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Volumn 20, Issue 8, 1997, Pages 439-444

Puberty influences expression of phospholipid hydroperoxide glutathione peroxidase (GPX4) in rat testis: Probable hypophysis regulation of the enzyme in male reproductive tract

Author keywords

Glutathione peroxidase; Hypophysis liver; Lung; Oxygen free radicals; Phospholipid hydroperoxide glutathione peroxidase; Puberty; Testis

Indexed keywords

ANTIOXIDANT; GLUTATHIONE PEROXIDASE; OXYGEN RADICAL; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; POLYUNSATURATED FATTY ACID; UNCLASSIFIED DRUG;

EID: 0030728911     PISSN: 03914097     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF03347999     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 0023617012 scopus 로고
    • Cellular basis of defective sperm function and its association with the genesis of reactive oxygen species by human spermatozoa
    • Aitken R.J., Clarkson J.S. Cellular basis of defective sperm function and its association with the genesis of reactive oxygen species by human spermatozoa. J. Reprod. Fertil. 81: 459, 1987.
    • (1987) J. Reprod. Fertil. , vol.81 , pp. 459
    • Aitken, R.J.1    Clarkson, J.S.2
  • 2
    • 0024337024 scopus 로고
    • Role of glutathione peroxidase in protecting mammalian spermatozoa from loss of motility caused by spontaneous lipid peroxidation
    • Alvarez J.G., Storey B.T. Role of glutathione peroxidase in protecting mammalian spermatozoa from loss of motility caused by spontaneous lipid peroxidation. Gamete Res. 23: 77, 1989.
    • (1989) Gamete Res. , vol.23 , pp. 77
    • Alvarez, J.G.1    Storey, B.T.2
  • 3
    • 0024420213 scopus 로고
    • Lipid peroxidation in human spermatozoa as related to midpiece abnormalities and motility
    • Rao B., Soufir J.C., Martin M., David G. Lipid peroxidation in human spermatozoa as related to midpiece abnormalities and motility. Gamete Res. 24: 127, 1989.
    • (1989) Gamete Res. , vol.24 , pp. 127
    • Rao, B.1    Soufir, J.C.2    Martin, M.3    David, G.4
  • 4
    • 0022730806 scopus 로고
    • The structure of the mouse glutathione peroxidase gene: The selenocysteine in the active site is encoded by the "termination" codon, TGA
    • Chambers I., Frampton J., Goldfard P., Affara N., McBain W., Harrison P.R. The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the "termination" codon, TGA. Embo J. 5: 1221, 1986.
    • (1986) Embo J. , vol.5 , pp. 1221
    • Chambers, I.1    Frampton, J.2    Goldfard, P.3    Affara, N.4    McBain, W.5    Harrison, P.R.6
  • 5
    • 0027536023 scopus 로고
    • Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI
    • Chu F.F., Doroshow J.H., Esworthy R.S. Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J. Biol. Chem. 268: 2571, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2571
    • Chu, F.F.1    Doroshow, J.H.2    Esworthy, R.S.3
  • 6
    • 0025327429 scopus 로고
    • Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences
    • Tokyo
    • Takahashi K., Akasaka M., Yamamoto Y., Kobayashi C., Mizoguchi J., Koyama J. Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences. J. Biochem. (Tokyo) 108: 145, 1990.
    • (1990) J. Biochem. , vol.108 , pp. 145
    • Takahashi, K.1    Akasaka, M.2    Yamamoto, Y.3    Kobayashi, C.4    Mizoguchi, J.5    Koyama, J.6
  • 7
    • 0026773732 scopus 로고
    • Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung and breast in humans and rodents
    • Chu F.F., Esworthy R.S., Doroshow J.H., Doan K., Liu X.F. Expression of plasma glutathione peroxidase in human liver in addition to kidney, heart, lung and breast in humans and rodents. Blood 79: 3233, 1992.
    • (1992) Blood , vol.79 , pp. 3233
    • Chu, F.F.1    Esworthy, R.S.2    Doroshow, J.H.3    Doan, K.4    Liu, X.F.5
  • 9
    • 0026714544 scopus 로고
    • Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon
    • Perry A.C.F., Jones R., Niang S.P., Jackson R.M., Hall L. Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon. Biochem. J. 285: 863, 1992.
    • (1992) Biochem. J. , vol.285 , pp. 863
