Alterations in anti-oxidative defence enzymes in erythrocytes from sporadic amyotrophic lateral sclerosis (SALS) and familial ALS patients

Clinical Chemistry and Laboratory Medicine

Volumn 44, Issue 5, 2006, Pages 589-593

  Nikolić Kokić, Aleksandra ^a   Stević, Zorica ^b   Blagojević, Duško ^a   Davidović, Biljana ^a   Jones, David R ^c   Spasić, Mihajlo B ^a,c  

^a UNIVERSITY OF BELGRADE   (Serbia)

^b UNIVERSITY OF BELGRADE   (Serbia)

^c UNIVERSITY OF BELGRADE   (Serbia)

Author keywords

Amyotrophic lateral sclerosis; Anti oxidant defence enzymes; Copper zinc superoxide dismutase (CuZn SOD); Erythrocytes

Indexed keywords

ANTIOXIDANT; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; DIETHYLTHIOCARBAMATE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE; NITRIC OXIDE; REACTIVE OXYGEN METABOLITE;

ADULT; AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; BLOOD SAMPLING; CLINICAL ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MODIFICATION; ERYTHROCYTE COUNT; FAMILIAL DISEASE; FEMALE; GENE; GENE MUTATION; HIGH RISK PATIENT; HUMAN; MALE; PATHOGENESIS; PRIORITY JOURNAL; SOD1 GENE;

EID: 33646683583     PISSN: 14346621     EISSN: 14346621     Source Type: Journal    
DOI: 10.1515/CCLM.2006.111     Document Type: Article

References (45)

