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{{Infobox_gene}}
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'''Matrix metalloproteinase-26''' also known as '''matrilysin-2''' and '''endometase''' is an [[enzyme]] that in humans is encoded by the ''MMP26'' [[gene]].<ref name="pmid10801841">{{cite journal |vauthors=Park HI, Ni J, Gerkema FE, Liu D, Belozerov VE, Sang QX | title = Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor | journal = J Biol Chem | volume = 275 | issue = 27 | pages = 20540–4 |date=Aug 2000 | pmid = 10801841 | pmc =  | doi = 10.1074/jbc.M002349200 }}</ref><ref name="pmid10824119">{{cite journal |vauthors=de Coignac AB, Elson G, Delneste Y, Magistrelli G, Jeannin P, Aubry JP, Berthier O, Schmitt D, Bonnefoy JY, Gauchat JF | title = Cloning of MMP-26. A novel matrilysin-like proteinase | journal = Eur J Biochem | volume = 267 | issue = 11 | pages = 3323–9 |date=Jul 2000 | pmid = 10824119 | pmc =  | doi =10.1046/j.1432-1327.2000.01363.x  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MMP26 matrix metallopeptidase 26| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56547| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Matrix metallopeptidase 26
| HGNCid = 14249
| Symbol = MMP26
| AltSymbols =; MGC126590; MGC126592
| OMIM = 605470
| ECnumber = 
| Homologene = 49684
| MGIid = 
| GeneAtlas_image1 = PBB_GE_MMP26_220541_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase 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:0030574 |text = collagen catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 56547
    | Hs_Ensembl = ENSG00000167346
    | Hs_RefseqProtein = NP_068573
    | Hs_RefseqmRNA = NM_021801
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 4745076
    | Hs_GenLoc_end = 4970235
    | Hs_Uniprot = Q9NRE1
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Matrix metallopeptidase 26''', also known as '''MMP26''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MMP26 matrix metallopeptidase 26| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56547| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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. The encoded protein degrades type IV [[collagen]], [[fibronectin]], [[fibrinogen]], [[casein]], [[vitronectin]], alpha 1-antitrypsin ([[alpha 1-antitrypsin|A1AT]]), alpha 2-macroglobulin ([[alpha-2-Macroglobulin|A2M]]), and insulin-like growth factor-binding protein 1 ([[insulin-like growth factor binding protein|IGFBP]]), and activates [[MMP9]] by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain.<ref name="entrez" />
{{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. The encoded protein degrades type IV collagen, fibronectin, fibrinogen, casein, vitronectin, alpha 1-antitrypsin, alpha 2-macroglobulin, and insulin-like growth factor-binding protein 1, and activates MMP9 by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain.<ref name="entrez">{{cite web | title = Entrez Gene: MMP26 matrix metallopeptidase 26| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56547| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| 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  |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  | author=Park HI, Ni J, Gerkema FE, ''et al.'' |title=Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20540-4 |year= 2000 |pmid= 10801841 |doi= 10.1074/jbc.M002349200 }}
*{{cite journal  |vauthors=Uría JA, López-Otín C |title=Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity |journal=Cancer Res. |volume=60 |issue= 17 |pages= 4745–51 |year= 2000 |pmid= 10987280 |doi= }}
*{{cite journal | author=de Coignac AB, Elson G, Delneste Y, ''et al.'' |title=Cloning of MMP-26. A novel matrilysin-like proteinase. |journal=Eur. J. Biochem. |volume=267 |issue= 11 |pages= 3323-9 |year= 2000 |pmid= 10824119 |doi=  }}
*{{cite journal   |vauthors=Marchenko GN, Ratnikov BI, Rozanov DV, etal |title=Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin |journal=Biochem. J. |volume=356 |issue= Pt 3 |pages= 705–18 |year= 2001 |pmid= 11389678 |doi=10.1042/0264-6021:3560705  | pmc=1221897 }}
*{{cite journal | author=Uría JA, López-Otín C |title=Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity. |journal=Cancer Res. |volume=60 |issue= 17 |pages= 4745-51 |year= 2000 |pmid= 10987280 |doi=  }}
*{{cite journal   |vauthors=Gearing AJ, Thorpe SJ, Miller K, etal |title=Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin |journal=Immunol. Lett. |volume=81 |issue= 1 |pages= 41–8 |year= 2002 |pmid= 11841844 |doi=10.1016/S0165-2478(01)00333-9 }}
*{{cite journal  | author=Marchenko GN, Ratnikov BI, Rozanov DV, ''et al.'' |title=Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin. |journal=Biochem. J. |volume=356 |issue= Pt 3 |pages= 705-18 |year= 2001 |pmid= 11389678 |doi= }}
*{{cite journal  |vauthors=Marchenko ND, Marchenko GN, Strongin AY |title=Unconventional activation mechanisms of MMP-26, a human matrix metalloproteinase with a unique PHCGXXD cysteine-switch motif |journal=J. Biol. Chem. |volume=277 |issue= 21 |pages= 18967–72 |year= 2002 |pmid= 11889136 |doi= 10.1074/jbc.M201197200 }}
*{{cite journal  | author=Gearing AJ, Thorpe SJ, Miller K, ''et al.'' |title=Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin. |journal=Immunol. Lett. |volume=81 |issue= 1 |pages= 41-8 |year= 2002 |pmid= 11841844 |doi=  }}
*{{cite journal  |vauthors=Marchenko GN, Marchenko ND, Leng J, Strongin AY |title=Promoter characterization of the novel human matrix metalloproteinase-26 gene: regulation by the T-cell factor-4 implies specific expression of the gene in cancer cells of epithelial origin |journal=Biochem. J. |volume=363 |issue= Pt 2 |pages= 253–62 |year= 2002 |pmid= 11931652 |doi=10.1042/0264-6021:3630253  | pmc=1222473 }}
*{{cite journal | author=Marchenko ND, Marchenko GN, Strongin AY |title=Unconventional activation mechanisms of MMP-26, a human matrix metalloproteinase with a unique PHCGXXD cysteine-switch motif. |journal=J. Biol. Chem. |volume=277 |issue= 21 |pages= 18967-72 |year= 2002 |pmid= 11889136 |doi= 10.1074/jbc.M201197200 }}
