# MMP26

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Protein-coding gene in the species Homo sapiens

MMP26 Identifiers Aliases MMP26, matrix metallopeptidase 26 External IDs OMIM: 605470; HomoloGene: 49684; GeneCards: MMP26; OMA:MMP26 - orthologs Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11p15.4 Start 4,704,784 bp[1] End 4,992,431 bp[1] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in buccal mucosa cell testicle endometrium gonad prostate renal cortex myometrium hepatobiliary system skeletal muscle smooth muscle tissue n/a More reference expression data BioGPS More reference expression data Gene ontology Molecular function zinc ion binding peptidase activity metalloendopeptidase activity hydrolase activity metallopeptidase activity metal ion binding Cellular component extracellular region extracellular matrix extracellular space Biological process collagen catabolic process negative regulation of inflammatory response proteolysis extracellular matrix organization Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 56547 n/a Ensembl ENSG00000167346 n/a UniProt Q9NRE1 n/a RefSeq (mRNA) NM_021801 NM_001384608 n/a RefSeq (protein) NP_068573 n/a Location (UCSC) Chr 11: 4.7 – 4.99 Mb n/a PubMed search [2] n/a Wikidata View/Edit Human

**Matrix metalloproteinase-26** also known as **matrilysin-2** and **endometase** is an [enzyme](/source/Enzyme) that in humans is encoded by the *MMP26* [gene](/source/Gene).[3][4][5]

## Function

Proteins of the matrix metalloproteinase ([MMP](/source/Matrix_metalloproteinase)) family are involved in the breakdown of [extracellular matrix](/source/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](/source/Collagen), [fibronectin](/source/Fibronectin), [fibrinogen](/source/Fibrinogen), [casein](/source/Casein), [vitronectin](/source/Vitronectin), alpha 1-antitrypsin ([A1AT](/source/Alpha_1-antitrypsin)), alpha 2-macroglobulin ([A2M](/source/Alpha-2-Macroglobulin)), and insulin-like growth factor-binding protein 1 ([IGFBP](/source/Insulin-like_growth_factor_binding_protein)), and activates [MMP9](/source/MMP9) by cleavage. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain.[5]

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000167346](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000167346) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-2)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=56547). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid10801841_3-0)** 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"](https://doi.org/10.1074%2Fjbc.M002349200). *J Biol Chem*. **275** (27): 20540–4. [doi](/source/Doi_(identifier)):[10.1074/jbc.M002349200](https://doi.org/10.1074%2Fjbc.M002349200). [PMID](/source/PMID_(identifier)) [10801841](https://pubmed.ncbi.nlm.nih.gov/10801841).

1. **[^](#cite_ref-pmid10824119_4-0)** 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"](https://doi.org/10.1046%2Fj.1432-1327.2000.01363.x). *Eur J Biochem*. **267** (11): 3323–9. [doi](/source/Doi_(identifier)):[10.1046/j.1432-1327.2000.01363.x](https://doi.org/10.1046%2Fj.1432-1327.2000.01363.x). [PMID](/source/PMID_(identifier)) [10824119](https://pubmed.ncbi.nlm.nih.gov/10824119).

1. ^ [***a***](#cite_ref-entrez_5-0) [***b***](#cite_ref-entrez_5-1) ["Entrez Gene: MMP26 matrix metallopeptidase 26"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=56547).

## Further reading

- Nagase H, Woessner JF (1999). ["Matrix metalloproteinases"](https://doi.org/10.1074%2Fjbc.274.31.21491). *J. Biol. Chem*. **274** (31): 21491–4. [doi](/source/Doi_(identifier)):[10.1074/jbc.274.31.21491](https://doi.org/10.1074%2Fjbc.274.31.21491). [PMID](/source/PMID_(identifier)) [10419448](https://pubmed.ncbi.nlm.nih.gov/10419448).

- Uría JA, López-Otín C (2000). "Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity". *Cancer Res*. **60** (17): 4745–51. [PMID](/source/PMID_(identifier)) [10987280](https://pubmed.ncbi.nlm.nih.gov/10987280).

