Effect of heparin on viologen-stimulated enzymatic NADH depletion

Chemical Research in Toxicology

Volumn 19, Issue 5, 2006, Pages 668-673

  Zielonka, Jacek ^a   Rybak, Małgorzata ^a   Celińska, Joanna ^a   Adamus, Jan ^a   Marcinek, Andrzej ^a   Gebicki, Jerzy ^a  

^a LODZ UNIVERSITY OF TECHNOLOGY   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

DIQUAT; HEPARIN; OXYGEN RADICAL; PARAQUAT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SUPEROXIDE; VIOLOGEN; XANTHINE OXIDASE;

ANTIOXIDANT ACTIVITY; ARTICLE; CHEMICAL BINDING; DRUG MECHANISM; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PULSE RADIOLYSIS;

CYTOCHROME C GROUP; DIQUAT; HEPARIN; NADP; OXIDATION-REDUCTION; PARAQUAT; SUPEROXIDES; XANTHINE OXIDASE;

EID: 33744454394     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx050336s     Document Type: Article

References (50)

1. Summers, L. A. (1980) The Bipyridinium Herbicides, Academic Press, London, New York.
2. Lee, S. K., Ameno, K., In, S. W., Yang, J. Y., Kim, K. U., Koo, K. S., Yoo, Y. C., Ameno, S., and Ijiri, I. (1999) Levels of paraquat in fatal intoxications. Int. J. Legal Med. 112, 198-200.
3. Fuke, C., Ameno, K., Ameno, S., Kinoshita, H., and Ijiri, I. (1996) Detection of two metabolites of diquat in urine and serum of poisoned patients after ingestion of a combined herbicide of paraquat and diquat. Arch. Toxicol. 70, 504-507.
4. Tomita, M. (1991) Comparison of one-electron reduction activity against the bipirydyl herbicides, paraquat and diquat, in microsomal and mitochondrial fractions of liver, lung and kidney (in vitro). Biochem. Pharmacol. 42, 303-309.
5. Litchfield, M. H., Daniel, J., and Longshaw, S. (1973) The tissue distribution of the bipyridylium herbicides diquat and paraquat in rats and mice. Toxicology 1, 155-165.
6. Jones, G. M., and Vale, J. A. (2000) Mechanism of toxicity, clinical features, and managment of diquat poisoning: A review. Clin. Toxicol. 38, 123-128.
7. Bus, J. S., and Gibson, J. E. (1984) Paraquat: Model for oxidant-initiated toxicity. Environ. Health Perspect. 55, 37-46.
8. Tampo, Y., Tsukamoto, M., and Yonaha, M. (1999) Superoxide production from paraquat evoked by exogenous NADPH in pulmonary endothelial cells. Free Radical Biol. Med. 27, 588-595.
9. Kelner, M. J., Bagnell, R., Hale, B., and Alexander, N. M. (1988) Methylene blue competes with paraquat for reduction by flavoenzymes resulting in decreased superoxide production in the presence of heme proteins. Arch. Biochem. Biophys. 262, 422-426.
10. +)-analogues on the respiratory chain of bovine heart mitochondria. Arch. Biochem. Biophys. 337, 69-74.
11. Vasquez-Vivar, J., Hogg, N., Pritchard, K. A., Jr., Martasek, P., and Kalyanaraman, B. (1997) Superoxide anion formation from lucigenin: An electron spin resonance spin-trapping study. FEBS Lett. 403, 127-130.
12. Fukushima, T., Yamada, K., Isobe, A., Shiwaku, K., and Yamane, Y. (1993) Mechanism of cytotoxicity of paraquat. I. NADH oxidation and paraquat radical formation via complex I. Exp. Toxicol. Pathol. 45, 345-349.
13. Kitazawa, Y., Matsubara, M., Takeyama, N., and Tanaka, T. (1991) The role of xanthine oxidase in paraquat intoxication. Arch. Biochem. Biophys. 288, 220-224.
