Bioavailability and catalytic properties of copper and iron for Fenton chemistry in human cerebrospinal fluid

Redox Report

Volumn 15, Issue 1, 2010, Pages 29-35

  Spasojević, Ivan ^a   Mojović, Miloš ^b   Stević, Zorica ^c   Spasić, Snežana D ^b   Jones, David R ^d   Morina, Arian ^b   Spasić, Mihajlo B ^b  

^a UNIVERSITY OF BELGRADE   (Serbia)

^b UNIVERSITY OF BELGRADE   (Serbia)

^c CLINICAL CENTER OF SERBIA   (Serbia)

^d UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Cerebrospinal fluid; Copper; Diethyldithiocarbamate; Fenton reaction; Iron

Indexed keywords

COPPER CHLORIDE; EDETIC ACID; FERROUS CHLORIDE; HYDROGEN PEROXIDE; HYDROXYL RADICAL; ZALCITABINE;

ADULT; ANTIOXIDANT ACTIVITY; ARTICLE; BIOAVAILABILITY; CATALYSIS; CEREBROSPINAL FLUID; CLINICAL ARTICLE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; FEMALE; FENTON REACTION; HOMEOSTASIS; HUMAN; INHIBITION KINETICS; IRON CHELATION; MALE; NERVE DEGENERATION; OXIDATION; OXIDATION REDUCTION REACTION; PATHOPHYSIOLOGY; PRIORITY JOURNAL;

ADULT; BIOLOGICAL AVAILABILITY; CATALYSIS; CHELATING AGENTS; COPPER; CYCLIC N-OXIDES; DITIOCARB; EDETIC ACID; ELECTRON SPIN RESONANCE SPECTROSCOPY; FEMALE; FREE RADICALS; HUMANS; HYDROGEN PEROXIDE; HYDROXIDES; IRON; MALE; MIDDLE AGED;

EID: 77949463742     PISSN: 13510002     EISSN: 17432928     Source Type: Journal    
DOI: 10.1179/174329210X12650506623087     Document Type: Article

References (38)

