SOD1 and amyotrophic lateral sclerosis: Mutations and oligomerization

PLoS ONE

Volumn 3, Issue 2, 2008, Pages

  Banci, Lucia ^a,b   Bertini, Ivano ^a   Boca, Mirela ^a   Girotto, Stefania ^a   Martinelli, Manuele ^a   Valentine, Joan Selverstone ^c   Vieru, Miguela ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

^b FiorGen Foundation   (Italy)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; CYSTEINE; MUTANT PROTEIN; METAL; SUPEROXIDE DISMUTASE;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; GEL FILTRATION CHROMATOGRAPHY; GENE LOCUS; GENE MUTATION; HYDROGEN BOND; MITOCHONDRION; NONHUMAN; OLIGOMERIZATION; OXIDATIVE STRESS; CHEMISTRY; DIMERIZATION; GENETICS; HUMAN; KINETICS; METABOLISM; MUTATION; OXIDATION REDUCTION REACTION; PROTEIN CONFORMATION;

AMYOTROPHIC LATERAL SCLEROSIS; CYSTEINE; DIMERIZATION; HUMANS; HYDROGEN BONDING; KINETICS; METALS; MITOCHONDRIA; MUTATION; OXIDATION-REDUCTION; PROTEIN CONFORMATION; SUPEROXIDE DISMUTASE;

EID: 45949083132     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0001677     Document Type: Article

References (30)

1. Bruijn LI, Miller TM, Cleveland DW (2004) Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci 27: 723-749.
2. Rosen DR (1993) Mutation in Cu,Zn superoxide dismutase gene are associated with familial amyotrophyc lateral sclerosis. Nature 362: 59-62.
3. Valentine JS, Doucette PA, Potter SZ (2005) Copper-Zinc Superoxide Dismutase and Amyotrophic Lateral Sclerosis. Annu Rev Biochem 74: 563-593.
4. Andersen PM (2006) Amyotrophic lateral sclerosis associated with mutations in the CuZn superoxide dismutase gene. Curr Neurol Neurosci Rep 6: 37-46.
5. Tu PH, Raju P, Robinson KA, Gurney ME, Trojanowski JQ, et al. (1996) Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions. Proc Natl Acad Sci U S A 93: 3155-3160.
6. Valentine JS, Hart PJ (2003) Misfolded CuZnSOD and amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 100: 3617-3622.
7. Lindberg MJ, Bystrom R, Boknas N, Andersen PM, Oliveberg M (2005) Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)- associated SOD1 mutants. Proc Natl Acad Sci U S A 102: 9754-9759.
8. Furukawa Y, O'Halloran TV (2005) Amyotrophic Lateral Sclerosis Mutations Have the Greatest Destabilizing Effect on the Apo- and Reduced Form of SOD1, Leading to Unfolding and Oxidative Aggregation. J Biol (Chem 280: 17266-17274.
9. Taylor JP, Hardy J, Fischbeck KH (2005) Toxic proteins in neurodegenerative disease. Science 296: 1991-1995.
10. Bruijn LI, Houseweart MK, Kato S, Anderson KL, Anderson SD, et al. (1998) Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281: 1851-1854.
11. Ross CA, Poirier MA (2006) Protein Aggregation and Neurodegenerative Disease. Nat Med 10: S10-17.
12. Fridovich I (1978) The biology of oxygen radicals. Science 201: 875-879.
13. Bertini I, Mangani S, Viezzoli MS (1998) Advanced Inorganic Chemistry. San Diego: Academic Press. pp 127-250.
14. Culotta VC, Yang M, O'Halloran TV (2006) Activation of superoxide dismutases: putting the metal to the pedal. Biochim Biophys Acta 1763: 747-758.
15. Arnesano F, Banci L, Bestini I, Martinelli M, Furukawa Y, et al. (2004) The unusually stable quaternary structure of human SOD1 is controlled by both metal occupancy and disulfide status. J Biol Chem 279: 47998-48003.
16. Banci L, Bertini I, Durazo A, Girotto S, Gralla EB, et al. (2007) Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS. Proc Natl Acad Sci U S A 104: 11263-11267.
17. Krebs MR, Bromley EH, Donald AM (2005) The binding of thioflavin-T to amyloid fibrils: localisation and implications. J Struct Biol 149: 30-37.
18. Banci L, Bertini I, Cabelli DE, Hallewell RA, Tung JW, et al. (1991) A characterization of copper/zinc superoxide dismutase mutants at position 124 - Zinc-deficient proteins. Eur J Biochem 196: 123-128.
19. Ohi T, Nabeshima K, Kato S, Yazawa S, Tacheki S (2004) Familial amyotrophic lateral sclerosis with His46Arg mutation in Cu/Zn superoxide dismutase presenting characteristic clinical features and Lewy body-like hyaline inclusions. J Neurol Sci 225: 19-25.
20. Pasinelli P, Belford ME, Lennon N, Bacskai BJ, Hyman BT, et al. (2004) Amyotrophic Lateral Sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron 43: 19-30.
21. Stathopulos PB, Rumfeldt JAO, Scholz GA, Irani RA, Frey HE, et al. (2003) Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro. Proc Natl Acad Sci U S A 100: 7021-7026.
22. Tiwari A, Xu Z, Hayward LJ (2005) Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis. J.Biol.Chem. 280: 29771-29779.
23. Field LS, Furukawa Y, O'Halloran TV, Culotta VC (2003) Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. J.Biol.Chem. 278: 28052-28059.
24. Potter SZ, Valentine JS (2003) The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease). J Biol Inorg Chem. 8: 373-380.
25. Lindberg MJ, Tibell L, Oliveberg M (2002) Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state. Proc Natl Acad Sci U. S. A 99: 16607-16612.
26. Ferri A, Cozzolino M, Crosio C, Nencini M, Casciati A, et al. (2006) Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials. Proc Natl Acad Sci U S A 103: 13860-13865.
27. Niwa J, Yamada S, Ishigaki S, Sone J, Takahashi M, et al. (2007) Disulfide Bond Mediates Aggregation, Toxicity, and Ubiquitylation of Familial Amyotrophic Lateral Sclerosis-linked Mutant SOD1. J Biol Chem 282: 28087-28095.
28. Banci L, Benedetto M, Bertini I, Del Conte R, Piccioli M, et al. (1998) Solution structure of reduced monomeric Q133M2 Copper, Zinc Superoxide Dismutase. Why is SOD a dimeric enzyme? Biochemistry 37: 11780-11791.
29. McCord JM, Fridovich I (1969) Superoxide dismutase. Enzymic function for erythrocuprein. J Biol Chem 244: 6049-6055.
30. Deleage G, Geourjon C (1993) An interactive graphic programme for calculating the secondary structures content of proteins from circular dichroism spectrum. Comp Appl Biosc 9: 197-199.