MMP26
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
- ↑ 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.
- ↑ 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.
- ↑ 3.0 3.1 "Entrez Gene: MMP26 matrix metallopeptidase 26".
Further reading
- Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 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 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. doi:10.1042/0264-6021:3560705. PMC 1221897. PMID 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:10.1016/S0165-2478(01)00333-9. PMID 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". J. Biol. Chem. 277 (21): 18967–72. doi:10.1074/jbc.M201197200. PMID 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". Biochem. J. 363 (Pt 2): 253–62. doi:10.1042/0264-6021:3630253. PMC 1222473. PMID 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". J. Biol. Chem. 277 (38): 35168–75. doi:10.1074/jbc.M205071200. PMID 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". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 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". J. Biol. Chem. 278 (17): 15056–64. doi:10.1074/jbc.M210975200. PMID 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". Fertil. Steril. 80 (3): 564–70. doi:10.1016/S0015-0282(03)00797-0. PMID 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". J. Biol. Chem. 278 (51): 51646–53. doi:10.1074/jbc.M310109200. PMID 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:10.1158/0008-5472.CAN-03-1932. PMID 14744773.
- 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.
- 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.
- 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.
- 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. PMC 528928. PMID 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. doi:10.1158/0008-5472.CAN-04-3019. PMID 15574774.
External links
- The MEROPS online database for peptidases and their inhibitors: M10.029