*{{cite journal   |vauthors=Park HI, Turk BE, Gerkema FE, etal |title=Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26 |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35168–75 |year= 2002 |pmid= 12119297 |doi= 10.1074/jbc.M205071200 }}
*{{cite journal | author=Marchenko GN, Marchenko ND, Leng J, Strongin AY |title=Promoter characterization of the novel human matrix metalloproteinase-26 gene: regulation by the T-cell factor-4 implies specific expression of the gene in cancer cells of epithelial origin. |journal=Biochem. J. |volume=363 |issue= Pt 2 |pages= 253-62 |year= 2002 |pmid= 11931652 |doi=  }}
*{{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 | author=Park HI, Turk BE, Gerkema FE, ''et al.'' |title=Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26. |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35168-75 |year= 2002 |pmid= 12119297 |doi= 10.1074/jbc.M205071200 }}
*{{cite journal   |vauthors=Zhao YG, Xiao AZ, Newcomer RG, etal |title=Activation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cells |journal=J. Biol. Chem. |volume=278 |issue= 17 |pages= 15056–64 |year= 2003 |pmid= 12586837 |doi= 10.1074/jbc.M210975200 }}
*{{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  |vauthors=Chegini N, Rhoton-Vlasak A, Williams RS |title=Expression of matrix metalloproteinase-26 and tissue inhibitor of matrix metalloproteinase-3 and -4 in endometrium throughout the normal menstrual cycle and alteration in users of levonorgestrel implants who experience irregular uterine bleeding |journal=Fertil. Steril. |volume=80 |issue= 3 |pages= 564–70 |year= 2003 |pmid= 12969699 |doi=10.1016/S0015-0282(03)00797-0  }}
*{{cite journal | author=Zhao YG, Xiao AZ, Newcomer RG, ''et al.'' |title=Activation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cells. |journal=J. Biol. Chem. |volume=278 |issue= 17 |pages= 15056-64 |year= 2003 |pmid= 12586837 |doi= 10.1074/jbc.M210975200 }}
*{{cite journal   |vauthors=Park HI, Jin Y, Hurst DR, etal |title=The intermediate S1' pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51646–53 |year= 2004 |pmid= 14532275 |doi= 10.1074/jbc.M310109200 }}
*{{cite journal | author=Chegini N, Rhoton-Vlasak A, Williams RS |title=Expression of matrix metalloproteinase-26 and tissue inhibitor of matrix metalloproteinase-3 and -4 in endometrium throughout the normal menstrual cycle and alteration in users of levonorgestrel implants who experience irregular uterine bleeding. |journal=Fertil. Steril. |volume=80 |issue= 3 |pages= 564-70 |year= 2003 |pmid= 12969699 |doi= }}
*{{cite journal   |vauthors=Zhao YG, Xiao AZ, Park HI, etal |title=Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion |journal=Cancer Res. |volume=64 |issue= 2 |pages= 590–8 |year= 2004 |pmid= 14744773 |doi=10.1158/0008-5472.CAN-03-1932  }}
*{{cite journal | author=Park HI, Jin Y, Hurst DR, ''et al.'' |title=The intermediate S1' pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 51646-53 |year= 2004 |pmid= 14532275 |doi= 10.1074/jbc.M310109200 }}
*{{cite journal   |vauthors=Pilka R, Domanski H, Hansson S, etal |title=Endometrial TIMP-4 mRNA is high at midcycle and in hyperplasia, but down-regulated in malignant tumours. Coordinated expression with MMP-26 |journal=Mol. Hum. Reprod. |volume=10 |issue= 9 |pages= 641–50 |year= 2005 |pmid= 15273280 |doi= 10.1093/molehr/gah092 }}
*{{cite journal | author=Zhao YG, Xiao AZ, Park HI, ''et al.'' |title=Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion. |journal=Cancer Res. |volume=64 |issue= 2 |pages= 590-8 |year= 2004 |pmid= 14744773 |doi= }}
*{{cite journal   |vauthors=Yamamoto H, Vinitketkumnuen A, Adachi Y, etal |title=Association of matrilysin-2 (MMP-26) expression with tumor progression and activation of MMP-9 in esophageal squamous cell carcinoma |journal=Carcinogenesis |volume=25 |issue= 12 |pages= 2353–60 |year= 2005 |pmid= 15333466 |doi= 10.1093/carcin/bgh270 }}
*{{cite journal | author=Pilka R, Domanski H, Hansson S, ''et al.'' |title=Endometrial TIMP-4 mRNA is high at midcycle and in hyperplasia, but down-regulated in malignant tumours. Coordinated expression with MMP-26. |journal=Mol. Hum. Reprod. |volume=10 |issue= 9 |pages= 641-50 |year= 2005 |pmid= 15273280 |doi= 10.1093/molehr/gah092 }}
*{{cite journal   |vauthors=Pilka R, Norata GD, Domanski H, etal |title=Matrix metalloproteinase-26 (matrilysin-2) expression is high in endometrial hyperplasia and decreases with loss of histological differentiation in endometrial cancer |journal=Gynecol. Oncol. |volume=94 |issue= 3 |pages= 661–70 |year= 2004 |pmid= 15350356 |doi= 10.1016/j.ygyno.2004.05.024 }}
*{{cite journal | author=Yamamoto H, Vinitketkumnuen A, Adachi Y, ''et al.'' |title=Association of matrilysin-2 (MMP-26) expression with tumor progression and activation of MMP-9 in esophageal squamous cell carcinoma. |journal=Carcinogenesis |volume=25 |issue= 12 |pages= 2353-60 |year= 2005 |pmid= 15333466 |doi= 10.1093/carcin/bgh270 }}
*{{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 | author=Pilka R, Norata GD, Domanski H, ''et al.'' |title=Matrix metalloproteinase-26 (matrilysin-2) expression is high in endometrial hyperplasia and decreases with loss of histological differentiation in endometrial cancer. |journal=Gynecol. Oncol. |volume=94 |issue= 3 |pages= 661-70 |year= 2004 |pmid= 15350356 |doi= 10.1016/j.ygyno.2004.05.024 }}
*{{cite journal   |vauthors=Li W, Savinov AY, Rozanov DV, etal |title=Matrix metalloproteinase-26 is associated with estrogen-dependent malignancies and targets alpha1-antitrypsin serpin |journal=Cancer Res. |volume=64 |issue= 23 |pages= 8657–65 |year= 2005 |pmid= 15574774 |doi= 10.1158/0008-5472.CAN-04-3019 }}
*{{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=Li W, Savinov AY, Rozanov DV, ''et al.'' |title=Matrix metalloproteinase-26 is associated with estrogen-dependent malignancies and targets alpha1-antitrypsin serpin. |journal=Cancer Res. |volume=64 |issue= 23 |pages= 8657-65 |year= 2005 |pmid= 15574774 |doi= 10.1158/0008-5472.CAN-04-3019 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.029 M10.029]
 
