LOXL2
Lysyl oxidase homolog 2 is an enzyme that in humans is encoded by the LOXL2 gene.[1][2]
This gene encodes a member of the lysyl oxidase gene family. The prototypic member of the family is essential to the biogenesis of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. A highly conserved amino acid sequence at the C-terminus end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The N-terminus is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family.[2] According to a BBC article on 2/22/11, "scientists at the UK's Institute of Cancer Research have prevented breast cancer spreading to other organs in mice by blocking the enzyme LOXL2 ". Their findings were published in Cancer Research. The authors found that LOXL2 was important in the early stages of cancer spread and that high levels of the enzyme were linked with cancer spread and poor survival rates so they used chemicals and antibodies to block the enzyme and stopped the metastasis.[3]
See also
References
Further reading
- Csiszar K (2001). "Lysyl oxidases: a novel multifunctional amine oxidase family". Prog. Nucleic Acid Res. Mol. Biol.. Progress in Nucleic Acid Research and Molecular Biology 70: 1–32. doi:10.1016/S0079-6603(01)70012-8. ISBN 978-0-12-540070-1. PMID 11642359.
- Molnar J, Fong KS, He QP, et al. (2003). "Structural and functional diversity of lysyl oxidase and the LOX-like proteins". Biochim. Biophys. Acta 1647 (1–2): 220–4. PMID 12686136.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Saito H, Papaconstantinou J, Sato H, Goldstein S (1997). "Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence". J. Biol. Chem. 272 (13): 8157–60. doi:10.1074/jbc.272.13.8157. PMID 9079631.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Jourdan-Le Saux C, Tronecker H, Bogic L, et al. (1999). "The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed at high levels in reproductive tissues". J. Biol. Chem. 274 (18): 12939–44. doi:10.1074/jbc.274.18.12939. PMID 10212285.
- Hein S, Yamamoto SY, Okazaki K, et al. (2001). "Lysyl oxidases: expression in the fetal membranes and placenta". Placenta 22 (1): 49–57. doi:10.1053/plac.2000.0580. PMID 11162352.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Akiri G, Sabo E, Dafni H, et al. (2003). "Lysyl oxidase-related protein-1 promotes tumor fibrosis and tumor progression in vivo". Cancer Res. 63 (7): 1657–66. PMID 12670920.
- Rost T, Pyritz V, Rathcke IO, et al. (2003). "Reduction of LOX- and LOXL2-mRNA expression in head and neck squamous cell carcinomas". Anticancer Res. 23 (2B): 1565–73. PMID 12820424.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Vadasz Z, Kessler O, Akiri G, et al. (2005). "Abnormal deposition of collagen around hepatocytes in Wilson's disease is associated with hepatocyte specific expression of lysyl oxidase and lysyl oxidase like protein-2". J. Hepatol. 43 (3): 499–507. doi:10.1016/j.jhep.2005.02.052. PMID 16023247.
- Peinado H, Del Carmen Iglesias-de la Cruz M, Olmeda D, et al. (2006). "A molecular role for lysyl oxidase-like 2 enzyme in Snail regulation and tumor progression". EMBO J. 24 (19): 3446–58. doi:10.1038/sj.emboj.7600781. PMC 1276164. PMID 16096638. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1276164.
- Akagawa H, Narita A, Yamada H, et al. (2007). "Systematic screening of lysyl oxidase-like (LOXL) family genes demonstrates that LOXL2 is a susceptibility gene to intracranial aneurysms". Hum. Genet. 121 (3–4): 377–87. doi:10.1007/s00439-007-0333-3. PMID 17287949.