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SOD1  -  superoxide dismutase 1, soluble

Canis lupus familiaris

 
 
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Disease relevance of SOD1

 

High impact information on SOD1

  • We developed and characterised a cell model consisting of polarised epithelial Madin-Darby Canine Kidney (MDCK) cell lines stably expressing wild-type SOD1 or the ALS-linked SOD1 G93A mutant, and analysed the expression of glutamate transporters after transient transfection of the corresponding cDNAs [2].
  • Its loss and an increase in extracellular glutamate has been documented in cases of sporadic and familial ALS, as well as in animal models expressing ALS-linked Cu2+-Zn2+ superoxide dismutase (SOD1) mutations, but the underlying molecular mechanisms are still unclear [2].
  • Oxidative stress was measured by determining GSH/GSSG ratios and gene-expression (SOD1, CAT, GSHS, GPX1, CCS, p27KIP, Bcl-2) [3].
 

Anatomical context of SOD1

  • Moreover, mutant SOD1 affected the cytosolic tail of GLT-1 because reduced protein expression of EAAC-GLT but not GLT-EAAC chimeras was found in G93A-expressing cell lines [2].
 

Analytical, diagnostic and therapeutic context of SOD1

  • The canine SOD1 gene maps to CFA31 close to syntenic group 13 on the radiation hybrid (RH) map in the vicinity of sodium myo/inositol transporter (SMIT) gene [1].

References

  1. Structure, chromosomal location, and analysis of the canine Cu/Zn superoxide dismutase (SOD1) gene. Green, S.L., Tolwani, R.J., Varma, S., Quignon, P., Galibert, F., Cork, L.C. J. Hered. (2002) [Pubmed]
  2. Increased internalisation and degradation of GLT-1 glial glutamate transporter in a cell model for familial amyotrophic lateral sclerosis (ALS). Vanoni, C., Massari, S., Losa, M., Carrega, P., Perego, C., Conforti, L., Pietrini, G. J. Cell. Sci. (2004) [Pubmed]
  3. Copper metabolism and oxidative stress in chronic inflammatory and cholestatic liver diseases in dogs. Spee, B., Arends, B., van den Ingh, T.S., Penning, L.C., Rothuizen, J. J. Vet. Intern. Med. (2006) [Pubmed]
 
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