30
Views
10
CrossRef citations to date
0
Altmetric
Original Article

Effect of peroxisome proliferator on extracellular glutathione peroxidase in rat

, , , , , & show all
Pages 181-190 | Received 10 Feb 1999, Published online: 07 Jul 2009

References

  • Avissar N., Kerl E.A., Baker S.S., Cohen H.J. Extracellular glutathione peroxidase mRNA and protein in human cell lines. Archives of Biochemistry and Biophysics 1994; 309: 239–246
  • Maser R.L., Magenheimer B.S., Calvet J.P. Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion. Journal of Biological Chemistry 1994; 269: 27066–27073
  • Yoshimura S., Watanabe K., Suemizu H., Onozawa T., Mizoguchi J., Tsuda K., Hatta H., Moriuchi T. Tissue specific expression of the plasma glutathione peroxidase gene in rat kidney. Journal of Biochemistry 1991; 109: 918–923
  • Nakane T., Asayama K., Kodera K., Hayashibe H., Uchida U., Nakazawa S. Effect of selenium deficiency on cellular and extracellular glutathione peroxidase: immunochemical detection and mRNA analysis in rat kidney and serum. Free Radical Biology and Medicine 1998; 25: 504–511
  • Takahashi K., Avissar N., Whitin J., Cohen H. Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzymes. Archives of Biochemistry and Biophysics 1987; 256: 677–689
  • Ren B., Huang W., Akesson B., Ladenstein R. The crystal structure of seleno-glutathine peroxidase from human plasma at 2.9 A resolution. Journal of Molecular Biology 1997; 268: 869–885
  • Singh I. Biochemistry of peroxisomes in health and disease. Molecular and Cellular Biochemistry 1997; 167: 1–29
  • de Duve C. The peroxisome in retrospect. Annals of the New York Academy of Sciences 1996; 804: 1–10
  • Rao M.S., Reddy J.K. Hepatocarcinogenesis of peroxisome proliferators. Annals of the New York Academy of Sciences 1996; 804: 573–587
  • Bentley P., Calder I., Elcombe C., Grasso P., Stringer D., Wiegand H.J. Hepatic peroxisome proliferation in rodents and its significance for humans. Food Chemical and Toxicology 1993; 31: 857–907
  • Reddy P.G., Nemali M.R., Reddy M.K., Reddy M.N., Yuan P.M., Yuan S., Laffler T.G., Shiroza T., Kuramitsu H.K., Usuda N. Isolation and sequence determination of a cDNA clone for rat peroxisomal urate oxidase: liver-specific expression in the rat. Proceedings of the National Academy of Sciences of the United States of America 1988; 85: 9081–9085
  • Swierezynski J., Bannasch P., Mayer D. Increase of lipid peroxidation in rat liver microsomes by dehydroepiandrosterone feeding. Biochimica et Biophysica Acta 1996; 1315: 193–198
  • Takagi A., Sai K., Umemura T., Hasegawa R., Kurokawa Y. Relationship between hepatic peroxisome proliferation and 8-hydroxydeoxyguanosine formation in liver DNA of rats following long-term exposure to three peroxisome proliferators; di (2-ethylhexyl) phthalate, aluminium clofibrate and simfibrate. Cancer Letters 1990; 53: 33–38
  • Harris C.A., Henttu P., Parker M.G., Sumpter J.P. The estrogenic activity of phthalate esters in vivo. Environmental Health Perspectives 1997; 105: 802–811
  • Davis B.J., Maronpot R.R., Heindel J.J. Di-(2-ethylhexyl) phthalate suppresses estradiol and ovulation in cycling rats. Toxicology and Applied Pharmacology 1994; 128: 216–233
  • Thomas J.A., Thomas M.J. Biological effects of di-(2-ethylhexyl) phthalate and other phthalic acid esters. Critical Reviews in Toxicology 1984; 13: 283–317
  • Corton J.C., Bocos C., Moreno E.S., Merritt A., Cattley R.C., Gustafsson J.A. Peroxisome proliferators alter the expression of estrogen-metabolizing enzymes. Biochimie 1997; 79: 151–162
  • Baudhuin P., Beaufay Y., Rahman Li, Sellinger O.Z., Wattiaux R., Jacques P., de Duve C. Tissue fractionation studies. Biochemical Journal 1964; 92: 179–184
  • Dobashi K., Pahan K., Chahal A., Singh I. Modulation of endogenous antioxidant enzymes by nitric oxide in rat C6 glial cells. Journal of Neurochemistry 1997; 68: 1896–1903
  • Levander O.A., Deloach D.P., Morris V.C., Moser P.B. Platelet glutathione peroxidase activity as an index of selenium status in rats. Journal of Nutrition 1983; 113: 55–63
  • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Chemistry 1976; 72: 248–254
