Do posttranslational modifications of CuZnSOD lead to sporadic amyotrophic lateral sclerosis?

Annals of Neurology

Volumn 42, Issue 2, 1997, Pages 135-137

  Bredesen, D E ^a   Ellerby, L M ^a   Hart, P J ^a   Wiedau Pazos, M ^a   Valentine, J S ^a  

^a BURNHAM INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; AMYOTROPHIC LATERAL SCLEROSIS; ENZYME GLYCOSYLATION; GENE MUTATION; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; REVIEW;

EID: 0030811118     PISSN: 03645134     EISSN: None     Source Type: Journal    
DOI: 10.1002/ana.410420202     Document Type: Review

References (25)

1. 1 Rosen D, Siddique T, Patterson D, et al. Mutations in Cu, Zn superoxide dismutase gene are associated with familial amyotrophic laterals clerosis. Nature 1993 ; 362: 59–62
2. 2 Gurney ME, Pu H, Chiu AY, et al. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science 1994 ; 264: 1772–1775
3. 3 Rabizadeh S, Gralla EB, Borchelt DR, et al. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. Proc Natl Acad Sci USA 1995 ; 92: 3024–3028
4. 4 Siddique T, Deng H‐X. Genetics of amyotrophic lateral sclerosis. Hum Mol Genet 1996 ; 5: 1465–1470
5. 5 Deng H. Amyotrophic lateral sclerosis and structural defects in Cu, ZnSOD. Science 1993 ; 262: 1047–1051
6. 6 Brown RH Jr. Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell 1995 80: 687–692
7. 7 Wiedau‐Pazos M, Goto JJ, Rabizadeh S, et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 1996 271: 515–518
8. 8 Lyons TJ, Liu H, Goto JJ, et al. Mutant copper‐zinc superoxide dismutase proteins with defective zinc binding sites and altered redox behavior from patients with amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 1996 93: 12240–12244
9. 9 Yim MB, Kang J‐H, Yim H‐S, et al. A gain‐of‐function of an amyotrophic lateral sclerosis‐associated Cu, Zn‐superoxide dismutase mutant: an enhancement of free radical formation due to a decrease in K m for hydrogen peroxide. Proc Natl Acad Sci USA 1996 93: 5709–5714
10. 10 Beckman JS, Carson M, Smith CD, Koppenol WH. ALS, SOD and peroxynitrite. Nature 1993 364: 584 (Letter)
11. 11 Arai K, Maguchi S, Fujii S, et al. Glycation and inactivation of human Cu, Zn superoxide dismutase. Identification of the in vitro glycated sites. J Biol Chem 1987 262: 16969–16972
12. 12 Takata I, Kawamura N, Myint T, et al. Glycated Cu, Zn superoxide dismutase in rat lenses: evidence for the presence of fragmentation in vivo. Biochem Biophys Res Commun 1996 219: 243–248
13. 13 Li P‐F, Fang Y‐Z, Lu X. Oxidative modification of bovine erythrocyte superoxide dismutase by hydrogen peroxide and ascorbate‐Fe(III). Biochem Mol Biol Int 1993 29: 929–937
14. 14 Santa Maria C, Revilla E, Ayala A, et al. Changes in the histidine residues of Cu, Zn superoxide dismutase during aging. FEBS Lett 1995 374: 85–88
15. 15 Reiss U, Gershon D. Rat‐liver superoxide dismutase: purification and age‐related modifications. Eur J Biochem 1976 63: 617–623
16. 16 Stadman ER. Protein oxidation and aging. Science 1992 257: 12200–12204
17. 17 Schinina ME, Carlini P, Folticelli F, et al. Amino acid sequence of chicken Cu, Zn‐containing superoxide dismutase and identification of glutathionyl adducts at exposed cysteine residues. Eur J Biochem 1996 237: 433–439
18. 18 Salo DC, Pacifici RE, Lin SW, et al. Superoxide dismutase undergoes protoelysis and fragmentation following oxidative modification and inactivation. J Biol Chem 1990 ; 265: 11919–11927
19. 19 Iwasaki Y, Ikeda K, Kinoshita M. Decreased cerebrospinal‐fluid superoxide dismutase in amyotrophic lateral sclerosis. Lancet 1993 342: 1118 (Letter)
20. 20 Bowling AC, Schulz JB, Brown RH Jr, Beal MF. Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J Neurochem 1993 61: 2322–2325
21. 21 Cohen O, Kohen R, Lavon E, et al. Serum Cu, Zn superoxide dismutase activity is reduced in sporadic amyotrophic lateral sclerosis patients. J Neurol Sci 1996 143: 118–120
22. 22 Ookawara T, Kawamura N, Kitagawa Y, Taniguchi N. Site‐specific and random fragmentation of Cu, Zn superoxide dismutase by glycation reaction. Implication of reactive oxygen species. J Biol Chem 1992 267: 18505–18510
23. 23 Kraulis PJ, MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991 24: 946–950
24. 24 Bacon DJ, Anderson WF. A fast algorithm for rendering spacefilling molecule pictures (abstract of article presented at the Seventh Annual Meeting of the Molecular Graphics Society). J Mol Graph 1988 6: 219–220 (Abstract)
25. 25 Merritt EA, Murphy MEP. Raster 3D Version 2.0—a program for photorealistic molecular graphics. Acta Crystallogr D 1994 50: 869–873