The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Sod1  -  superoxide dismutase 1, soluble

Mus musculus

Synonyms: B430204E11Rik, Cu(2+)-Zn2+ superoxide dismutase, Cu/Zn-SOD, CuZnSOD, Ipo-1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Sod1

  • Using mice bearing a disruption of the CuZn-SOD gene (Sod1), the present study was designed to clarify the role of superoxide anion in the pathogenesis of selective vulnerability after transient global ischemia [1].
  • These results together suggest that a lesser degree of oxidative damage and a more inducible CuZnSOD activity observed in the mesolimbic dopaminergic pathway may partially explain the differential toxicity MPTP produced in these two dopaminergic systems [2].
  • Glioma cells that stably overexpressed CuZnSOD demonstrated additional suppressive effects on the malignant phenotype when compared with the parental cells and vector controls [3].
  • We evaluated this possibility in the model of transient focal cerebral ischemia in mice bearing a disruption of the CuZn-SOD gene (Sod1) [4].
  • The Sod1 +/- animals also had increased infarct volume and brain swelling, accompanied by increased apoptotic neuronal cell death as indicated by the in situ nick-end labeling technique to detect DNA fragmentation and morphological criteria [4].

Psychiatry related information on Sod1


High impact information on Sod1

  • Copper-zinc superoxide dismutase (CuZnSOD, SOD1 protein) is an abundant copper- and zinc-containing protein that is present in the cytosol, nucleus, peroxisomes, and mitochondrial intermembrane space of human cells [6].
  • To investigate the possible involvement of Cu/Zn-superoxide dismutase (CuZnSOD) gene dosage in the neuropathological symptoms of Down's syndrome, we analyzed the tongue muscle of transgenic mice that express elevated levels of human CuZnSOD [7].
  • The findings suggest that CuZnSOD gene dosage is involved in the pathological abnormalities of tongue NMJ observed in Down's syndrome patients [7].
  • The results show that expression of elevated levels of CuZnSOD decreases pulmonary oxygen toxicity and associated histologic damage and mortality [8].
  • Upon exposure to hyperoxia (greater than 99% O2, 630 torr) the transgenic CuZnSOD mice showed increased survival, decreased morphologic evidence of lung damage such as edema and hyaline membrane formation, and reduction in the number of lung neutrophils [8].

Chemical compound and disease context of Sod1


Biological context of Sod1


Anatomical context of Sod1

  • When cultured cells were subjected to treatment with paraquat to assess their ability to grow in the presence of high levels of superoxide radicals, Sod1-/- cells were 80 times more sensitive and Sod2-/- cells were 12 times more sensitive to paraquat than wild-type cells [15].
  • The investigations of Sod1 transgenic cell-lines and mice, as well as Gpx1 knockout mice (both models favor H(2)O(2) accumulation), are presented [17].
  • All of the anti-oxidant enzyme activities were lower in general in the 2 transformed cell lines than in the in vitro normal cell line, except Cu-ZnSOD, which showed little change [18].
  • Our results suggest that CuZnSOD-deficient cells are more sensitive to oxygen toxicity than are MnSOD-deficient cells, that paraquat causes free radical-induced damage in both the mitochondria and cytoplasm, and that SOD compartmentalized in the cytosol cannot compensate for the loss of SOD in the mitochondria and vice versa [15].
  • In human, all the enzymes (except for catalase) were expressed in MII oocytes and Cu-Zn-SOD was particularly highly expressed [19].

Associations of Sod1 with chemical compounds

  • However, it has been suggested that H2O2 production, via Sod1 dismutation, is rate-limited by the availability of the substrate O2*-, and therefore age-related changes may occur as a result of other functions of Sod1 [20].
  • Because Sod1 (Cu/ZnSOD) and alphaB crystalline were expressed only in spleen, and protein tyrosine kinase and platelet membrane glycoprotein lib were expressed in both spleen and lung, these genes may also be potential markers for detection of radiation exposure, especially low-dose radiation, in these tissues [21].
  • Inhibition by hypericin in the dark was demonstrated for purified CuZnSOD, Se-dependent glutathione peroxidase, glutathione S-transferase, and glutathione reductase activities in vitro [22].
  • Copper zinc superoxide dismutase (CuZnSOD) is an essential primary antioxidant enzyme that converts superoxide radical to hydrogen peroxide and molecular oxygen in the cytoplasm [3].
  • Furthermore, the protective effect of CuZnSOD at the DNA level, as shown by reduced thymine glycol generation, was demonstrated in paraquat-treated transgenic fibroblasts [23].