{{Metalloendopeptidases}}
 
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[[Category:Matrix metalloproteinases]]
 
 
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Latest revision as of 06:41, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Wikidata
View/Edit Human

Matrix metalloproteinase-26 also known as matrilysin-2 and endometase is an enzyme that in humans is encoded by the MMP26 gene.[1][2][3]

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. The encoded protein degrades type IV collagen, fibronectin, fibrinogen, casein, vitronectin, alpha 1-antitrypsin (A1AT), alpha 2-macroglobulin (A2M), and insulin-like growth factor-binding protein 1 (IGFBP), and activates MMP9 by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain.[3]

References

  1. ↑ Park HI, Ni J, Gerkema FE, Liu D, Belozerov VE, Sang QX (Aug 2000). "Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor". J Biol Chem. 275 (27): 20540–4. doi:10.1074/jbc.M002349200. PMID 10801841.
  2. ↑ de Coignac AB, Elson G, Delneste Y, Magistrelli G, Jeannin P, Aubry JP, Berthier O, Schmitt D, Bonnefoy JY, Gauchat JF (Jul 2000). "Cloning of MMP-26. A novel matrilysin-like proteinase". Eur J Biochem. 267 (11): 3323–9. doi:10.1046/j.1432-1327.2000.01363.x. PMID 10824119.
  3. ↑ 3.0 3.1 "Entrez Gene: MMP26 matrix metallopeptidase 26".

Further reading

External links

  • The MEROPS online database for peptidases and their inhibitors: M10.029


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