    • Perry, A.C.F.1    Jones, R.2    Niang, S.P.3    Jackson, R.M.4    Hall, L.5
  • 10
    • 0020065662 scopus 로고
    • Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides
    • Ursini F., Maiorino M., Gregolin C. Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides. Biochim. Biophys. Acta 710: 197, 1982.
    • (1982) Biochim. Biophys. Acta , vol.710 , pp. 197
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 11
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • Ursini,F., Maiorino M., Gregolin C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta 839: 62, 1985.
    • (1985) Biochim. Biophys. Acta , vol.839 , pp. 62
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 12
    • 0025744144 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase is a selenoenzyme distinct from the classical glutathione peroxidase as evident from cDNA and amino acid sequencing
    • Schuckelt R., Brigelius-Flohe R., Maiorino M., Roveri A., Reumkens J., Srtabburger W., Ursini F., Flohe L. Phospholipid hydroperoxide glutathione peroxidase is a selenoenzyme distinct from the classical glutathione peroxidase as evident from cDNA and amino acid sequencing. Free Radical Res. Commun. 14: 343, 1991.
    • (1991) Free Radical Res. Commun. , vol.14 , pp. 343
    • Schuckelt, R.1    Brigelius-Flohe, R.2    Maiorino, M.3    Roveri, A.4    Reumkens, J.5    Srtabburger, W.6    Ursini, F.7    Flohe, L.8
  • 13
    • 0024350070 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase: Specific activity in tissues of rats of different age and comparison with other glutathione peroxidases
    • Zhang L., Maiorino M., Roveri A., Ursini, F. Phospholipid hydroperoxide glutathione peroxidase: specific activity in tissues of rats of different age and comparison with other glutathione peroxidases. Biochim. Biophys. Acta 1006: 140, 1989.
    • (1989) Biochim. Biophys. Acta , vol.1006 , pp. 140
    • Zhang, L.1    Maiorino, M.2    Roveri, A.3    Ursini, F.4
  • 14
    • 0026760653 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase of rat testis- gonadotropin dependence and immunocytochemical identification
    • Roveri A., Casasco A., Maiorino M., Dalan P., Calligaro A., Ursini F. Phospholipid hydroperoxide glutathione peroxidase of rat testis-gonadotropin dependence and immunocytochemical identification. J. Biol. Chem. 267: 6142, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6142
    • Roveri, A.1    Casasco, A.2    Maiorino, M.3    Dalan, P.4    Calligaro, A.5    Ursini, F.6
  • 15
    • 0028122601 scopus 로고
    • Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase
    • Esworthy R.S., Doan K., Doroshow J.H., Chu F.F. Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase. Gene 144:317, 1994.
    • (1994) Gene , vol.144 , pp. 317
    • Esworthy, R.S.1    Doan, K.2    Doroshow, J.H.3    Chu, F.F.4
  • 16
    • 0027290565 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase: Full-length pig blastocyst cDNA sequence and regulation by selenium status
    • Sunde R.A., Dyer J.A., Moran T.V., Everson J.K., Sugimoto M. Phospholipid hydroperoxide glutathione peroxidase: full-length pig blastocyst cDNA sequence and regulation by selenium status. Biochem. Biophys. Res. Commun. 193: 905, 1993.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 905
    • Sunde, R.A.1    Dyer, J.A.2    Moran, T.V.3    Everson, J.K.4    Sugimoto, M.5
  • 17
    • 0026527823 scopus 로고
    • Structure and expression of the rat epididymal secretory protein I gene
    • Girotti M., Jones R., Emery D.C., Chia W., Hall L. Structure and expression of the rat epididymal secretory protein I gene. Biochem. J. 281:203, 1992.
    • (1992) Biochem. J. , vol.281 , pp. 203
    • Girotti, M.1    Jones, R.2    Emery, D.C.3    Chia, W.4    Hall, L.5
  • 18
    • 0023941841 scopus 로고
    • Generation of cDNA probes directed by amino acid sequence: Cloning of urate oxidase
    • Lee C.C., Wu X., Gibbs R.A., Cook R.G., Muzny D.M., Caskey C.T. Generation of cDNA probes directed by amino acid sequence: cloning of urate oxidase. Science 239: 1288, 1988.