1. Smith MA, Harris PLR, Sayre LM, Perry G. Iron accumulation in Alzheimer disease is a source of redox generated free radicals. Proc Natl Acad Sci USA 1997; 94: 9866-9868.
2. Koppenol WH. Fenton chemistry and iron chelation under physiologically relevant conditions: electrochemistry and kinetics. Chem Res Toxicol 2006; 19: 1263-1269.
3. Cui K, Luo X, Xu K, Murthy MRV. Role of oxidative stress in neurodegeneration: recent developments in assay methods for oxidative stress and nutraceutical antioxidants. Prog Neuropsychopharmacol Biol Psychiatry 2004; 28: 771-799.
4. Boll MC, Alcaraz-Zubeldia M, Montes S, Rios C. Free copper, ferroxidase and SOD1 activities, lipid peroxidation and NOx content in the CSF. A different marker profile in four neurodegenerative diseases. Neurochem Res 2008; 33: 1717-1723.
5. Liu D, Wen J, Liu J, Li L. The roles of free radicals in amyotrophic lateral sclerosis: reactive oxygen species and elevated oxidation of protein, DNA, and membrane phospholipids. FASEB J 1999; 13: 2318-2328.
6. Huang X, Atwood CS, Hartshorn MA et al. The AΒ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 1999; 38: 7609-7616.
7. Takahashi S, Takahashi I, Sato H, Kubota Y, Yoshida S, Muramatsu Y. Age-related changes in the concentrations of major and trace elements in the brain of rats and mice. Biol Trace Elem Res 2001; 80: 145-158.
8. Valko M, Morris H, Cronin MTD. Metals, toxicity and oxidative stress. Curr Med Chem 2005; 12: 1161-1208.
9. Barnham KJ, Masters CL, Bush AI. Neurodegenerative diseases and oxidative stress. Nat Rev 2004; 3: 205-214.
10. Cookson MR, Shaw PJ. Oxidative stress and motor neurone disease. Brain Pathol 1999; 9: 165-186.
11. Glenner GG, Wong CW. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984; 120: 885-890.
12. Nakamura M, Shishido N, Nunomura A et al. Three histidine residues of amyloid-Β peptide control the redox activity of copper and iron. Biochemistry 2007; 46: 12737-12743.
13. Shapira AHV, Mann VM, Cooper JM, Krige D, Jenner PJ, Marsden CD. Mitochondrial function in Parkinson's disease. Ann Neurol 1992; 32: S116-S124.
14. Hirsch E, Graybiel AM, Agid YA. Melanized dopaminergic neurons are differentially susceptible to degeneration in Parkinson's disease. Nature 1988; 334: 345-348.
15. Wakamatsu K, Fujikawa K, Zucca FA, Zecca L, Ito S. The structure of neuromelanin as studied by chemical degradative methods. J Neurochem 2003; 86: 1015-1023.
16. Gerard C, Chehhal H, Hugel RP. Complexes of iron(III) with ligands of biological interest: dopamine and 8-hydroxyquinoline-5- sulfonic acid. Polyhedron 1994; 13: 591-597.
17. 2. J Biol Chem 2002; 277: 40302-40308.
18. Oba H, Araki T, Ohtomo K et al. Amyotrophic lateral sclerosis: T2 shortening in motor cortex at MR imaging. Radiology 1993; 189: 843-846.
19. Ihara Y, Nobukuni K, Takata H, Hayabara T. Oxidative stress and metal content in blood and cerebrospinal fluid of amyotrophic lateral sclerosis patients with and without a Cu,Zn-superoxide dismutase mutation. Neurol Res 2005; 27: 105-108.
20. Sedlak DL, Hoigne J. The role of copper and oxalate in the redox cycling of iron in atmospheric waters. Atmos Environ 1993; 27: 2173-2185.
21. Buettner GR, Jurkiewicz BA. Catalytic metals, ascorbate and free radicals: combinations to avoid. Radic Res 1996; 145: 532-541.
22. Bacic G, Spasojevic I, Secerov B, Mojovic M. Spin-trapping of oxygen free radicals in chemical and biological systems: new traps, radicals and possibilities. Spectrochim Acta A 2008; 69: 1354-1366.
23. Teixeira MC, Telo JP, Duarte NF, Sá-Correiaa I. The herbicide 2,4- dichlorophenoxyacetic acid induces the generation of free-radicals and associated oxidative stress responses in yeast. Biochem Biophys Res Commun 2004; 324: 1101-1107.
24. Lentner C. Geigy Scientific Tables, vol 1, 8th edn. Basel: Ciba-Geigy, 1981.
25. Barb WG, Baxendale JH, George P, Hargrave KR. Reactions of ferrous and ferric ions with hydrogen peroxide. Part 1. - The ferrous ion reaction. Trans Farad Soc 1951; 47: 462-500.
26. Gutteridge JMC, Wilkins S. Copper salt-dependent hydroxyl radical formation damage to proteins acting as antioxidants. Biochim Biophys Acta 1983; 759: 38-41.
27. Yamamoto K, Kawanishi S. Hydroxyl free radical is not the main active species in site-specific DNA damage induced by copper (II) ion and hydrogen peroxide. J Biol Chem 1989; 264: 15435-15440.
28. Rae TD, Schmidt PJ, Pufahl RA, Culotta VC, O'Halloran TV. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 1999; 284: 805-808.
29. Graf E, Mahoney JR, Bryant RG, Eaton JW. Iron-catalyzed hydroxyl radical formation: stringent requirement for free iron coordination site. J Biol Chem 1984; 259: 3620-3624.
30. Michelson AM, Maral J. Carbonate anions; effects on the oxidation of luminal, oxidative hemolysis, γ-irradiation and the reaction of activated oxygen species with enzymes containing various active centres. Biochimie 1983; 65: 95-104.
31. Engelmann MD, Bobier RT, Hiatt T, Cheng IF. Variability of the Fenton reaction characteristics of the EDTA, DTPA, and citrate complexes of iron. Biometals 2003; 16: 519-527.
32. Fong KL, McCay PB, Poyer JL. Evidence for superoxide dependent reduction of Fe3+ and its role in enzyme generated hydroxyl radical formation. Chem Biol Interact 1976; 15: 77-89.
33. Nikolic-Kokic A, Stevic Z, Stojanovic S et al. Biotransformation of nitric oxide in the cerebrospinal fluid of amyotrophic lateral sclerosis patients. Redox Rep 2005; 10: 265-270.
34. Taqui Khan MM, Martel1 AE. Metal ion and metal chelate catalyzed oxidation of ascorbic acid by molecular oxygen. I Cupric and ferric ion catalyzed oxidation. J Am Chem Soc 1967; 89: 4176-4185.
35. Ghosh SK, Gould ES. Electron transfer. 98. Copper(II) and vanadium(IV) catalysis of the reduction of peroxide-bound chromium(IV) with ascorbic acid. Inorg Chem 1989; 28: 1948-1951.
36. Merkofer M, Kissner R, Hider R, Brunk UT, Koppenol WH. Fenton chemistry and iron chelation under physiologically relevant conditions: electrochemistry and kinetics. Chem Res Toxicol 2006; 19: 1263-1269.
37. Orescanin-Dusic Z, Milovanovic S, Nikolic-Kokic A, Radojcic R, Spasojevic I, Spasic M. Diethyldithiocarbamate potentiates the effects of protamine sulphate in the isolated rat uterus. Redox Rep 2009; 14: 48-54.
38. Van Faassen E, Vanin AF. (eds) Radicals for life. The various forms of nitric oxide, 1st edn. Amsterdam: Elsevier, 2007.