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Volumn 31, Issue 3, 1999, Pages 181-190

Effect of peroxisome proliferator on extracellular glutathione peroxidase in rat

Author keywords

Clofibrate; Diethylhexyl phthalate; Glutathione peroxidase; Lipid peroxide; Microbodies; Rat kidney

Indexed keywords

4 HYDROXYNONENAL; CATALASE; CLOFIBRATE; GLUTATHIONE PEROXIDASE; LIPID PEROXIDE; MESSENGER RNA; PEROXISOME PROLIFERATOR; PHTHALIC ACID BIS(2 ETHYLHEXYL) ESTER; TERT BUTYL HYDROPEROXIDE;

EID: 0032882116     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/10715769900300731     Document Type: Article
Times cited : (12)

References (42)
  • 2
    • 0027993038 scopus 로고
    • Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion
    • R.L. Maser, B.S. Magenheimer and J.P. Calvet (1994) Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion. Journal of Biological Chemistry, 269, 27066-27073.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 27066-27073
    • Maser, R.L.1    Magenheimer, B.S.2    Calvet, J.P.3
  • 4
    • 0032171220 scopus 로고    scopus 로고
    • Effect of selenium deficiency on cellular and extracellular glutathione peroxidase: Immunochemical detection and mRNA analysis in rat kidney and serum
    • T. Nakane, K. Asayama, K. Kodera, H. Hayashibe, U. Uchida and S. Nakazawa (1998) 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, 25, 504-511.
    • (1998) Free Radical Biology and Medicine , vol.25 , pp. 504-511
    • Nakane, T.1    Asayama, K.2    Kodera, K.3    Hayashibe, H.4    Uchida, U.5    Nakazawa, S.6
  • 5
    • 0023186348 scopus 로고
    • Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzymes
    • K. Takahashi, N. Avissar, J. Whitin and H. Cohen (1987) Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzymes. Archives of Biochemistry and Biophysics, 256, 677-689.
    • (1987) Archives of Biochemistry and Biophysics , vol.256 , pp. 677-689
    • Takahashi, K.1    Avissar, N.2    Whitin, J.3    Cohen, H.4
  • 6
    • 0031584269 scopus 로고    scopus 로고
    • The crystal structure of seleno-glutathine peroxidase from human plasma at 2.9 å resolution
    • B. Ren, W. Huang, B. Akesson and R. Ladenstein (1997) The crystal structure of seleno-glutathine peroxidase from human plasma at 2.9 Å resolution. Journal of Molecular Biology, 268, 869-885.
    • (1997) Journal of Molecular Biology , vol.268 , pp. 869-885
    • Ren, B.1    Huang, W.2    Akesson, B.3    Ladenstein, R.4
  • 7
    • 0031055817 scopus 로고    scopus 로고
    • Biochemistry of peroxisomes in health and disease
    • I. Singh (1997) Biochemistry of peroxisomes in health and disease. Molecular and Cellular Biochemistry, 167, 1-29.
    • (1997) Molecular and Cellular Biochemistry , vol.167 , pp. 1-29
    • Singh, I.1
  • 12
    • 0029873233 scopus 로고    scopus 로고
    • Increase of lipid peroxidation in rat liver microsomes by dehydroepiandrosterone feeding
    • J. Swierezynski, P. Bannasch and D. Mayer (1996) Increase of lipid peroxidation in rat liver microsomes by dehydroepiandrosterone feeding. Biochimica et Biophysica Acta, 1315, 193-198.
    • (1996) Biochimica et Biophysica Acta , vol.1315 , pp. 193-198
    • Swierezynski, J.1    Bannasch, P.2    Mayer, D.3
  • 13
    • 0025004340 scopus 로고
    • 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
    • A. Takagi, K. Sai, T. Umemura, R. Hasegawa and Y. Kurokawa (1990) 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, 53, 33-38.
    • (1990) Cancer Letters , vol.53 , pp. 33-38
    • Takagi, A.1    Sai, K.2    Umemura, T.3    Hasegawa, R.4    Kurokawa, Y.5
  • 15
    • 0027948537 scopus 로고
    • Di-(2-ethylhexyl) phthalate suppresses estradiol and ovulation in cycling rats
    • B.J. Davis, R.R. Maronpot and J.J. Heindel (1994) Di-(2-ethylhexyl) phthalate suppresses estradiol and ovulation in cycling rats. Toxicology and Applied Pharmacology, 128, 216-233.
    • (1994) Toxicology and Applied Pharmacology , vol.128 , pp. 216-233
