MMP26

Matrix metallopeptidase 26
Identifiers
Symbols	MMP26 ; MGC126590; MGC126592
External IDs	Template:OMIM5 HomoloGene: 49684
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE MMP26 220541 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Matrix metallopeptidase 26, also known as MMP26, is a human gene.

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.

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. PMID 10419448.
• Park HI, Ni J, Gerkema FE; et al. (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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• de Coignac AB, Elson G, Delneste Y; et al. (2000). "Cloning of MMP-26. A novel matrilysin-like proteinase". Eur. J. Biochem. 267 (11): 3323–9. PMID 10824119.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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 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". Biochem. J. 356 (Pt 3): 705–18. PMID 11389678.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 11841844.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Marchenko ND, Marchenko GN, Strongin AY (2002). "Unconventional activation mechanisms of MMP-26, a human matrix metalloproteinase with a unique PHCGXXD cysteine-switch motif". J. Biol. Chem. 277 (21): 18967–72. doi:10.1074/jbc.M201197200. PMID 11889136.CS1 maint: Multiple names: authors list (link)
• 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". Biochem. J. 363 (Pt 2): 253–62. PMID 11931652.CS1 maint: Multiple names: authors list (link)
• Park HI, Turk BE, Gerkema FE; et al. (2002). "Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26". J. Biol. Chem. 277 (38): 35168–75. doi:10.1074/jbc.M205071200. PMID 12119297.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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". J. Biol. Chem. 278 (17): 15056–64. doi:10.1074/jbc.M210975200. PMID 12586837.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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". Fertil. Steril. 80 (3): 564–70. PMID 12969699.CS1 maint: Multiple names: authors list (link)
• 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". J. Biol. Chem. 278 (51): 51646–53. doi:10.1074/jbc.M310109200. PMID 14532275.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 14744773.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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". Mol. Hum. Reprod. 10 (9): 641–50. doi:10.1093/molehr/gah092. PMID 15273280.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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". Carcinogenesis. 25 (12): 2353–60. doi:10.1093/carcin/bgh270. PMID 15333466.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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:10.1016/j.ygyno.2004.05.024. PMID 15350356.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1158/0008-5472.CAN-04-3019. PMID 15574774.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)