Advanced search
Publication Cover
Amyotrophic Lateral Sclerosis Volume 12, 2011 - Issue 3
Journal homepage
271
Views
15
CrossRef citations to date
0
Altmetric
Research Article

A novel ALS SOD1 C6S mutation with implications for aggregation related toxicity and genetic counseling

Terrell Brotherton Department of Neurology, Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, Georgia, USA
,
Meraida Polak Department of Neurology, Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, Georgia, USA
,
Crystal Kelly Department of Neurology, Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, Georgia, USA
,
Anna Birve Department of Pharmacology and Clinical Neuroscience, Umeå University, Umeå, Sweden
,
Peter Andersen Department of Pharmacology and Clinical Neuroscience, Umeå University, Umeå, Sweden
,
Stefan L. Marklund Department of Medical Biosciences, Umeå University, Umeå, Sweden
&
Jonathan D. Glass Department of Neurology, Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, Georgia, USACorrespondence[email protected]
 show all
Pages 215-219 | Received 20 Aug 2010, Accepted 07 Oct 2010, Published online: 12 Nov 2010

References

  • Siddique T, Figlewicz DA, Pericak-Vance MA, Haines JL, Rouleau G, Jeffers AJ, . Linkage of a gene causing familial amyotrophic lateral sclerosis to chromosome 21 and evidence of genetic-locus heterogeneity. N Engl J Med. 1991; 324:1381–4.
  • Rosen DR. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993;364:362.
  • Tainer JA, Getzoff ED, Beem KM, Richardson JS, Richardson DC. Determination and analysis of the 2 A-structure of copper/zinc superoxide dismutase. J Mol Biol. 1982;160: 181–217.
  • Wroe R, Wai-Ling Butler A, Andersen PM, Powell JF, Al-Chalabi A. ALSOD: the Amyotrophic Lateral Sclerosis Online Database. Amyotroph Lateral Scler. 2008;9:249–50.
  • Kawamata H, Manfredi G. Different regulation of wild-type and mutant Cu/Zn superoxide dismutase localization in mammalian mitochondria. Hum Mol Genet. 2008;17: 3303–17.
  • den Dunnen JT, Antonarakis SE. Mutation nomenclature extensions and suggestions to describe complex mutations: a discussion. Hum Mutat. 2000;15:7–12.
  • Marklund S. Spectrophotometric study of spontaneous disproportionation of superoxide anion radical and sensitive direct assay for superoxide dismutase. J Biol Chem. 1976; 251:7504–7.
  • Jonsson PA, Ernhill K, Andersen PM, Bergemalm D, Brannstrom T, Gredal O, . Minute quantities of misfolded mutant superoxide dismutase 1 cause amyotrophic lateral sclerosis. Brain. 2004;127:73–88.
  • Andersen PM, Nilsson P, Forsgren L, Marklund SL. Cu/Zn superoxide dismutase, extracellular superoxide dismutase, and glutathione peroxidase in blood from individuals homozygous for Asp(90)Ala Cu/Zn superoxide dismutase mutation. J Neurochem. 1998;70:715–20.
  • Watanabe M, Dykes-Hoberg M, Culotta VC, Price DL, Wong PC, Rothstein JD. Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol Dis. 2001; 8:933–41.
  • Shibata N, Hirano A, Kobayashi M, Sasaki S, Kato T, Matsumoto S, . Cu/Zn superoxide dismutase-like immunoreactivity in Lewy body-like inclusions of sporadic amyotrophic lateral sclerosis. Neurosci Lett. 1994;179:149–52.
  • Shibata N, Hirano A, Kobayashi M, Siddique T, Deng HX, Hung WY, . Intense superoxide dismutase 1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement. J Neuropathol Exp Neurol. 1996;55:481–90.
  • Shibata N, Asayama K, Hirano A, Kobayashi M. Immunohistochemical study on superoxide dismutases in spinal cords from autopsied patients with amyotrophic lateral sclerosis. Dev Neurosci. 1996;18:492–8.
  • Johnston JA, Dalton MJ, Gurney ME, Kopito RR. Formation of high molecular weight complexes of mutant Cu/Zn superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A. 2000;97: 12571–6.
  • Kohno S, Takahashi Y, Miyajima H, Serizawa M, Mizoguchi K. A novel mutation (Cys6Gly) in the Cu/Zn superoxide dismutase gene associated with rapidly progressive familial amyotrophic lateral sclerosis. Neurosci Lett. 1999;276: 135–7.
  • Morita M, Aoki M, Abe K, Hasegawa T, Sakuma R, Onodera Y, . A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis in Japan. Neurosci Lett. 1996;205:79–82.
  • Siddique T, Deng HX. Genetics of amyotrophic lateral sclerosis. Hum Mol Genet. 1996;5:1465–70.
  • Ripps ME, Huntley GW, Hof PR, Morrison JH, Gordon JW. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. P Natl Acad Sci USA. 1995;92:689–93.
  • Karch CM, Borchelt DR. A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis. J Biol Chem. 2008;283: 13528–37.
  • Cozzolino M, Amori I, Pesaresi MG, Ferri A, Nencini M, Carri MT. Cysteine 111 affects aggregation and cytotoxicity of mutant Cu/Zn superoxide dismutase associated with familial amyotrophic lateral sclerosis. J Biol Chem. 2008; 283:866–74.
  • Niwa J, Yamada S, Ishigaki S, Sone J, Takahashi M, Katsuno M, . Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1. J Biol Chem. 2007;282:28087–95.
  • Felbecker A, Camu W, Valdmanis PN, Sperfeld AD, Waibel S, Steinbach P, . Four familial ALS pedigrees discordant for two SOD1 mutations: are all SOD1 mutations pathogenic? J Neurol Neurosur Ps. 2010;81:572–7.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.