    • Davis, B.J.1    Maronpot, R.R.2    Heindel, J.J.3
  • 16
    • 0021603008 scopus 로고
    • Biological effects of di-(2-ethylhexyl) phthalate and other phthalic acid esters
    • J.A. Thomas and M.J. Thomas (1984) Biological effects of di-(2-ethylhexyl) phthalate and other phthalic acid esters. Critical Reviews in Toxicology, 13, 283-317.
    • (1984) Critical Reviews in Toxicology , vol.13 , pp. 283-317
    • Thomas, J.A.1    Thomas, M.J.2
  • 20
    • 0020526811 scopus 로고
    • Platelet glutathione peroxidase activity as an index of selenium status in rats
    • O.A. Levander, D.P. Deloach, V.C. Morris and P.B. Moser (1983) Platelet glutathione peroxidase activity as an index of selenium status in rats. Journal of Nutrition, 113, 55-63.
    • (1983) Journal of Nutrition , vol.113 , pp. 55-63
    • Levander, O.A.1    Deloach, D.P.2    Morris, V.C.3    Moser, P.B.4
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • M. Bradford (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Chemistry, 72, 248-254.
    • (1976) Analytical Chemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 22
    • 0028169847 scopus 로고
    • Purification and immunoelectron microscopic localization of cellular glutathione peroxidase in rat hepatocytes: Quantitative analysis by postembedding method
    • K. Asayama, S. Yokata, K. Dobashi, H. Hayashibe, A. Kawaoi and S. Nakazawa (1994) Purification and immunoelectron microscopic localization of cellular glutathione peroxidase in rat hepatocytes: quantitative analysis by postembedding method. Histochemistry, 102, 213-219.
    • (1994) Histochemistry , vol.102 , pp. 213-219
    • Asayama, K.1    Yokata, S.2    Dobashi, K.3    Hayashibe, H.4    Kawaoi, A.5    Nakazawa, S.6
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0026071549 scopus 로고
    • Effect of diabetes mellitus induced by streptozotocin on renal superoxide dismutases in the rat. A radioimmunoassay and immunohistochemical study
    • K. Dobashi, K. Asayama, H. Hayashibe, N. Uchida, M. Kobayashi, A. Kawaoi and K. Kato (1991) Effect of diabetes mellitus induced by streptozotocin on renal superoxide dismutases in the rat. A radioimmunoassay and immunohistochemical study. Virchows Archiv B, 60, 67-72.
    • (1991) Virchows Archiv B , vol.60 , pp. 67-72
    • Dobashi, K.1    Asayama, K.2    Hayashibe, H.3    Uchida, N.4    Kobayashi, M.5    Kawaoi, A.6    Kato, K.7
  • 28
    • 0030034128 scopus 로고    scopus 로고
    • Decreased glutathione peroxidase activity in mice in response to nafenopin is caused by changes in selenium metabolism
    • P. Garberg and M. Thullberg (1996) Decreased glutathione peroxidase activity in mice in response to nafenopin is caused by changes in selenium metabolism. Chemico Biological Interactions, 99, 165-177.
    • (1996) Chemico Biological Interactions , vol.99 , pp. 165-177
    • Garberg, P.1    Thullberg, M.2
  • 29
    • 0030841938 scopus 로고    scopus 로고
    • Recent update on the PPAR alpha-null mouse
    • F.J. Gonzalez (1997) Recent update on the PPAR alpha-null mouse. Biochimie, 79, 139-144.
    • (1997) Biochimie , vol.79 , pp. 139-144
    • Gonzalez, F.J.1
  • 31
    • 0025769968 scopus 로고
    • Immunohistochemical localization of glutathione-S-transferase and glutathione peroxidase in adult syrian hamster tissues and during kidney development
    • T.D. Oberley, L.W. Oberley, A.F. Slattery and J.H. Elwell (1991) Immunohistochemical localization of glutathione-S-transferase and glutathione peroxidase in adult Syrian hamster tissues and during kidney development. American Journal of Pathology, 139, 355-369.
    • (1991) American Journal of Pathology , vol.139 , pp. 355-369
    • Oberley, T.D.1    Oberley, L.W.2    Slattery, A.F.3    Elwell, J.H.4
  • 32
    • 0344600822 scopus 로고
    • Immunohistochemical localization of cellular glutathione peroxidase in adult rat tissues by use of newly prepared polyclonal antibodies
