Abstract
We examined oxidative stress markers of 31 patients suffering from ALS, 24 patients suffering from PD and 30 healthy subjects were included. We determined the plasma levels of lipid peroxidation (malondialdehyde, MDA), of protein oxidative lesions (plasma glutathione, carbonyls and thiols) and the activity of antioxidant enzymes i.e. erythrocyte Cu,Zn-Superoxide dismutase (SOD), Glutathione peroxidase (GSH-Px) and catalase. MDA and thiols were significantly different in both neurodegenerative diseases versus control population. A trend for an enhancement of oxidized glutathione was noted in ALS patients. Univariate analysis showed that SOD activity was significantly decreased in ALS and GSH-Px activity was decreased in PD. After adjusting for demographic parameters and enzyme cofactors, we could emphasize a compensatory increase of SOD activity in PD. Different antioxidant systems were not involved in the same way in ALS and PD, suggesting that oxidative stress may be a cause rather than a consequence of the neuronal death.
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Abbreviations
- ALS:
-
Amyotrophic lateral sclerosis
- EDTA:
-
Ethylenediaminetetraacetic acid
- GSH-Px:
-
Glutathione peroxidase
- MDA:
-
Malondialdehyde
- MOPS:
-
3-N-morpholinopropaneslfonic acid
- PD:
-
Parkinson’s disease
- SOD:
-
Cu,Zn-Superoxide dismutase
References
Evans PH, Yano E, Klinowski J et al (1992) Oxidative damage in Alzheimer’s dementia, and the potential etiopathogenic role of aluminosilicates, microglia and micronutrient interactions. Exs 62:178–189
Facheris M, Beretta S, Ferrarese C (2004) Peripheral markers of oxidative stress and excitotoxicity in neurodegenerative disorders: tools for diagnosis and therapy? J Alzheimers Dis 6:177–184
Bonnefont-Rousselot D, Lacomblez L, Jaudon M et al (2000) Blood oxidative stress in amyotrophic lateral sclerosis. J Neurol Sci 178:57–62
Siciliano G, D’Avino C, Del Corona A et al (2002) Impaired oxidative metabolism and lipid peroxidation in exercising muscle from ALS patients. Amyotroph Lateral Scler Other Motor Neuron Disord 3:57–62
Jenner P, Dexter DT, Sian J et al (1992) Oxidative stress as a cause of nigral cell death in Parkinson’s disease and incidental Lewy body disease. The Royal Kings and Queens Parkinson’s Disease Research Group. Ann Neurol 32(Suppl):S82–S87
Jenner P, Schapira AH, Marsden CD (1992) New insights into the cause of Parkinson’s disease. Neurology 42:2241–2250
Schapira AH, Mann VM, Cooper JM et al (1990) Anatomic and disease specificity of NADH CoQ1 reductase (complex I) deficiency in Parkinson’s disease. J Neurochem 55:2142–2145
Janetzky B, Hauck S, Youdim MB et al (1994) Unaltered aconitase activity, but decreased complex I activity in substantia nigra pars compacta of patients with Parkinson’s disease. Neurosci Lett 169:126–128
Parker WD Jr, Boyson SJ, Parks JK (1989) Abnormalities of the electron transport chain in idiopathic Parkinson’s disease. Ann Neurol 26:719–723
Singer TP, Castagnoli N Jr, Ramsay RR et al (1987) Biochemical events in the development of parkinsonism induced by 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine. J Neurochem 49:1–8
Przedborski S, Jackson-Lewis V, Djaldetti R et al (2000) The parkinsonian toxin MPTP: action and mechanism. Restor Neurol Neurosci 16:135–142
Greenamyre JT, Sherer TB, Betarbet R et al (2001) Complex I and Parkinson’s disease. IUBMB Life 52:135–141
Agil A, Duran R, Barrero F et al (2006) Plasma lipid peroxidation in sporadic Parkinson’s disease. Role of the L-dopa. J Neurol Sci 240:31–36
Rosen DR, Siddique T, Patterson D et al (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362:59–62
Oteiza PI, Uchitel OD, Carrasquedo F et al (1997) Evaluation of antioxidants, protein, and lipid oxidation products in blood from sporadic amyotrophic lateral sclerosis patients. Neurochem Res 22:535–539
Bogdanov M, Brown RH, Matson W et al (2000) Increased oxidative damage to DNA in ALS patients. Free Radic Biol Med 29:652–658
Beal MF, Ferrante RJ, Browne SE et al (1997) Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann Neurol 42:644–654
Shibata N, Nagai R, Uchida K et al (2001) Morphological evidence for lipid peroxidation and protein glycoxidation in spinal cords from sporadic amyotrophic lateral sclerosis patients. Brain Res 917:97–104
Cookson MR, Shaw PJ (1999) Oxidative stress and motor neurone disease. Brain Pathol 9:165–186
Grundman M (2000) Vitamin E and Alzheimer disease: the basis for additional clinical trials. Am J Clin Nutr 71:630S–636S
Sano M, Ernesto C, Thomas RG et al (1997) A controlled trial of selegiline, alpha-tocopherol, or both as treatment for Alzheimer’s disease. The Alzheimer’s Disease Cooperative Study. N Engl J Med 336:1216–1222
Ascherio A, Weisskopf MG, O’Reilly EJ et al (2005) Vitamin E intake and risk of amyotrophic lateral sclerosis. Ann Neurol 57:104–110
