Xanthine oxidase-derived reactive oxygen species contribute to the development of D-galactosamine-induced liver injury in rats

Free Radical Research

Volumn 41, Issue 2, 2007, Pages 135-144

  Ohta, Yoshiji ^a   Matsura, Tatsuya ^b   Kitagawa, Akira ^c   Tokunaga, Kenji ^d   Yamada, Kazuo ^b  

^a FUJITA HEALTH UNIVERSITY   (Japan)

^b TOTTORI UNIVERSITY   (Japan)

^c Chukyo Women's University   (Japan)

^d Kagawa Prefectural College of Health Sciences   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOPURINOL; ASCORBIC ACID; CATALASE; GALACTOSAMINE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; LIPID PEROXIDE; MYELOPEROXIDASE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; XANTHINE OXIDASE; ALANINE AMINOTRANSFERASE; ANTIOXIDANT; ASPARTATE AMINOTRANSFERASE; PEROXIDASE; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; PHOSPHOLIPID-HYDROPEROXIDE GLUTATHIONE PEROXIDASE; UNCLASSIFIED DRUG; URIC ACID; XANTHINE DEHYDROGENASE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DISEASE COURSE; DOSE RESPONSE; DRUG MECHANISM; ENZYME ACTIVITY; ENZYME ANALYSIS; LIVER INJURY; MALE; NONHUMAN; RAT; ANIMAL; BLOOD; DRUG ANTAGONISM; DRUG EFFECT; ENZYMOLOGY; LIPID PEROXIDATION; LIVER; METABOLISM; NEUTROPHIL; PHYSIOLOGY; TOXIC HEPATITIS; WISTAR RAT;

RATTUS;

ALANINE TRANSAMINASE; ALLOPURINOL; ANIMALS; ANTIOXIDANTS; ASCORBIC ACID; ASPARTATE AMINOTRANSFERASES; CATALASE; GALACTOSAMINE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HEPATITIS, TOXIC; LIPID PEROXIDATION; LIVER; MALE; NEUTROPHILS; PEROXIDASE; RATS; RATS, WISTAR; REACTIVE OXYGEN SPECIES; SUPEROXIDE DISMUTASE; URIC ACID; XANTHINE DEHYDROGENASE; XANTHINE OXIDASE;

EID: 34250859412     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.1080/10715760600953842     Document Type: Article

References (46)