14. Halliwell, B., and Gutteridge, J. M. C. (2000) Free Radicals in Biology and Medicine, Oxford University Press, Oxford.
15. Sakai, M., Yamagami, K., Kitazawa, Y., Takeyama, N., and Tanaka, T. (1995) Xanthine oxidase mediates paraquat-induced toxicity on cultured endothelial cells. Pharmacol. Toxicol. 77, 36-40.
16. 2. FEBS Lett. 128, 339-342.
17. Tsukamoto, M., Tampo, Y., Sawada, M., and Yonaha, M. (2000) Paraquat-induced membrane dysfunction in pulmonary microvascular endothelial cells. Pharmacol. Toxicol. 86, 102-109.
18. Day, B. J., and Crapo, J. D. (1996) A metalloporphyrin superoxide dismutase mimetic protects against paraquat-induced lung injury in vivo. Toxicol. Appl. Pharmacol. 140, 94-100.
19. Day, B. J., Shawen, S., Liochev, S. I., and Crapo, J. D. (1995) A metalloporphyrin superoxide dismutase mimetic protects against paraquat-induced endothelial cell injury, in vitro. J. Pharmacol. Exp. Ther. 275, 1227-1232.
20. Suntres, Z. E. (2002) Role of antioxidants in paraquat toxicity. Toxicology 180, 65-72.
21. Tsuchiya, T., Yoshida, T., Imaeda, A., Sakushima, M., and Kiho, T. (1993) The effect of carbohydrate sulfate salts on the absorption and excretion of paraquat in rats. Biol. Pharm. Bull. 16, 1111-1113.
22. Tsuchiya, T., Yoshida, T., Imaeda, A., Kiho, T., and Ukai, S. (1995) Detoxification of paraquat poisoning: Effects of alkyl sulfates and alkylsulfonates on paraquat poisoning in mice and rats. Biol. Pharm. Bull. 18, 523-528.
23. Tsuchiya, T., Imaeda, A., Kiho, T., and Ukai, S. (1995) Detoxification of paraquat poisoning: Effects of carbohydrate sulfate, alkyl sulfate and alkylsulfonate on active oxygen. Biol. Pharm. Bull. 18, 1700-1704.
24. Hiebert, L., and Ping, T. (1997) Protective effect of dextran sulfate and heparin on adult rat cardiomyocytes damaged by free radicals. J. Mol. Cell. Cardiol. 29, 229-235.
25. Ram, I. J., and Hiebert, M. L. (2003) Dextran sulfate protects porcine but not bovine cultured endothelial cells from free radical injury. Can. J. Vet. Res. 67, 81-87.
26. Mattai, J., and Kwak, J. C. T. (1981) Mg and Ca binding to heparin in the presence of added univalent salt. Biochim. Biophys. Acta 677, 303-312.
27. Rabenstein, D. L., Robert, J. M., and Peng, J. (1995) Multinuclear magnetic resonance studies of the interaction of inorganic cations with heparin. Carbohydr. Res. 278, 239-256.
28. Horecker, B. L., and Kornberg, A. (1948) The extinction coefficients of the reduced band of pyridine nucleotides. J. Biol. Chem. 175, 385-390.
29. Massey, V. (1959) The microestimation of succinate and the extinction coefficient of cytochrome c. Biochim. Biophys. Acta 34, 255-256.
30. Karolczak, S., Hodyr, K., and Połowiński, M. (1992) Pulse radiolysis system based on ELU-6E linac II. Development and upgrading the system. Radiat. Phys. Chem. 39, 1-5.
31. Zielonka, J., Gebicki, J., and Grynkiewicz, G. (2003) Radical scavenging properties of genistein. Free Radical Biol. Med. 35, 958-965.
32. -) in aqueous solution. J. Phys. Chem. Ref. Data 17, 513-882.
33. Harrison, R. (2000) Xanthine oxidoreductase. In Free Radicals and Inflammation (Winyard, P. G., Blake, D. R., and Evans, C. H., Eds.) pp 65-81, Birkhäuser, Basel.
34. Bray, R. C. (1975) Molybdenum iron-sulfur flavin hydroxylases and related enzymes. In The Enzymes (Boyer, P. D., Ed.) pp 299-419, Academic Press, New York.