    • (1988) Science , vol.239 , pp. 1288
    • Lee, C.C.1    Wu, X.2    Gibbs, R.A.3    Cook, R.G.4    Muzny, D.M.5    Caskey, C.T.6
  • 20
    • 0017616363 scopus 로고
    • Analysis of restriction fragments of T7 DNA and determination of molecular weights by electrophoresis in neutral and alkaline gels
    • MacDonell M.W., Simon M.N., Studier F.W. Analysis of restriction fragments of T7 DNA and determination of molecular weights by electrophoresis in neutral and alkaline gels. J. Mol. Biol. 110: 119, 1977.
    • (1977) J. Mol. Biol. , vol.110 , pp. 119
    • MacDonell, M.W.1    Simon, M.N.2    Studier, F.W.3
  • 21
    • 0017822995 scopus 로고
    • Use of the T4 polynucleotide ligase in the joining of flush-ended DNA segments generated by restriction endonucleases
    • Sgaramella V., Ehrlich S.D. Use of the T4 polynucleotide ligase in the joining of flush-ended DNA segments generated by restriction endonucleases. Eur. J. Biochem. 86: 531, 1978.
    • (1978) Eur. J. Biochem. , vol.86 , pp. 531
    • Sgaramella, V.1    Ehrlich, S.D.2
  • 22
    • 0000374924 scopus 로고
    • Polynucleotide kinase from Escherichia coli infected with bacteriophage T4
    • Richardson C.C. Polynucleotide kinase from Escherichia coli infected with bacteriophage T4. In: procedures in nucleic acid research. 2: 815, 1971.
    • (1971) Procedures in Nucleic Acid Research , vol.2 , pp. 815
    • Richardson, C.C.1
  • 23
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electrophoration
    • Downer W.J., Miller J.F., Ragsdale C.W. High efficiency transformation of E. coli by high voltage electrophoration. Nucleic Acids Res. 16: 6127, 1988.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6127
    • Downer, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 24
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim H.C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7: 1513, 1979.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513
    • Birnboim, H.C.1    Doly, J.2
  • 27
    • 0021381028 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg A.P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 737:266, 1984.
    • (1984) Anal. Biochem. , vol.737 , pp. 266
    • Feinberg, A.P.1    Vogelstein, B.2
  • 29
    • 0024616214 scopus 로고
    • Spermatogenic cell-somatic cell interactions are required for maintenance of spermatogenic cell glutathione
    • Luyuan Li, A.P. Seddon., A. Meister., M.S. Risley. Spermatogenic cell-somatic cell interactions are required for maintenance of spermatogenic cell glutathione. Biol. Reprod. 40: 317, 1989.
    • (1989) Biol. Reprod. , vol.40 , pp. 317
    • Li, L.1    Seddon, A.P.2    Meister, A.3    Risley, M.S.4
  • 30
    • 0024578662 scopus 로고
    • Glutathione deficiency in the epithelial lining fluid of the lower respiratory tract in idiopathic pulmonary fibrosis
    • Cantin A.M., Hubbard R.C., Crystal R.G. Glutathione deficiency in the epithelial lining fluid of the lower respiratory tract in idiopathic pulmonary fibrosis. Am. Rev. Respir. Dis. 139: 370, 1989.
    • (1989) Am. Rev. Respir. Dis. , vol.139 , pp. 370
    • Cantin, A.M.1    Hubbard, R.C.2    Crystal, R.G.3
  • 31
    • 0024296177 scopus 로고
    • A 13 bp palindrome is a functional estrogen responsive element and interacts specifically with estrogen receptor
    • Klein-Hitpass L., Ryffel G.U., Heitlinger E., Cato A.C.B. A 13 bp palindrome is a functional estrogen responsive element and interacts specifically with estrogen receptor. Nucleic Acids Res. 16: 647, 1988.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 647
    • Klein-Hitpass, L.1    Ryffel, G.U.2    Heitlinger, E.3    Cato, A.C.B.4
  • 32
    • 0023850112 scopus 로고
    • Cooperativity of the glucocorticoid receptor and the CACCC-box binding factor
    • Schule R., Muller M., Otsuka-Murakami H., Renkawitz R. Cooperativity of the glucocorticoid receptor and the CACCC-box binding factor. Nature 332: 87, 1988.
    • (1988) Nature , vol.332 , pp. 87
    • Schule, R.1    Muller, M.2    Otsuka-Murakami, H.3    Renkawitz, R.4


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