SOD1

From Wikipedia, the free encyclopedia

Superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))

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

Symbol(s)

SOD1; ALS; ALS1; IPOA; SOD; homodimer

External IDs

OMIM: 147450 MGI: 98351 HomoloGene: 392

Gene ontology
Molecular Function:	• copper, zinc superoxide dismutase activity • copper ion binding • zinc ion binding • antioxidant activity • oxidoreductase activity • metal ion binding
Cellular Component:	• cytoplasm
Biological Process:	• superoxide metabolic process • response to oxidative stress • nervous system development

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_000454 (mRNA)
NP_000445 (protein)

NM_011434 (mRNA)
NP_035564 (protein)

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 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. Rare transcript variants have been reported for this gene.^[1]

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

[edit] References

^ Entrez Gene: SOD1 superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult)).

[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. 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. 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:10.1007/s00775-003-0447-6. 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. 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:10.1161/01.ATV.0000133604.20182.cf. PMID 15166009.