35. Sander, S. A., Eisenthal, R., and Harrison, R. (1997) NADH oxidase activity of human xanthine oxidoreductase. Generation of superoxide anion. Eur. J. Biochem. 245, 541-548.
36. Wieczorkowska, M., Zielonka, J., Celińska, J., Adamus, J., Ciesielska, E., Marcinek, A., Szmigiero, L., Gebicki, J. (2003) 1-Methyl-3-nitropyridine: an efficient oxidant of NADH in nonenzymatic and enzyme-mediated processes. Free Radical Res. 37, 1157-1162.
37. Farrington, J. A., Ebert, M., Land, E. J., and Fletcher, K. (1973) Bipyridylium quaternary salts and related compounds. V. Pulse radiolysis studies of the reaction of paraquat radical with oxygen. Implications for the mode of action of bipyridyl herbicides. Biochim. Biophys. Acta 314, 372-381.
38. Farrington, J. A., Ebert, M., and Land, E. J (1978) Bipyridylium quaternary salts and related compounds. Part 6. Pulse-radiolysis studies of reaction of paraquat radical analogues with oxygen. J. Chem. Soc., Faraday Trans. 174, 665-675.
39. Watanabe, T., and Honda, K. (1982) Measurement of the extinction coefficient of the methyl viologen cation radical and the efficiency of its formation by semiconductor photocatalysis. J. Phys. Chem. 86, 2617-2619.
40. Ross, A. B., Bielski, B. H. J., Buxton, G. V., Greenstock, C. L., Helman, W. P., Huie, R. E., Grodkowski, J., Neta, P., and Mallard, W. G. (1994) NDRL-NIST Solution Kinetics Database, version 3, National Institute of Standards and Technology, Gaithersburg, Maryland.
41. Butler, J., Koppenol, W. H., and Maergoliash, E. (1993) Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion. J. Biol. Chem. 257, 10747-10750.
42. Balazs, E. A., Davies, J. V., Phillips, G. O., and Scheufele, D. S. (1968) A study of polyanion-cation interactions using hydrated electrons. Biochem. Biophys. Res. Commun. 30, 386-392.
43. Balazs, E. A., Davies, J. V., Phillips, G. O., and Scheufele, D. S. (1968) Polyanions and their complexes. Part IV. A pulse radiolysis study of the interaction between methylene blue and heparin in aqueous solution. J. Chem. Soc. C, 1424-1429.
44. Moore, J. S., Phillips, G. O., Power, D. M., and Davies, J. (1970) Polyanions and their complexes. Part VII. Mechanism of methylene blue-polyanion interactions. J. Chem. Soc. A, 1155-1159.
45. Jonah, C. D., Matheson, M. S., and Meisel, D. (1977) Polyelectrolyte effects on rates of hydrated electrons. J. Phys. Chem. 81, 1805-1810.
46. Manning, G. S. (1979) Counterion binding in polyelectrolyte theory. Acc. Chem. Res. 12, 443-449.
47. Rabenstein, D. L. (2002) Heparin and heparan sulfate: Structure and function. Nat. Prod. Rep. 19, 312-331.
48. Hsu, K. S., and Lin-Shiau, S. Y. (1995) Antagonism by paraquat of the relaxing effects of acetylcholine and A23187 in rat thoracic aorta. Eur. J. Pharmacol. 292, 315-320.
49. Radi, R., Rubbo, H., Bush, K., and Freeman, B. A. (1997) Xanthine oxidase binding to glycosaminoglycans: Kinetics and superoxide dismutase interactions of immobilized xanthine oxidase-heparin complexes. Arch. Biochem. Biophys. 339, 125-135.
50. Houston, M., Estevez, A., Chumley, P., Aslan, M., Marklund, S., Parks, A. D., and Freeman A. B. (1999) Binding of xanthine oxidase to vascular endothelium. J. Biol. Chem. 274, 4985-4994.