SOD1

SOD1

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.

PBB_Summary
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summary_text = SOD1 binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally occurring, but harmful, superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. [cite journal|last=Conwit|first=Robin A.|title=Preventing familial ALS: A clinical trial may be feasible but is an efficacy trial warranted?|journal=Journal of the Neurological Sciences|year=2006|month=December|volume=251|issue=1–2|pages=1–2|doi=10.1016/j.jns.2006.07.009|issn=0022-510X] [cite journal|last=Al-Chalabi|first=Ammar|coauthor=P. Nigel Leigh|title=Recent advances in amyotrophic lateral sclerosis|journal=Current Opinion in Neurology|year=2000|month=August|volume=13|issue=4|pages=397–405|doi=|issn=1473-6551] Rare transcript variants have been reported for this gene. [cite web | title = Entrez Gene: SOD1 superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6647| accessdate = ]

Mice lacking Sod1 have increased age-related muscle mass loss, early development of cataracts, macular degeneration, thymic involution, hepatocellular carcinoma, and shortned lifespan.

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=de Belleroche J, Orrell R, King A |title=Familial amyotrophic lateral sclerosis/motor neurone disease (FALS): a review of current developments. |journal=J. Med. Genet. |volume=32 |issue= 11 |pages= 841–7 |year= 1996 |pmid= 8592323 |doi=
*cite journal | author=Ceroni M, Curti D, Alimonti D |title=Amyotrophic lateral sclerosis and SOD1 gene: an overview. |journal=Funct. Neurol. |volume=16 |issue= 4 Suppl |pages= 171–80 |year= 2002 |pmid= 11996514 |doi=
*cite journal | author=Zelko IN, Mariani TJ, Folz RJ |title=Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. |journal=Free Radic. Biol. Med. |volume=33 |issue= 3 |pages= 337–49 |year= 2003 |pmid= 12126755 |doi=
*cite journal | author=Hadano S |title= [Causative genes for familial amyotrophic lateral sclerosis] |journal=Seikagaku |volume=74 |issue= 6 |pages= 483–9 |year= 2002 |pmid= 12138710 |doi=
*cite journal | author=Noor R, Mittal S, Iqbal J |title=Superoxide dismutase--applications and relevance to human diseases. |journal=Med. Sci. Monit. |volume=8 |issue= 9 |pages= RA210–5 |year= 2003 |pmid= 12218958 |doi=
*cite journal | author=Potter SZ, Valentine JS |title=The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease). |journal=J. Biol. Inorg. Chem. |volume=8 |issue= 4 |pages= 373–80 |year= 2004 |pmid= 12644909 |doi= 10.1007/s00775-003-0447-6
*cite journal | author=Rotilio G, Aquilano K, Ciriolo MR |title=Interplay of Cu,Zn superoxide dismutase and nitric oxide synthase in neurodegenerative processes. |journal=IUBMB Life |volume=55 |issue= 10-11 |pages= 629–34 |year= 2004 |pmid= 14711010 |doi=
*cite journal | author=Jafari-Schluep HF, Khoris J, Mayeux-Portas V, "et al." |title= [Superoxyde dismutase 1 gene abnormalities in familial amyotrophic lateral sclerosis: phenotype/genotype correlations. The French experience and review of the literature] |journal=Rev. Neurol. (Paris) |volume=160 |issue= 1 |pages= 44–50 |year= 2004 |pmid= 14978393 |doi=
*cite journal | author=Faraci FM, Didion SP |title=Vascular protection: superoxide dismutase isoforms in the vessel wall. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 8 |pages= 1367–73 |year= 2005 |pmid= 15166009 |doi= 10.1161/01.ATV.0000133604.20182.cf

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