- Marchenko GN, Ratnikov BI, Rozanov DV, et al. (2001). ["Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221897). *Biochem. J*. **356** (Pt 3): 705–18. [doi](/source/Doi_(identifier)):[10.1042/0264-6021:3560705](https://doi.org/10.1042%2F0264-6021%3A3560705). [PMC](/source/PMC_(identifier)) [1221897](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221897). [PMID](/source/PMID_(identifier)) [11389678](https://pubmed.ncbi.nlm.nih.gov/11389678).

- Gearing AJ, Thorpe SJ, Miller K, et al. (2002). "Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin". *Immunol. Lett*. **81** (1): 41–8. [doi](/source/Doi_(identifier)):[10.1016/S0165-2478(01)00333-9](https://doi.org/10.1016%2FS0165-2478%2801%2900333-9). [PMID](/source/PMID_(identifier)) [11841844](https://pubmed.ncbi.nlm.nih.gov/11841844).

- Marchenko ND, Marchenko GN, Strongin AY (2002). ["Unconventional activation mechanisms of MMP-26, a human matrix metalloproteinase with a unique PHCGXXD cysteine-switch motif"](https://doi.org/10.1074%2Fjbc.M201197200). *J. Biol. Chem*. **277** (21): 18967–72. [doi](/source/Doi_(identifier)):[10.1074/jbc.M201197200](https://doi.org/10.1074%2Fjbc.M201197200). [PMID](/source/PMID_(identifier)) [11889136](https://pubmed.ncbi.nlm.nih.gov/11889136).

- Marchenko GN, Marchenko ND, Leng J, Strongin AY (2002). ["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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222473). *Biochem. J*. **363** (Pt 2): 253–62. [doi](/source/Doi_(identifier)):[10.1042/0264-6021:3630253](https://doi.org/10.1042%2F0264-6021%3A3630253). [PMC](/source/PMC_(identifier)) [1222473](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222473). [PMID](/source/PMID_(identifier)) [11931652](https://pubmed.ncbi.nlm.nih.gov/11931652).

- Park HI, Turk BE, Gerkema FE, et al. (2002). ["Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26"](https://doi.org/10.1074%2Fjbc.M205071200). *J. Biol. Chem*. **277** (38): 35168–75. [doi](/source/Doi_(identifier)):[10.1074/jbc.M205071200](https://doi.org/10.1074%2Fjbc.M205071200). [PMID](/source/PMID_(identifier)) [12119297](https://pubmed.ncbi.nlm.nih.gov/12119297).

- 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"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). *Proc. Natl. Acad. Sci. U.S.A*. **99** (26): 16899–903. [Bibcode](/source/Bibcode_(identifier)):[2002PNAS...9916899M](https://ui.adsabs.harvard.edu/abs/2002PNAS...9916899M). [doi](/source/Doi_(identifier)):[10.1073/pnas.242603899](https://doi.org/10.1073%2Fpnas.242603899). [PMC](/source/PMC_(identifier)) [139241](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). [PMID](/source/PMID_(identifier)) [12477932](https://pubmed.ncbi.nlm.nih.gov/12477932).

- Zhao YG, Xiao AZ, Newcomer RG, et al. (2003). ["Activation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cells"](https://doi.org/10.1074%2Fjbc.M210975200). *J. Biol. Chem*. **278** (17): 15056–64. [doi](/source/Doi_(identifier)):[10.1074/jbc.M210975200](https://doi.org/10.1074%2Fjbc.M210975200). [PMID](/source/PMID_(identifier)) [12586837](https://pubmed.ncbi.nlm.nih.gov/12586837).

- Chegini N, Rhoton-Vlasak A, Williams RS (2003). ["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"](https://doi.org/10.1016%2FS0015-0282%2803%2900797-0). *Fertil. Steril*. **80** (3): 564–70. [doi](/source/Doi_(identifier)):[10.1016/S0015-0282(03)00797-0](https://doi.org/10.1016%2FS0015-0282%2803%2900797-0). [PMID](/source/PMID_(identifier)) [12969699](https://pubmed.ncbi.nlm.nih.gov/12969699).

