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Gene Review

Sod  -  Superoxide dismutase

Drosophila melanogaster

Synonyms: CG11793, Cu, Cu-Zn SOD, Cu/Zn SOD, Cu/Zn sod, ...
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Disease relevance of Sod

  • We tested the hypothesis that the Drosophila Cu,Zn SOD is capable of protecting Escherichia coli from oxidative damage caused by the herbicide paraquat [1].
  • Phenotypic effects of familial amyotrophic lateral sclerosis mutant Sod alleles in transgenic Drosophila [2].
  • This striking differential restoration of pleiotropic phenotypes could be the result of a threshhold of CuZnSOD expression necessary for normal male fertility and resistance to the toxicity of paraquat or hyperoxia which is lower than the threshold required to sustain a normal adult life span [3].
  • The O. volvulus cytosolic and extracellular CuZnSOD genes (Ov-sod-1 and Ov-sod-2) are separated by 0.8 kb of sequence and are convergently transcribed [4].
  • Our results show that, although the low-activity CuZnSOD allele of D. melanogaster confers hypersensitivity to paraquat, the near UV radiation damage was not affected [5].

Psychiatry related information on Sod


High impact information on Sod

  • Altogether, these data show that increased expression of SOD1 is not required for the evolution of extreme lifespan, even in a system in which differential gene expression is the only way to express phenotypes with great lifespan differences [7].
  • Moreover, interspecific comparisons show lower levels of antioxidant activities in longer-lived species, suggesting that life-span extension may evolve through less reactive oxygen species generation from the mitochondria rather than higher expression of SOD1 [7].
  • The tremendous variation in lifespan between ant castes, ranging over 2 orders of magnitude, coupled with the fact that all individuals share the same genome, provides a system to investigate the role of SOD1 in the wild [7].
  • Patterns of DNA sequence polymorphism at Sod vicinities in Drosophila melanogaster: unraveling the footprint of a recent selective sweep [8].
  • The human wild-type and five FALS Sod mutant transgenes were introduced into the fruit fly, Drosophila melanogaster, in a Cu-Zn Sod null background [2].

Biological context of Sod


Anatomical context of Sod


Associations of Sod with chemical compounds

  • We also report that glutathione (GSH) depletion induced by administration of buthionine sulfoximine (BSO) selectively reduces the viability of mutants lacking CuZnSOD [15].
  • Overexpression of Cu,Zn-SOD and catalase caused a retardation in the accumulation of 8-hydroxydeoxyguanosine during aging and in response to the exposure of live flies to x-rays [16].
  • Copper-zinc superoxide dismutase appears to be a very erratic evolutionary clock [17].
  • Homozygotes are viable as larvae, which indicates that cSOD is not essential for cell viability per se. cSODn108 confers recessive sensitivity to the superoxide anion (O2-)-generator paraquat and to the transition metal compound CuSO4, which indicates that the cSOD-null condition in fact leads to impaired O2- metabolism [18].
  • The gene for cytoplasmic superoxide dismutase (cSOD) maps within this interval, as does low xanthine dehydrogenase (lxd).--Recessive lethal mutations were generated within the region by ethyl methanesulfonate mutagenesis and by hybrid dysgenesis [19].

Other interactions of Sod

  • Significant increases in the activities of both CuZn-SOD and catalase had no beneficial effect on survivorship in relatively long-lived y w mutant flies and were associated with slightly decreased life spans in wild type flies of the Oregon-R strain [20].
  • This allowed us to confirm the results of (Clancy et al. 2001) and extend the results by measuring CuZn SOD and Mn SOD activities in addition to the previously determined overall SOD activity [9].
  • I review the evolution of two genes, Gpdh and Sod [21].
  • In addition, there are striking similarities to patterns of variation observed at the Est6 and Est-P loci, which are located approximately 1,000 kb from Sod [22].
  • The combined data for three genes (Adh, Sod, and Gpdh) statistically resolves outstanding issues [23].