  • Asayama K., Yokata S., Dobashi K., Hayashibe H., Kawaoi A., Nakazawa S. Purification and immunoelectron microscopic localization of cellular glutathione peroxidase in rat hepatocytes: quantitative analysis by postembedding method. Histochemistry 1994; 102: 213–219
  • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
  • Furuta S., Hayashi H., Hijikata M., Miyazawa S., Osumi T., Hashimoto T. Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase. Proceedings of the National Academy of Sciences of the United States of America 1986; 83: 313–317
  • Toyokuni S., Miyake N., Hiai H., Hagiwara M., Kawakishi S., Osawa T., Uchida K. The monoclonal antibody specific for the 4-hydroxy-2-nonenal histidine adduct. F.E.B.S. Letters 1995; 359: 189–191
  • Toyokuni S., Luo X.P., Tanaka T., Uchida K., Hiai H., Lehotay D.C. Induction of a wide range of C2–12 aldehydes and C2–12 acyloins in the kidney of wister rats after treatment with a renal carcinogen, ferric nitrilotriacetate. Free Radical Biology and Medicine 1997; 22: 1019–1027
  • Dobashi K., Asayama K., Hayashibe H., Uchida N., Kobayashi M., Kawaoi A., Kato K. Effect of diabetes mellitus induced by streptozotocin on renal superoxide dismutases in the rat. A radioimmunoassay and immunohistochemical study. Virchows Archiv B 1991; 60: 67–72
  • Garberg P., Thullberg M. Decreased glutathione peroxidase activity in mice in response to nafenopin is caused by changes in selenium metabolism. Chemico Biological Interactions 1996; 99: 165–177
  • Gonzalez F.J. Recent update on the PPAR alpha-null mouse. Biochimie 1997; 79: 139–144
  • Reubsaet F.A., Veerkamp J.H., Bruckwilder M.L., Trijbels J.M., Monnens L.A. Peroxisomal oxidases and catalase in liver and kidney homogenates of normal and di(ethylhexyl)phthalate-fed rats. International Journal of Biochemistry 1991; 23: 961–967
  • Oberley T.D., Oberley L.W., Slattery A.F., Elwell J.H. Immunohistochemical localization of glutathione-S-transferase and glutathione peroxidase in adult Syrian hamster tissues and during kidney development. American Journal of Pathology 1991; 139: 355–369
  • Dobashi K., Asayama K., Hayashibe H., Munim A., Uchida N., Kawaoi A., Nakazawa S. Immunohistochemical localization of cellular glutathione peroxidase in adult rat tissues by use of newly prepared polyclonal antibodies. Yamanashi Medical Journal 1994; 9: 69–79
  • Asayama K., Dobashi K., Kawada Y., Nakane T., Kawaoi A., Nakazawa S. Immunohistochemical localization and quantitative analysis of cellular glutathione peroxidase in fetal and neonatal rat tissues: fluorescence microscopy image analysis. Histochemical Journal 1996; 28: 63–71
  • Nemali N.R., Usuda N., Reddy M.K., Oyasu K., Hashimoto T., Osumi T., Rao M.S., Reddy J.K. Comparison of constitutive and inducible levels of expression of peroxisomal β-oxidation and catalase gene in liver and extrahepatic tissues of rat. Cancer Research 1988; 48: 5316–5324
  • Mackerer C.R., Haettinger J.R. Renal gluconeogenesis in clofibrate-treated rats. Journal of Pharmacology and Experimantal Therapeutics 1978; 204: 683–689
  • Fukuda A., Osawa T., Hitomi K., Uchida K. 4-hydroxy-2-nonenal cytotoxicity in renal proximal tubular cells: protein modification and redox alteration. Archives of Biochemistry and Biophysics 1996; 333: 419–426
  • Bartsch H., Nair J., Velic I. Etheno-DNA base adducts as tools in human cancer aetiology and chemoprevention. European Journal of Cancer Prevention 1997; 6: 529–534
  • Mashima R., Yamamoto Y., Yoshimura S. Reduction of phosphatidylcholine hydroperoxide by apolipoprotein A-I: purification of the hydroperoxide-reducing proteins from human blood plasma. Journal of Lipid Research 1998; 39: 1133–1140
  • Esworthy R.S., Chu F.F., Geiger P., Girotti A.W., Doroshow J.H. Reactivity of plasma glutathione peroxidase with hydroperoxide substrates and glutathione. Archives of Biochemistry and Biophysics 1993; 307: 29–34
  • Crocker J.F., Safe S.H., Acott P. Effects of chronic phthalate exposure on the kidney. Journal of Toxicology and Environmental Health 1988; 23: 433–444
  • Woodward K.N. Phthalate esters, cystic kidney disease in animals and possible effects on human health: a review. Human and Experimental Toxicology 1990; 9: 397–401
  • Cumming A. Acute renal failure and interstitial nephritis after clofibrate treatment. British Medical Journal 1980; 281: 1529–1530

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.