1. Patterson D, Warner HR, Fox LM, Rahmani Z. Superoxide dismutase, oxygen radical metabolism, and amyotrophic lateral sclerosis. Mol Genet Med 1994;4:79-118.
2. Tohgi H, Abe T, Yamazaki K, Murata T, Ishizaki E, Isobe C. Increase in oxidized NO products and reduction in oxidized glutathione in cerebrospinal fluid from patients with sporadic form of amyotrophic lateral sclerosis. Neurosci Lett 1999;260:204-6.
3. Nikolić Kokić A, Stević Z, Stojanović S, Blagojević PD, Jones DR, Pavlović S, et al. Biotransformation of nitric oxide in the cerebrospinal fluid of amyotrophic lateral sclerosis patients Redox Rep 2005;10:265-70.
4. Przedborski S, Donaldson DM, Murphy PL, Hirsch O, Lange D, Naini AB, et al. Blood superoxide dismutase, catalase and glutathione peroxidase activities in familial and sporadic amyotrophic lateral sclerosis. Neurodegeneration 1996;5:57-64.
5. Apostolski S, Marinkovic Z, Nikolic A, Blagojevic D, Spasic MB, Michelson AM. Glutathione peroxidase in amyotrophic lateral sclerosis: the effects of selenium supplementation. J Environ Pathol Toxicol Oncol 1998;17:325-9.
6. Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, Hentati A, et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993;362:59-62.
7. Bonnefont-Rousselot D, Lacomblez L, Jaudon M, Lepage S, Salachas F, Bensimon G, et al. Blood oxidative stress in amyotrophic lateral sclerosis. J Neurol Sci 2000;178:57-62.
8. Beal MF, Ferrante RJ, Browne SE, Matthews RT, Kowall NW, Brown RH Jr. Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann Neurol 1997;42:644-54.
9. Bruijn LI, Beal MF, Becher MW, Schulz JB, Wong PC, Price DL, et al. Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant. Proc Natl Acad Sci USA 1997;94:7606-11.
10. Andrus PK, Fleck TJ, Gurney ME, Hall ED. Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis. J Neurochem 1998;71:2041-8.
11. Hall ED, Andrus PK, Oostveen JA, Fleck TJ, Gurney ME. Relationship of oxygen radical-induced lipid peroxidative damage to disease onset and progression in a transgenic model of familial ALS. J Neurosci Res 1998;53:66-77.
12. Liochev SI, Fridovich I. Copper- and zinc-containing superoxide dismutase can act as a superoxide reductase and a superoxide oxidase. J Biol Chem 2000;275:38482-5.
13. Durham HD, Roy J, Dong L, Figlewich DA. Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J Neuropathol Exp Neurol 1997;56:523-30.
14. Estevez AG, Crow JP, Sampson JB, Reiter C, Zhuang Y, Richardson GJ, et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science 1999;286:2498-500.
15. Wiedau-Pazos M, Goto JJ, Rabizadeh S, Gralla EB, Roe JA, Lee MK, et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 1996;271:515-8.
16. Simpson EP, Yen AA, Appel SH. Oxidative stress: a common denominator in the pathogenesis of amyotrophic lateral sclerosis. Curr Opin Rheumatol 2003;15:730-6.
17. Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 1979;59:527-605.
18. Gul M, Kutay FZ, Temocin S, Hanninen O. Cellular and clinical implications of glutathione. Indian J Exp Biol 2000;38:625-34.
19. Andersen HR, Nielsen JB, Nielsen F, Grandjean P. Anti-oxidative enzyme activity in human erythrocytes. Clin Chem 1997;43:562-8.
20. Sinet PM, Lavelle F, Michelson AM, Jerome H. Superoxide dismutase activities of blood platelets in Trisomy 21. Biochem Biophys Res Commun 1975;67:904-9.
21. Sinet PM, Michelson AM, Bazin A, Lejeune J, Jerome H. Increase in glutathione peroxidase activity in erythrocytes from Trisomy 21 subjects. Biochem Biophys Res Commun 1975;67:910-5.
22. Pastor MC, Sierra C, Dolade M, Navarro E, Brandi N, Cabre E, et al. Antioxidant enzymes and fatty acid status in erythrocytes of Down syndrome patients. Clin Chem 1998;44:924-9.
23. Ferri A, Nencini M, Casciati A, Cozzolino M, Angelini DF, Longone P, et al. Cell death in amyotrophic lateral sclerosis: interplay between neuronal and glial cells. FASEB J 2004;18:1261-3.
24. Brooks BR. El escorial World Federation of Neurology criteria for the diagnosis of amyotrophic lateral sclerosis. J Neurol Sci 1994;124(Suppl 1):96-107.
25. Norris FH Jr, Calanchini PR, Fallat RJ, Panchari S, Jewett B. The administration of guanidine in amyotrophic lateral sclerosis. Neurology 1974;24:721-8.
26. Tsuchihashi M. Zur Kenntnis der Blutkatalase. Biochem Z 1923;140:65-74.
27. McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969;244:6049-55.
28. Beutler E. Catalase: a manual of biochemical methods. In: Beutler E, editor. Red cell metabolism. New York: Grune and Stratton, 1982:105-6.
29. Paglia DE, Valentine WN. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 1967;70:74-7.
30. Glatzle D, Vuilleumier JP, Weber F, Decker K. Glutathione reductase test with whole blood: a convenient procedure for the assessment of the riboflavin status in humans. Experientia 1974;30:665-8.
31. Drabkin D, Austin H. Spectrophotometric studies: preparations from washed blood cells. J Biol Chem 1935;112:51-5.
32. Hinkle ED, Wiersma W, Jurs GS. Applied statistics for behavioral sciences, 3rd ed. Boston, MA: Houghton Mifflin Company, 1994.
33. Manley BFJ. Multivariate statistical methods. A primer. London: Chapman and Hall, 1986.
34. Blagojevic D, Buzadzic B, Korac B, Saicic ZS, Radojicic R, Spasic MB, et al. Seasonal changes in the antioxidant defense in ground squirrel (Citellus citellus): possible role of GSH-Px. J Environ Pathol Toxicol Oncol 1998;17:241-50.
35. Jovanović-Galović A, Blagojević DP, Grubor-Lajšić G, Worland R, Spasić MB. Role of anti-oxidant defense during different stages of preadult life cycle in European corn borer (Ostrinia nubilalis, Hubn.): diapause and metamorphosis. Arch Insect Biochem Physiol 2004;55:79-89.
36. Perluigi M, Fai Poon H, Hensley K, Pierce WM, Klein JB, Calabrese V, et al. Proteomic analysis of 4-hydroxy-2-nonenal-modified proteins in G93A-SOD1 transgenic mice - a model of familial amyotrophic lateral sclerosis. Free Radic Biol Med 2005;38:960-8.
37. Nikolić A, Blagojević D, Stević Z, Niketić V, Saičić ZS, Spasić MB. Activities of AD enzymes in the blood of ALS patients - base for use of anti-oxidants in the treatment of ALS. In: Proceedings of the 11th Biennial Meeting of the Society for Free Radical Research International, 2002. Bologna, Italy: Medimond srl-Monduzzi Editore, 2002:323-6.
38. Mase G, Ros S, Gemma A, Bonfigli L, Carraro N, Cazzato G, et al. ALS with variable phenotypes in a six-generation family caused by leu144phe mutation in the SOD1 gene. J Neurol Sci 2001;191:11-8.
39. Oteiza PI, Uchitel OD, Carrasquedo F, Dubrovski AL, Roma JC, Fraga CG. Evaluation of anti-oxidants, protein, and lipid oxidation products in blood from sporadic amyotrophic lateral sclerosis patients. Neurochem Res 1997;22:535-9.
40. Dobashi K, Pahan K, Chahal A, Singh I. Modulation of endogenous antioxidant enzymes by nitric oxide in rat C6 glial cells. J Neurochem 1997;68:1896-903.
41. Kim YS, Han S. Nitric oxide protects Cu,Zn-superoxide dismutase from hydrogen peroxide-induced inactivation. FEBS Lett 2000;479:25-8.
42. Niketic V, Stojanovic S, Nikolic A, Spasic M, Michelson AM. Exposure of Mn and Fe SODs, but not Cu/Zn SOD, to NO leads to nitrosonium and nitroxyl ions generation which cause enzyme modification and inactivation: an in vitro study. Free Radic Biol Med 1999;27:992-6.
43. Poon HF, Hensley K, Thongboonkerd V, Merchant ML, Lynn BC, Pierce WM, et al. Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice - a model of familial amyotrophic lateral sclerosis. Free Radic Biol Med 2005;39:453-62.
44. Bruijn LI, Miller TM, Cleveland DW. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci 2004;27:723-49.
45. Pioro E. Antioxidant therapy in ALS. Amyotroph Lateral Scler Other Motor Neuron Disord 2000;4:5-15.