Desnuelle C, Dib M, Garrel C et al (2001) A double-blind, placebo-controlled randomized clinical trial of alpha-tocopherol (vitamin E) in the treatment of amyotrophic lateral sclerosis. ALS riluzole-tocopherol Study Group. Amyotroph Lateral Scler Other Motor Neuron Disord 2:9–18
Group TPS (1996) Impact of deprenyl and tocopherol treatment on Parkinson’s disease in DATATOP patients requiring levodopa. Parkinson Study Group. Ann Neurol 39:37–45
Group PS (1993) Effects of tocopherol and deprenyl on the progression of disability in early Parkinson’s disease. The Parkinson Study Group. N Engl J Med 328:176–183
Fukunaga K, Yoshida M, Nakazono N (1998) A simple, rapid, highly sensitive and reproducible quantification method for plasma malondialdehyde by high-performance liquid chromatography. Biomed Chromatogr 12:300–303
Ellman GL (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82:70–77
Levine RL, Garland D, Oliver CN et al (1990) Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol 186:464–478
Marklund S, Marklund G (1974) Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 47:469–474
Richard MJ, Belleville F, Chalas J et al (1997) Glutathione peroxidases: value of their determination in clinical biology. Ann Biol Clin (Paris) 55:195–207
Maehly AC, Chance B (1954) The assay of catalases and peroxidases. Methods Biochem Anal 1:357–424
Rowland LP (2000) Six important themes in amyotrophic lateral sclerosis (ALS) research, 1999. J Neurol Sci 180:2–6
Zarkovic K (2003) 4-Hydroxynonenal and neurodegenerative diseases. Mol Aspects Med 24:293–303
Martignoni E, Blandini F, Godi L et al (1999) Peripheral markers of oxidative stress in Parkinson’s disease. The role of L-DOPA. Free Radic Biol Med 27:428–437
Olanow CW, Tatton WG (1999) Etiology and pathogenesis of Parkinson’s disease. Annu Rev Neurosci 22:123–144
Saraymen R, Kilic E, Yazar S et al (2003) Influence of sex and age on the activity of antioxidant enzymes of polymorphonuclear leukocytes in healthy subjects. Yonsei Med J 44:9–14
Kawamoto EM, Munhoz CD, Glezer I et al (2005) Oxidative state in platelets and erythrocytes in aging and Alzheimer’s disease. Neurobiol Aging 26:857–864
Bracco F, Scarpa M, Rigo A et al (1991) Determination of superoxide dismutase activity by the polarographic method of catalytic currents in the cerebrospinal fluid of aging brain and neurologic degenerative diseases. Proc Soc Exp Biol Med 196:36–41
Barthwal MK, Srivastava N, Shukla R et al (1999) Polymorphonuclear leukocyte nitrite content and antioxidant enzymes in Parkinson’s disease patients. Acta Neurol Scand 100:300–304
Sudha K, Rao AV, Rao S et al (2003) Free radical toxicity and antioxidants in Parkinson’s disease. Neurol India 51:60–62
Bao B, Prasad AS, Beck FW et al (2008) Zinc supplementation decreases oxidative stress, incidence of infection, and generation of inflammatory cytokines in sickle cell disease patients. Transl Res 152:67–80
Prasad AS, Beck FW, Bao B et al (2007) Zinc supplementation decreases incidence of infections in the elderly: effect of zinc on generation of cytokines and oxidative stress. Am J Clin Nutr 85:837–844
Taysi S, Cikman O, Kaya A et al (2008) Increased oxidant stress and decreased antioxidant status in erythrocytes of rats fed with zinc-deficient diet. Biol Trace Elem Res 123:161–167
Messaoudi I, El Heni J, Hammouda F et al (2009) Protective effects of selenium, zinc, or their combination on cadmium-induced oxidative stress in rat kidney. Biol Trace Elem Res 130:152–161
Alexandrova A, Kebis A, Misl’anova C et al (2007) Copper impairs biliary epithelial cells and induces protein oxidation and oxidative DNA damage in the isolated perfused rat liver. Exp Toxicol Pathol 58:255–261
Kish SJ, Morito C, Hornykiewicz O (1985) Glutathione peroxidase activity in Parkinson’s disease brain. Neurosci Lett 58:343–346
Gil L, Siems W, Mazurek B et al (2006) Age-associated analysis of oxidative stress parameters in human plasma and erythrocytes. Free Radic Res 40:495–505
Mehmetcik G, Alptekin N, Toker G et al (1997) Mitochondrial lipid peroxides and antioxidant enzymes in the liver following phorone-induced glutathione depletion. Res Commun Mol Pathol Pharmacol 96:353–356
Rondanelli M, Melzi d’Eril GV, Anesi A, Ferrari E (1997) Altered oxidative stress in healthy old subjects. Aging (Milano) 9:221–223
Przedborski S, Donaldson DM, Murphy PL et al (1996) Blood superoxide dismutase, catalase and glutathione peroxidase activities in familial and sporadic amyotrophic lateral sclerosis. Neurodegeneration 5:57–64
Storch A, Jost WH, Vieregge P et al (2007) Randomized, double-blind, placebo-controlled trial on symptomatic effects of coenzyme Q(10) in Parkinson disease. Arch Neurol 64:938–944
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Baillet, A., Chanteperdrix, V., Trocmé, C. et al. The Role of Oxidative Stress in Amyotrophic Lateral Sclerosis and Parkinson’s Disease. Neurochem Res 35, 1530–1537 (2010). https://doi.org/10.1007/s11064-010-0212-5
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DOI: https://doi.org/10.1007/s11064-010-0212-5