SOD1
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Superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))
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| PDB rendering based on 1azv. | ||||||||||||||
| Available structures: 1azv, 1ba9, 1dsw, 1fun, 1hl4, 1hl5, 1kmg, 1l3n, 1mfm, 1n18, 1n19, 1oez, 1ozt, 1ozu, 1p1v, 1ptz, 1pu0, 1rk7, 1sos, 1spd, 1uxl, 1uxm, 2af2, 2c9s, 2c9u, 2c9v, 2gbt, 2gbu, 2gbv, 2nnx | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbols | SOD1; ALS; ALS1; IPOA; SOD; homodimer | |||||||||||||
| External IDs | OMIM: 147450 MGI: 98351 HomoloGene: 392 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 6647 | 20655 | ||||||||||||
| Ensembl | ENSG00000142168 | n/a | ||||||||||||
| Uniprot | P00441 | n/a | ||||||||||||
| Refseq | NM_000454 (mRNA) NP_000445 (protein) |
NM_011434 (mRNA) NP_035564 (protein) |
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| Location | Chr 21: 31.95 - 31.96 Mb | n/a | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult)), also known as SOD1, is a human protein and gene. This gene encodes one of three forms of the human superoxide dismutase.
SOD1 binds copper and zinc ions and is one of three isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic and mitochondrial intermembrane space protein, acting as a homodimer to convert naturally occurring, but harmful, superoxide radicals to molecular oxygen and hydrogen peroxide. Mutations (over 100 identified to date) in this gene have been linked to familial amyotrophic lateral sclerosis.[1][2] The most frequent mutation are A4V (in the U.S.A.) and H46R (Japan). The most studied ALS mouse model is G93A. Rare transcript variants have been reported for this gene.[3]
In one study, deletions in the gene were reported in two familial cases of keratoconus.[4]
Mice lacking Sod1 have increased age-related muscle mass loss (sarcopenia), early development of cataracts, macular degeneration, thymic involution, hepatocellular carcinoma, and shortened lifespan [5].
[edit] References
- ^ Conwit, Robin A. (December 2006). "Preventing familial ALS: A clinical trial may be feasible but is an efficacy trial warranted?". Journal of the Neurological Sciences 251 (1–2): 1–2. doi:. ISSN 0022-510X.
- ^ Al-Chalabi, Ammar; P. Nigel Leigh (August 2000). "Recent advances in amyotrophic lateral sclerosis". Current Opinion in Neurology 13 (4): 397–405. ISSN 1473-6551.
- ^ "Entrez Gene: SOD1 superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6647.
- ^ Udar N, Atilano SR, Brown DJ, Holguin B, Small K, Nesburn AB, Kenney MC (August 2006). "SOD1: a candidate gene for keratoconus". Invest. Ophthalmol. Vis. Sci. 47 (8): 3345–51. doi:. PMID 16877401. http://www.iovs.org/cgi/pmidlookup?view=long&pmid=16877401.
- ^ Trends in oxidative aging theories. Free Radic Biol Med. 2007 Aug 15;43(4):477-503.
[edit] Further reading
- de Belleroche J, Orrell R, King A (1996). "Familial amyotrophic lateral sclerosis/motor neurone disease (FALS): a review of current developments.". J. Med. Genet. 32 (11): 841–7. doi:. PMID 8592323.
- Ceroni M, Curti D, Alimonti D (2002). "Amyotrophic lateral sclerosis and SOD1 gene: an overview.". Funct. Neurol. 16 (4 Suppl): 171–80. PMID 11996514.
- Zelko IN, Mariani TJ, Folz RJ (2003). "Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression.". Free Radic. Biol. Med. 33 (3): 337–49. doi:. PMID 12126755.
- Hadano S (2002). "[Causative genes for familial amyotrophic lateral sclerosis]". Seikagaku 74 (6): 483–9. PMID 12138710.
- Noor R, Mittal S, Iqbal J (2003). "Superoxide dismutase--applications and relevance to human diseases.". Med. Sci. Monit. 8 (9): RA210–5. PMID 12218958.
- Potter SZ, Valentine JS (2004). "The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease).". J. Biol. Inorg. Chem. 8 (4): 373–80. doi:. PMID 12644909.
- Rotilio G, Aquilano K, Ciriolo MR (2004). "Interplay of Cu,Zn superoxide dismutase and nitric oxide synthase in neurodegenerative processes.". IUBMB Life 55 (10-11): 629–34. doi:. PMID 14711010.
- Jafari-Schluep HF, Khoris J, Mayeux-Portas V, et al. (2004). "[Superoxyde dismutase 1 gene abnormalities in familial amyotrophic lateral sclerosis: phenotype/genotype correlations. The French experience and review of the literature]". Rev. Neurol. (Paris) 160 (1): 44–50. PMID 14978393.
- Faraci FM, Didion SP (2005). "Vascular protection: superoxide dismutase isoforms in the vessel wall.". Arterioscler. Thromb. Vasc. Biol. 24 (8): 1367–73. doi:. PMID 15166009.
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