Regulatory relationships of Sod1


Other interactions of Sod1

  • We also found that high fat diet enhanced fatty changes of the liver in Sod1 KO and double KO mice but not in Sod2 KO mice [14].
  • CuZnSOD and catalase activities peaked within 0.5 h following irradiation for nontoxic 0.5 microM hypericin and toxic 1.0 microM hypericin [22].
  • Previously, we demonstrated that a perturbation in the Sod1-to-Gpx1 ratio, as a consequence of Sod1 overexpression, leads to senescence-like changes [20].
  • Five of these represented genes that mapped within the Sod-1 to Ets-2 interval, which was shown previously to contain the weaver (wv) gene [25].
  • The other markers included in this study were Prm-1, Gap43 and Sod-1 [26].

Analytical, diagnostic and therapeutic context of Sod1


  1. Exacerbation of delayed cell injury after transient global ischemia in mutant mice with CuZn superoxide dismutase deficiency. Kawase, M., Murakami, K., Fujimura, M., Morita-Fujimura, Y., Gasche, Y., Kondo, T., Scott, R.W., Chan, P.H. Stroke (1999) [Pubmed]
  2. MPTP produces differential oxidative stress and antioxidative responses in the nigrostriatal and mesolimbic dopaminergic pathways. Hung, H.C., Lee, E.H. Free Radic. Biol. Med. (1998) [Pubmed]
  3. Overexpression of copper zinc superoxide dismutase suppresses human glioma cell growth. Zhang, Y., Zhao, W., Zhang, H.J., Domann, F.E., Oberley, L.W. Cancer Res. (2002) [Pubmed]
  4. Reduction of CuZn-superoxide dismutase activity exacerbates neuronal cell injury and edema formation after transient focal cerebral ischemia. Kondo, T., Reaume, A.G., Huang, T.T., Carlson, E., Murakami, K., Chen, S.F., Hoffman, E.K., Scott, R.W., Epstein, C.J., Chan, P.H. J. Neurosci. (1997) [Pubmed]
  5. Quantitative autoradiographic distribution of [3H]mazindol-labeled dopamine uptake sites in the brains of superoxide dismutase transgenic mice. Cadet, J.L., Przedborski, S., Kostic, V., Jackson-Lewis, V., Carlson, E., Epstein, C.J. Brain Res. Bull. (1990) [Pubmed]
  6. Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Selverstone Valentine, J., Doucette, P.A., Zittin Potter, S. Annu. Rev. Biochem. (2005) [Pubmed]
  7. Down's syndrome: abnormal neuromuscular junction in tongue of transgenic mice with elevated levels of human Cu/Zn-superoxide dismutase. Avraham, K.B., Schickler, M., Sapoznikov, D., Yarom, R., Groner, Y. Cell (1988) [Pubmed]
  8. Transgenic mice with expression of elevated levels of copper-zinc superoxide dismutase in the lungs are resistant to pulmonary oxygen toxicity. White, C.W., Avraham, K.B., Shanley, P.F., Groner, Y. J. Clin. Invest. (1991) [Pubmed]
  9. Decreased copper-zinc superoxide dismutase activity and increased resistance to oxidative stress in glia maturation factor-null astrocytes. Zaheer, A., Yang, B., Cao, X., Lim, R. Neurochem. Res. (2004) [Pubmed]
  10. Gene dosage of CuZnSOD and Down's syndrome: diminished prostaglandin synthesis in human trisomy 21, transfected cells and transgenic mice. Minc-Golomb, D., Knobler, H., Groner, Y. EMBO J. (1991) [Pubmed]
  11. Diminished serotonin uptake in platelets of transgenic mice with increased Cu/Zn-superoxide dismutase activity. Schickler, M., Knobler, H., Avraham, K.B., Elroy-Stein, O., Groner, Y. EMBO J. (1989) [Pubmed]
  12. An adenovirus encoding CuZnSOD protects cultured striatal neurones against glutamate toxicity. Barkats, M., Bemelmans, A.P., Geoffroy, M.C., Robert, J.J., Loquet, I., Horellou, P., Revah, F., Mallet, J. Neuroreport (1996) [Pubmed]
  13. Impaired genomic stability and increased oxidative stress exacerbate different features of Ataxia-telangiectasia. Ziv, S., Brenner, O., Amariglio, N., Smorodinsky, N.I., Galron, R., Carrion, D.V., Zhang, W., Sharma, G.G., Pandita, R.K., Agarwal, M., Elkon, R., Katzin, N., Bar-Am, I., Pandita, T.K., Kucherlapati, R., Rechavi, G., Shiloh, Y., Barzilai, A. Hum. Mol. Genet. (2005) [Pubmed]
  14. CuZn-SOD Deficiency Causes ApoB Degradation and Induces Hepatic Lipid Accumulation by Impaired Lipoprotein Secretion in Mice. Uchiyama, S., Shimizu, T., Shirasawa, T. J. Biol. Chem. (2006) [Pubmed]
