name = Matrix metallopeptidase 11 (stromelysin 3)
| HGNCid = 7157
| Symbol = MMP11
| AltSymbols =; SL-3; ST3; STMY3
| OMIM = 185261
| ECnumber = 
| Homologene = 38116
| MGIid = 97008
| GeneAtlas_image1 = PBB_GE_MMP11_203878_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MMP11_203876_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004249 |text = stromelysin 3 activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0030574 |text = collagen catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4320
    | Hs_Ensembl = ENSG00000099953
    | Hs_RefseqProtein = NP_005931
    | Hs_RefseqmRNA = NM_005940
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 22
    | Hs_GenLoc_start = 22445036
    | Hs_GenLoc_end = 22456502
    | Hs_Uniprot = P24347
    | Mm_EntrezGene = 17385
    | Mm_Ensembl = ENSMUSG00000000901
    | Mm_RefseqmRNA = NM_008606
    | Mm_RefseqProtein = NP_032632
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 75366940
    | Mm_GenLoc_end = 75376185
    | Mm_Uniprot = Q3UQT3
  }}
}}
'''Matrix metallopeptidase 11 (stromelysin 3)''', also known as '''MMP11''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4320| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| 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.<ref name="entrez">{{cite web | title = Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4320| accessdate = }}</ref>
}}
==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_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 }}
}}
{{refend}}


{{gene-22-stub}}
{{gene-22-stub}}
{{WikiDoc Sources}}

Latest revision as of 12:26, 9 January 2019

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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n/a

RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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


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