MMP11
Stromelysin-3 (SL-3) also known as matrix metalloproteinase-11 (MMP-11) is an enzyme that in humans is encoded by the MMP11 gene.[1][2][3][4]
Function
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. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP’s, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix.[4]
References
References
- ↑ Levy A, Zucman J, Delattre O, Mattei MG, Rio MC, Basset P (Aug 1992). “Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22”. Genomics. 13 (3): 881–3. doi:10.1016/0888-7543(92)90175-R. PMID 1639418.
- ↑ Anglard P, Melot T, Guerin E, Thomas G, Basset P (Oct 1995). “Structure and promoter characterization of the human stromelysin-3 gene”. J Biol Chem. 270 (35): 20337–44. doi:10.1074/jbc.270.35.20337. PMID 7657606.
- ↑ Luo D, Mari B, Stoll I, Anglard P (Jul 2002). “Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase”. J Biol Chem. 277 (28): 25527–36. doi:10.1074/jbc.M202494200. PMID 12006591.
- ↑ 4.0 4.1 “Entrez Gene: MMP11 matrix metallopeptidase 11 (stromelysin 3)”.
Further reading
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.
- Basset P, Bellocq JP, Wolf C, et al. (1991). “A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas”. Nature. 348 (6303): 699–704. doi:10.1038/348699a0. PMID 1701851.
- Pei D, Majmudar G, Weiss SJ (1994). “Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3”. J. Biol. Chem. 269 (41): 25849–55. PMID 7523394.
- Pei D, Weiss SJ (1995). “Furin-dependent intracellular activation of the human stromelysin-3 zymogen” (PDF). Nature. 375 (6528): 244–7. doi:10.1038/375244a0. PMID 7746327.
- Boulay A, Masson R, Chenard MP, et al. (2001). “High cancer cell death in syngeneic tumors developed in host mice deficient for the stromelysin-3 matrix metalloproteinase”. Cancer Res. 61 (5): 2189–93. PMID 11280785.
- Perret AG, Duthel R, Fotso MJ, et al. (2002). “Stromelysin-3 is expressed by aggressive meningiomas”. Cancer. 94 (3): 765–72. doi:10.1002/cncr.10270. PMID 11857311.
- Nakopoulou L, Panayotopoulou EG, Giannopoulou I, et al. (2003). “Stromelysin-3 protein expression in invasive breast cancer: relation to proliferation, cell survival and patients’ outcome”. Mod. Pathol. 15 (11): 1154–61. doi:10.1097/01.MP.0000037317.84782.CD. PMID 12429794.
- 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.
- Wasenius VM, Hemmer S, Kettunen E, et al. (2003). “Hepatocyte growth factor receptor, matrix metalloproteinase-11, tissue inhibitor of metalloproteinase-1, and fibronectin are up-regulated in papillary thyroid carcinoma: a cDNA and tissue microarray study”. Clin. Cancer Res. 9 (1): 68–75. PMID 12538453.
- Fromigué O, Louis K, Wu E, et al. (2003). “Active stromelysin-3 (MMP-11) increases MCF-7 survival in three-dimensional Matrigel culture via activation of p42/p44 MAP-kinase”. Int. J. Cancer. 106 (3): 355–63. doi:10.1002/ijc.11232. PMID 12845673.
- Skoglund J, Emterling A, Arbman G, et al. (2004). “Clinicopathological significance of stromelysin-3 expression in colorectal cancer”. Oncology. 67 (1): 67–72. doi:10.1159/000080288. PMID 15459498.
- 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.
- Louis K, Guérineau N, Fromigué O, et al. (2005). “Tumor cell-mediated induction of the stromal factor stromelysin-3 requires heterotypic cell contact-dependent activation of specific protein kinase C isoforms”. J. Biol. Chem. 280 (2): 1272–83. doi:10.1074/jbc.M405482200. PMID 15509588.
- Deng H, Guo RF, Li WM, et al. (2005). “Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells”. Biochem. Biophys. Res. Commun. 326 (2): 274–81. doi:10.1016/j.bbrc.2004.11.027. PMID 15582574.
- Arora S, Kaur J, Sharma C, et al. (2005). “Stromelysin 3, Ets-1, and vascular endothelial growth factor expression in oral precancerous and cancerous lesions: correlation with microvessel density, progression, and prognosis”. Clin. Cancer Res. 11 (6): 2272–84. doi:10.1158/1078-0432.CCR-04-0572. PMID 15788677.
- Vazquez-Ortiz G, Pina-Sanchez P, Vazquez K, et al. (2006). “Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer”. BMC Cancer. 5: 68. doi:10.1186/1471-2407-5-68. PMC 1175083. PMID 15989693.
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