Analytical, diagnostic and therapeutic context of Sod


  1. Drosophila Cu,Zn superoxide dismutase gene confers resistance to paraquat in Escherichia coli. Goulielmos, G.N., Arhontaki, K., Eliopoulos, E., Tserpistali, K., Tsakas, S., Loukas, M. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  2. Phenotypic effects of familial amyotrophic lateral sclerosis mutant Sod alleles in transgenic Drosophila. Mockett, R.J., Radyuk, S.N., Benes, J.J., Orr, W.C., Sohal, R.S. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  3. Phenotypic rescue by a bovine transgene in a Cu/Zn superoxide dismutase-null mutant of Drosophila melanogaster. Reveillaud, I., Phillips, J., Duyf, B., Hilliker, A., Kongpachith, A., Fleming, J.E. Mol. Cell. Biol. (1994) [Pubmed]
  4. Onchocerca volvulus superoxide dismutase genes: identification of functional promoters for pre-mRNA transcripts which undergo trans-splicing. Tawe, W., Walter, R.D., Henkle-Dührsen, K. Exp. Parasitol. (2000) [Pubmed]
  5. Low-activity allele of copper-zinc superoxide dismutase (CuZnSOD) in Drosophila increases paraquat genotoxicity but does not affect near UV radiation damage. Vontas, J.G., Tsakas, S.C., Loukas, M., Hemingway, J. Genome (2001) [Pubmed]
  6. Overexpression of Mn-containing superoxide dismutase in transgenic Drosophila melanogaster. Mockett, R.J., Orr, W.C., Rahmandar, J.J., Benes, J.J., Radyuk, S.N., Klichko, V.I., Sohal, R.S. Arch. Biochem. Biophys. (1999) [Pubmed]
  7. Decreased expression of Cu-Zn superoxide dismutase 1 in ants with extreme lifespan. Parker, J.D., Parker, K.M., Sohal, B.H., Sohal, R.S., Keller, L. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  8. Patterns of DNA sequence polymorphism at Sod vicinities in Drosophila melanogaster: unraveling the footprint of a recent selective sweep. Sáez, A.G., Tatarenkov, A., Barrio, E., Becerra, N.H., Ayala, F.J. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  9. Superoxide dismutase activities in long-lived Drosophila melanogaster females: chico (1) genotypes and dietary dilution. Kabil, H., Partridge, L., Harshman, L.G. Biogerontology (2007) [Pubmed]
  10. Genetic polymorphism at two linked loci, Sod and Est-6, in Drosophila melanogaster. Ayala, F.J., Balakirev, E.S., Sáez, A.G. Gene (2002) [Pubmed]
  11. FLP recombinase-mediated induction of Cu/Zn-superoxide dismutase transgene expression can extend the life span of adult Drosophila melanogaster flies. Sun, J., Tower, J. Mol. Cell. Biol. (1999) [Pubmed]
  12. Overexpression of Cu-Zn superoxide dismutase in Drosophila does not affect life-span. Seto, N.O., Hayashi, S., Tener, G.M. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  13. Superoxide and hydrogen peroxide production by Drosophila mitochondria. Miwa, S., St-Pierre, J., Partridge, L., Brand, M.D. Free Radic. Biol. Med. (2003) [Pubmed]
  14. CuZn-SOD promoter-driven expression in the Drosophila central nervous system. Klichko, V.I., Radyuk, S.N., Orr, W.C. Neurobiol. Aging (1999) [Pubmed]
  15. Genetic and biochemical analysis of glutathione-S-transferase in the oxygen defense system of Drosophila melanogaster. Parkes, T.L., Hilliker, A.J., Phillips, J.P. Genome (1993) [Pubmed]
  16. Simultaneous overexpression of copper- and zinc-containing superoxide dismutase and catalase retards age-related oxidative damage and increases metabolic potential in Drosophila melanogaster. Sohal, R.S., Agarwal, A., Agarwal, S., Orr, W.C. J. Biol. Chem. (1995) [Pubmed]
  17. Complete amino acid sequence of copper-zinc superoxide dismutase from Drosophila melanogaster. Lee, Y.M., Friedman, D.J., Ayala, F.J. Arch. Biochem. Biophys. (1985) [Pubmed]
  18. Null mutation of copper/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity. Phillips, J.P., Campbell, S.D., Michaud, D., Charbonneau, M., Hilliker, A.J. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  19. Cytogenetic analysis of the cSOD microregion in Drosophila melanogaster. Campbell, S.D., Hilliker, A.J., Phillips, J.P. Genetics (1986) [Pubmed]
  20. Effects of overexpression of copper-zinc and manganese superoxide dismutases, catalase, and thioredoxin reductase genes on longevity in Drosophila melanogaster. Orr, W.C., Mockett, R.J., Benes, J.J., Sohal, R.S. J. Biol. Chem. (2003) [Pubmed]
  21. Vagaries of the molecular clock. Ayala, F.J. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  22. DNA variation at the Sod locus of Drosophila melanogaster: an unfolding story of natural selection. Hudson, R.R., Sáez, A.G., Ayala, F.J. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  23. Phylogeny of Drosophila and related genera: conflict between molecular and anatomical analyses. Kwiatowski, J., Ayala, F.J. Mol. Phylogenet. Evol. (1999) [Pubmed]
  24. Cloning, sequence analysis and chromosomal localization of the Cu-Zn superoxide dismutase gene of Drosophila melanogaster. Seto, N.O., Hayashi, S., Tener, G.M. Gene (1989) [Pubmed]
  25. Isolation and chromosomal localization of genomic DNA sequences coding for cytoplasmic superoxide dismutase from Drosophila melanogaster. Kirkland, K.C., Phillips, J.P. Gene (1987) [Pubmed]
  26. Immunological confirmation of elevated levels of CuZn superoxide dismutase protein in an artificially selected long-lived strain of Drosophila melanogaster. Hari, R., Burde, V., Arking, R. Exp. Gerontol. (1998) [Pubmed]
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