Biology:MMP26

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

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

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.

Further reading

• "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. 1999. doi:10.1074/jbc.274.31.21491. PMID 10419448. 
• "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. 2000. PMID 10987280. 
• "Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin". Biochem. J. 356 (Pt 3): 705–18. 2001. doi:10.1042/0264-6021:3560705. PMID 11389678. 
• "Selective cleavage of human IgG by the matrix metalloproteinases, matrilysin and stromelysin". Immunol. Lett. 81 (1): 41–8. 2002. doi:10.1016/S0165-2478(01)00333-9. PMID 11841844. 
• "Unconventional activation mechanisms of MMP-26, a human matrix metalloproteinase with a unique PHCGXXD cysteine-switch motif". J. Biol. Chem. 277 (21): 18967–72. 2002. doi:10.1074/jbc.M201197200. PMID 11889136. 
• "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. 2002. doi:10.1042/0264-6021:3630253. PMID 11931652. 
• "Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26". J. Biol. Chem. 277 (38): 35168–75. 2002. doi:10.1074/jbc.M205071200. PMID 12119297. 
• "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M. 
• "Activation of pro-gelatinase B by endometase/matrilysin-2 promotes invasion of human prostate cancer cells". J. Biol. Chem. 278 (17): 15056–64. 2003. doi:10.1074/jbc.M210975200. PMID 12586837. 
• "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. 2003. doi:10.1016/S0015-0282(03)00797-0. PMID 12969699. 
• "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. 2004. doi:10.1074/jbc.M310109200. PMID 14532275. 
• "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. 2004. doi:10.1158/0008-5472.CAN-03-1932. PMID 14744773. 
• "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. 2005. doi:10.1093/molehr/gah092. PMID 15273280. 
• "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. 2005. doi:10.1093/carcin/bgh270. PMID 15333466. 
• "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. 2004. doi:10.1016/j.ygyno.2004.05.024. PMID 15350356. 
• "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334. 
• "Matrix metalloproteinase-26 is associated with estrogen-dependent malignancies and targets alpha1-antitrypsin serpin". Cancer Res. 64 (23): 8657–65. 2005. doi:10.1158/0008-5472.CAN-04-3019. PMID 15574774. 

External links

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