  15. Superoxide-mediated cytotoxicity in superoxide dismutase-deficient fetal fibroblasts. Huang, T.T., Yasunami, M., Carlson, E.J., Gillespie, A.M., Reaume, A.G., Hoffman, E.K., Chan, P.H., Scott, R.W., Epstein, C.J. Arch. Biochem. Biophys. (1997) [Pubmed]
  16. Antioxidant enzyme levels as a function of growth state in cell culture. Oberley, T.D., Schultz, J.L., Li, N., Oberley, L.W. Free Radic. Biol. Med. (1995) [Pubmed]
  17. An imbalance in antioxidant defense affects cellular function: the pathophysiological consequences of a reduction in antioxidant defense in the glutathione peroxidase-1 (Gpx1) knockout mouse. De Haan, J.B., Crack, P.J., Flentjar, N., Iannello, R.C., Hertzog, P.J., Kola, I. Redox Rep. (2003) [Pubmed]
  18. Antioxidant enzyme activities in normal and transformed mouse liver cells. Sun, Y., Oberley, L.W., Elwell, J.H., Sierra-Rivera, E. Int. J. Cancer (1989) [Pubmed]
  19. Expression of genes encoding antioxidant enzymes in human and mouse oocytes during the final stages of maturation. El Mouatassim, S., Guérin, P., Ménézo, Y. Mol. Hum. Reprod. (1999) [Pubmed]
  20. Fibroblasts derived from Gpx1 knockout mice display senescent-like features and are susceptible to H2O2-mediated cell death. de Haan, J.B., Bladier, C., Lotfi-Miri, M., Taylor, J., Hutchinson, P., Crack, P.J., Hertzog, P., Kola, I. Free Radic. Biol. Med. (2004) [Pubmed]
  21. Organ-specific gene expressions in C57BL/6 mice after exposure to low-dose radiation. Lee, W.J., Majumder, Z.R., Jeoung, D.I., Lee, H.J., Kim, S.H., Bae, S., Lee, Y.S. Radiat. Res. (2006) [Pubmed]
  22. Antioxidant enzyme response to hypericin in EMT6 mouse mammary carcinoma cells. Johnson, S.A., Pardini, R.S. Free Radic. Biol. Med. (1998) [Pubmed]
  23. Relationship of resistance to oxygen free radicals to CuZn-superoxide dismutase activity in transgenic, transfected, and trisomic cells. Huang, T.T., Carlson, E.J., Leadon, S.A., Epstein, C.J. FASEB J. (1992) [Pubmed]
  24. Age-related changes in antioxidant enzymes and lipid peroxidation in brains of control and transgenic mice overexpressing copper-zinc superoxide dismutase. Ceballos-Picot, I., Nicole, A., Clément, M., Bourre, J.M., Sinet, P.M. Mutat. Res. (1992) [Pubmed]
  25. High-resolution mapping of D16led-1, Gart, Gas-4, Cbr, Pcp-4, and Erg on distal mouse chromosome 16. Mjaatvedt, A.E., Citron, M.P., Reeves, R.H. Genomics (1993) [Pubmed]
  26. Genetic mapping of two DNA markers, D16Ros1 and D16Ros2, flanking the mutation site in the chakragati mouse, a transgenic insertional mutant. Ratty, A.K., Matsuda, Y., Elliott, R.W., Chapman, V.M., Gross, K.W. Mamm. Genome (1992) [Pubmed]
  27. Deletions are easy detectable in cochlear mitochondrial DNA of Cu/Zn superoxide dismutase gene knockout mice. Zhang, X., Han, D., Ding, D., Dai, P., Yang, W., Jiang, S., Salvi, R.J. Chin. Med. J. (2002) [Pubmed]
  28. Glutathione peroxidase-1 contributes to the neuroprotection seen in the superoxide dismutase-1 transgenic mouse in response to ischemia/reperfusion injury. Crack, P.J., Taylor, J.M., de Haan, J.B., Kola, I., Hertzog, P., Iannello, R.C. J. Cereb. Blood Flow Metab. (2003) [Pubmed]
  29. Extracellular superoxide dismutase tissue distribution and the patterns of superoxide dismutase mRNA expression following ultraviolet irradiation on mouse skin. Choung, B.Y., Byun, S.J., Suh, J.G., Kim, T.Y. Exp. Dermatol. (2004) [Pubmed]
  30. Cellular clones and transgenic mice overexpressing copper-zinc superoxide dismutase: models for the study of free radical metabolism and aging. Ceballos-Picot, I., Nicole, A., Sinet, P.M. EXS. (1992) [Pubmed]
  31. Cloning and sequencing of a rat CuZn superoxide dismutase cDNA. Correlation between CuZn superoxide dismutase mRNA level and enzyme activity in rat and mouse tissues. Delabar, J.M., Nicole, A., D'Auriol, L., Jacob, Y., Meunier-Rotival, M., Galibert, F., Sinet, P.M., Jérôme, H. Eur. J. Biochem. (1987) [Pubmed]
WikiGenes - Universities