1. Kaplowitz, N. and Tsukamoto, H. (1996) Oxidative stress and liver disease. Prog Liver Dis, 14, pp. 131-159.
2. Fridovich, I. (1970) Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase. J Biol Chem, 245, pp. 4053-4057.
3. Porras, A., Olson, JS and Palmer, G. (1981) The reaction of reduced xanthine oxidase with oxygen. Kinetics of peroxide and superoxide formation. J Biol Chem, 256, pp. 9096-9103.
4. Ramboer, C., Piessens, F. and de Groote, J. (1970) Serum xanthine oxidase and liver disease. Digestion, 7, pp. 183-195.
5. Battelli, MG, Musiani, S., Valgimigli, M., Gramantieri, L., Tomassoni, F., Bolondi, L. and Stirpe, F. (2001) Serum xanthine oxidase in human liver disease. Am J Gastroenterol, 96, pp. 1194-1199.
6. Stirpe, F., Ravaioli, M., Battelli, MG, Musiani, S. and Grazi, GL (2002) Xanthine oxidoreductase activity in human liver disease. Am J Gastroenterol, 97, pp. 2079-2085.
7. Ohta, Y., Kongo-Nishimura, M., Imai, Y. and Kishikawa, T. (2003) Contribution of xanthine oxidase-derived oxygen free radicals to the development of carbon tetrachloride-induced acute liver injury in rats. J Clin Biochem Nutr, 33, pp. 83-93.
8. Ali, S., Diwaker, G., Pawa, S., Siddiqui, MR, Adbin, MZ, Ahmad, FJ and Jain, SK (2001) Xanthine oxidase-derived reactive oxygen metabolites contribute to liver necrosis: Protection by 4-hydropyrazolo[3,4-]pyrimidine. Biochim Biophys Acta, 1536, pp. 21-30.
9. Pawa, S. and Ali, S. (2004) Liver necrosis and fluminant hepatic failure in rats: Protection by oxyanionic form of tungsten. Biochim Biophys Acta, 1688, pp. 210-222.
10. Takeyama, N., Shoji, Y., Ohashi, K. and Tanaka, T. (1996) Role of reactive oxygen intermediates in lipopolysaccharide-mediated hepatic injury in the rat. J Surg Res, 60, pp. 258-262.
11. Schimpl, G., Pesendorfer, P., Kuesz, A-M, Ratschek, M. and Hollwarth, ME (2000) The impact on hepatic xanthine oxidase and xanthine dehydrogenase activities on liver function in chronic cholestasis. Pediatr Surg Int, 16, pp. 297-301.
12. Gonzalez-Flecha, B., Cutrin, JC and Boveris, A. (1993) Time course and mechanism of oxidative stress and tissue damage in rat liver subjected to in vivo ischemia-reperfusion. J Clin Invest, 91, pp. 456-464.
13. Brass, CA, Narciso, J. and Gollan, JL (1991) Enhanced activity on the free radical producing enzyme xanthine oxidase in hypoxic rat liver. J Clin Invest, 87, pp. 424-431.
14. Keppler, D., Lesch, R., Retutter, W. and Decker, K. (1968) Experimental hepatitis induced by -galactosamine. Exp Mol Pathol, 9, pp. 279-290.
15. Medline, A., Schaffner, F. and Popper, H. (1970) Ultrastructural features in galactosamine-induced hepatitis. Exp Mol Pathol, 12, pp. 201-211.
16. Shiratori, Y., Kawase, T., Shiina, S., Okano, K., Sugimoto, T., Teraoka, H., Matano, S., Matsumoto, K. and Kamii, K. (1988) Modulation of hepatotoxicity by macrophages in the liver. Hepatology, 8, pp. 815-821.
17. Okuno, F., Yamada, M., Seishima, M., Moriwaki, H., Yoshida, H., Ando, T. and Muto, Y. (1989) Role of singlet oxygen in pathogenesis of liver injury in rats treated with -galactosamine. Jpn J Gastroenterol, 86, pp. 1266-1272.
18. Hu, H-L and Chen, R-D (1992) Changes in free radicals, trace elements, and neurophysiological function in rats with liver damage induced by -galactosamine. Biol Trace Elem Res, 34, pp. 19-21.
19. Se çkin, S., Koçak-Toker, N., Uysal, M. and Öz, B. (1993) The role of lipid peroxidation and calcium in galactosamine induced toxicity in the rat liver. Res Commun Chem Pathol Pharmacol, 80, pp. 117-120.
20. Hino, Y., Kumashiro, R., Tanaka, M., Shimada, M., Harada, M., Yoshitake, M., Sata, M., Sugiyama, M., Haramaki, N. and Tanikawa, K. (1994) Involvement of activated polymorphoneuclear leukocytes in galactosamine-induced hepatic injury in rats. J Clin Biochem Nutr, 16, pp. 27-36.
21. Sun, F., Hamagawa, E., Tsutsui, C., Sakaguchi, N., Kakura, Y., Tokumaru, S. and Kojo, S. (2003) Evaluation of oxidative stress during apoptosis and necrosis caused by -galactosamine in rat liver. Biochem Pharmacol, 65, pp. 101-107.
22. Ohta, Y., Kongo-Nishimura, M., Hayashi, T. and Kishikawa, T. (2004) Effect of Oren-gedoku-to (Huangliab-Jie-Du-Tang) extract on disruption of hepatic antioxidant defense systems in rats treated with -galatosamine. J Ethnopharmacol, 94, pp. 323-329.