- Park HI, Jin Y, Hurst DR, et al. (2004). ["The intermediate S1' pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling"](https://doi.org/10.1074%2Fjbc.M310109200). *J. Biol. Chem*. **278** (51): 51646–53. [doi](/source/Doi_(identifier)):[10.1074/jbc.M310109200](https://doi.org/10.1074%2Fjbc.M310109200). [PMID](/source/PMID_(identifier)) [14532275](https://pubmed.ncbi.nlm.nih.gov/14532275).

- Zhao YG, Xiao AZ, Park HI, et al. (2004). "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". *Cancer Res*. **64** (2): 590–8. [doi](/source/Doi_(identifier)):[10.1158/0008-5472.CAN-03-1932](https://doi.org/10.1158%2F0008-5472.CAN-03-1932). [PMID](/source/PMID_(identifier)) [14744773](https://pubmed.ncbi.nlm.nih.gov/14744773). [S2CID](/source/S2CID_(identifier)) [15342778](https://api.semanticscholar.org/CorpusID:15342778).

- Pilka R, Domanski H, Hansson S, et al. (2005). ["Endometrial TIMP-4 mRNA is high at midcycle and in hyperplasia, but down-regulated in malignant tumours. Coordinated expression with MMP-26"](https://doi.org/10.1093%2Fmolehr%2Fgah092). *Mol. Hum. Reprod*. **10** (9): 641–50. [doi](/source/Doi_(identifier)):[10.1093/molehr/gah092](https://doi.org/10.1093%2Fmolehr%2Fgah092). [PMID](/source/PMID_(identifier)) [15273280](https://pubmed.ncbi.nlm.nih.gov/15273280).

- Yamamoto H, Vinitketkumnuen A, Adachi Y, et al. (2005). ["Association of matrilysin-2 (MMP-26) expression with tumor progression and activation of MMP-9 in esophageal squamous cell carcinoma"](https://doi.org/10.1093%2Fcarcin%2Fbgh270). *Carcinogenesis*. **25** (12): 2353–60. [doi](/source/Doi_(identifier)):[10.1093/carcin/bgh270](https://doi.org/10.1093%2Fcarcin%2Fbgh270). [PMID](/source/PMID_(identifier)) [15333466](https://pubmed.ncbi.nlm.nih.gov/15333466).

- Pilka R, Norata GD, Domanski H, et al. (2004). "Matrix metalloproteinase-26 (matrilysin-2) expression is high in endometrial hyperplasia and decreases with loss of histological differentiation in endometrial cancer". *Gynecol. Oncol*. **94** (3): 661–70. [doi](/source/Doi_(identifier)):[10.1016/j.ygyno.2004.05.024](https://doi.org/10.1016%2Fj.ygyno.2004.05.024). [PMID](/source/PMID_(identifier)) [15350356](https://pubmed.ncbi.nlm.nih.gov/15350356).

- 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)"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928). *Genome Res*. **14** (10B): 2121–7. [doi](/source/Doi_(identifier)):[10.1101/gr.2596504](https://doi.org/10.1101%2Fgr.2596504). [PMC](/source/PMC_(identifier)) [528928](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928). [PMID](/source/PMID_(identifier)) [15489334](https://pubmed.ncbi.nlm.nih.gov/15489334).

- Li W, Savinov AY, Rozanov DV, et al. (2005). "Matrix metalloproteinase-26 is associated with estrogen-dependent malignancies and targets alpha1-antitrypsin serpin". *Cancer Res*. **64** (23): 8657–65. [CiteSeerX](/source/CiteSeerX_(identifier)) [10.1.1.316.8634](https://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.316.8634). [doi](/source/Doi_(identifier)):[10.1158/0008-5472.CAN-04-3019](https://doi.org/10.1158%2F0008-5472.CAN-04-3019). [PMID](/source/PMID_(identifier)) [15574774](https://pubmed.ncbi.nlm.nih.gov/15574774). [S2CID](/source/S2CID_(identifier)) [33047996](https://api.semanticscholar.org/CorpusID:33047996).

## External links

- The [MEROPS](/source/MEROPS) online database for peptidases and their inhibitors: [M10.029](http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.029)

v t e Proteases: metalloendopeptidases (EC 3.4.24) ADAM proteins Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13 Matrix metalloproteinases Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28 Other Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

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Adapted from the Wikipedia article [MMP26](https://en.wikipedia.org/wiki/MMP26) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/MMP26?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.