    • K. Dobashi, K. Asayama, H. Hayashibe, A. Munim, N. Uchida, A. Kawaoi and S. Nakazawa (1994) Immunohistochemical localization of cellular glutathione peroxidase in adult rat tissues by use of newly prepared polyclonal antibodies. Yamanashi Medical Journal, 9, 69-79.
    • (1994) Yamanashi Medical Journal , vol.9 , pp. 69-79
    • Dobashi, K.1    Asayama, K.2    Hayashibe, H.3    Munim, A.4    Uchida, N.5    Kawaoi, A.6    Nakazawa, S.7
  • 33
    • 0029892360 scopus 로고    scopus 로고
    • Immunohistochemical localization and quantitative analysis of cellular glutathione peroxidase in fetal and neonatal rat tissues: Fluorescence microscopy image analysis
    • K. Asayama, K. Dobashi, Y. Kawada, T. Nakane, A. Kawaoi and S. Nakazawa (1996) Immunohistochemical localization and quantitative analysis of cellular glutathione peroxidase in fetal and neonatal rat tissues: fluorescence microscopy image analysis. Histochemical Journal, 28, 63-71.
    • (1996) Histochemical Journal , vol.28 , pp. 63-71
    • Asayama, K.1    Dobashi, K.2    Kawada, Y.3    Nakane, T.4    Kawaoi, A.5    Nakazawa, S.6
  • 34
    • 0023755328 scopus 로고
    • Comparison of constitutive and inducible levels of expression of peroxisomal β-oxidation and catalase gene in liver and extrahepatic tissues of rat
    • N.R. Nemali, N. Usuda, M.K. Reddy, K. Oyasu, T. Hashimoto, T. Osumi, M.S. Rao and J.K. Reddy (1988) Comparison of constitutive and inducible levels of expression of peroxisomal β-oxidation and catalase gene in liver and extrahepatic tissues of rat. Cancer Research, 48, 5316-5324.
    • (1988) Cancer Research , vol.48 , pp. 5316-5324
    • Nemali, N.R.1    Usuda, N.2    Reddy, M.K.3    Oyasu, K.4    Hashimoto, T.5    Osumi, T.6    Rao, M.S.7    Reddy, J.K.8
  • 36
    • 0030587573 scopus 로고    scopus 로고
    • 4-hydroxy-2-nonenal cytotoxicity in renal proximal tubular cells: Protein modification and redox alteration
    • A. Fukuda, T. Osawa, K. Hitomi and K. Uchida (1996) 4-hydroxy-2-nonenal cytotoxicity in renal proximal tubular cells: protein modification and redox alteration. Archives of Biochemistry and Biophysics, 333, 419-426.
    • (1996) Archives of Biochemistry and Biophysics , vol.333 , pp. 419-426
    • Fukuda, A.1    Osawa, T.2    Hitomi, K.3    Uchida, K.4
  • 37
    • 0031431392 scopus 로고    scopus 로고
    • Etheno-DNA base adducts as tools in human cancer aetiology and chemoprevention
    • H. Bartsch, J. Nair and I. Velic (1997) Etheno-DNA base adducts as tools in human cancer aetiology and chemoprevention. European Journal of Cancer Prevention, 6, 529-534.
    • (1997) European Journal of Cancer Prevention , vol.6 , pp. 529-534
    • Bartsch, H.1    Nair, J.2    Velic, I.3
  • 38
    • 0031863735 scopus 로고    scopus 로고
    • Reduction of phosphatidylcholine hydroperoxide by apolipoprotein A-I: Purification of the hydroperoxide-reducing proteins from human blood plasma
    • R. Mashima, Y. Yamamoto and S. Yoshimura (1998) Reduction of phosphatidylcholine hydroperoxide by apolipoprotein A-I: purification of the hydroperoxide-reducing proteins from human blood plasma. Journal of Lipid Research, 39, 1133-1140.
    • (1998) Journal of Lipid Research , vol.39 , pp. 1133-1140
    • Mashima, R.1    Yamamoto, Y.2    Yoshimura, S.3
  • 41
    • 0025007192 scopus 로고
    • Phthalate esters, cystic kidney disease in animals and possible effects on human health: A review
    • K.N. Woodward (1990) Phthalate esters, cystic kidney disease in animals and possible effects on human health: a review. Human and Experimental Toxicology, 9, 397-401.
    • (1990) Human and Experimental Toxicology , vol.9 , pp. 397-401
    • Woodward, K.N.1
  • 42
    • 0019171588 scopus 로고
    • Acute renal failure and interstitial nephritis after clofibrate treatment
    • A. Cumming (1980) Acute renal failure and interstitial nephritis after clofibrate treatment. British Medical Journal, 281, 1529-1530.
    • (1980) British Medical Journal , vol.281 , pp. 1529-1530
    • Cumming, A.1


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