23. Mourelle, M. and Meza, MA (1989) Colchicine prevents -galactosamine-induced hepatitis. J Hepatol, 8, pp. 165-172.
24. Wendel, A., Tiegs, G. and Werner, C. (1987) Evidence for the involvement of a reperfusion injury in galactosamine/endotoxin-induced hepatitis in mice. Biochem Pharmacol, 36, pp. 2637-2639.
25. Neihorster, M., Inoue, M. and Wendel, A. (1992) A link between extracellular reactive oxygen and endotoxin-induced release of tumor necrosis factor α in vivo. Biochem Pharmacol, 43, pp. 1151-1154.
26. Phan, SH, Ganonn, DE, Ward, PA and Karmiol, S. (1992) Mechanisms of neutrophil-induced xanthine dehydrogenase to xanthine oxidase conversion in endothelial cells: Evidence of a role in elastase. Am J Respir Cell Mol Biol, 6, pp. 270-278.
27. Varani, J. and Ward, PA (1994) Mechanisms of neutrophil-dependent and neutrophil-independent endothelial cell injury. Biol Signals, 3, pp. 1-14.
28. Sellak, H., Franzini, E., Hakim, J. and Pasquier, C. (1994) Reactive oxygen species rapidly increase endothelial ICAM-1 ability to bind neutrophils without detectable upregulation. Blood, 9, pp. 2669-2677.
29. Galkina, SI, Dormeneva, E., Bachschmid, M., Pushkareva, MA, Sud'ina, GF and Ullrich, V. (2004) Endothelium-leukocyte interactions under the influence of the superoxide-nitrogen system. Med Sci Monit, 10, pp. BR307-BR316.
30. Duval, DL, Howard, D., McCalden, TA and Billings, RE (1990) The determination of myeloperoxidase activity in liver. Life Sci, 47, pp. PL-145-PL-150.
31. Schierwagen, C., Bylund-Fellenous, A-C and Lundberg, C. (1990) Improved method for quantification of tissue PMN accumulation measured by myeloperoxidase. J Pharmacol Methods, 23, pp. 179-186.
32. Komatsu, H., Koo, A., Ghadishah, E., Zeng, H., Kuhlenkamp, JF, Inoue, M., Guth, PH and Kaplowitz, N. (1992) Neutrophil accumulation in ischemia reperfused rat liver: Evidence for a role for superoxide free radicals. Am J Physiol, 262, pp. G669-G676.
33. Klein, AS, Joh, JW, Rangan, U., Wang, D. and Bulkley, GB (1996) Allopurinol: Discrimination of antioxidant from enzyme inhibitory activities. Free Radic Biol Med, 21, pp. 713-717.
34. Majkic-Singh, N., Bogavac, L., Kalimanovska, V., Jelic, Z. and Spasic, S. (1987) Sperctrophotometric assay of xanthine oxidase with 2,2'-azino-di(3-ethylbenzthiazoline-6-sulfonate; ABTS) as chromogen. Clin Chim Acta, 162, pp. 29-36.
35. Hashimato, S. (1974) A new spectrophotometric assay method of xanthine oxidase in crude tissue homogenate. Anal Biochem, 62, pp. 426-433.
36. Oyanagui, Y. (1984) Reevaluation of assay methods and establishment of kit for superoxide dismutase. Anal Biochem, 142, pp. 290-296.
37. Bergmeyer, HU (1955) Measurement of catalase activity. Biochem Z, 327, pp. 255-258.
38. Hochstein, P. and Utley, H. (1968) Hydrogen peroxide detoxication by glutathione peroxidase and catalase in rat liver homogenates. Mol Pharmacol, 34, pp. 574-579.
39. Suzuki, K., Ota, H., Sasagawa, S., Sakatani, T. and Fujiura, T. (1983) Assay method for myeloperoxidase in human polymorphonuclear leukocytes. Anal Biochem, 132, pp. 345-353.
40. Ohkawa, H., Ohishi, N. and Yagi, K. (1979) Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem, 95, pp. 351-358.
41. Sedlak, J. and Lindsay, RH (1968) Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Elaman's reagent. Anal Biochem, 25, pp. 192-205.
42. Zannoi, V., Lynch, M., Goldstein, S. and Sato, P. (1974) A rapid micormethod for the determination of ascorbic acid in plasma and tissues. Biochem Med, 11, pp. 41-48.
43. Lowry, OH, Rosebrough, NH, Farr, AD and Randall, RJ (1951) Protein measurement with the Folin-phenol reagent. J Biol Chem, 193, pp. 265-275.
44. Das, DK, Engelman, RM, Clement, R., Otani, H., Prasad, R. and Rao, P. (1987) Role of xanthine oxidase inhibitors as free radical scavengers: A novel mechanism of active allopurinol and oxypurinol in myocardial salvage. Biochem Biophys Res Commun, 148, pp. 314-319.
45. Moorhouse, PC, Grootveld, M., Halliwell, B., Quinlan, JG and Gutteridge, JM (1987) Allopurinol and oxypurinol are hydroxyl radical scavengers. FEBS Lett, 213, pp. 23-28.
46. MacDonald, JR, Beckstead, JH and Smuckler, EA (1987) An ultrastructural and histochemcial study on the prominent inflammatory response in (+)-galactosamine hepatotoxicity. Br J Exp Pathol, 68, pp. 189-199.