Effect of selenium deficiency on cellular and extracellular glutathione peroxidases: Immunochemical detection and mRNA analysis in rat kidney and serum

Free Radical Biology and Medicine

Volumn 25, Issue 4-5, 1998, Pages 504-511

  Nakane, Takaya ^a   Asayama, Kohtaro ^a   Kodera, Kohji ^a   Hayashibe, Hidemasa ^a   Uchida, Norihiko ^a   Nakazawa, Shinpei ^a  

^a UNIVERSITY OF YAMANASHI   (Japan)

Author keywords

Antioxidants; Free radicals; Gene expression; Glutathione peroxidase; Protein purification; Rocket immunoelectrophoresis; Selenium; Serum protein

Indexed keywords

BETA ACTIN; GLUTATHIONE PEROXIDASE; MESSENGER RNA; POLYCLONAL ANTIBODY; SELENIUM;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; IMMUNOCHEMISTRY; KIDNEY; LIVER; MALE; NONHUMAN; PRIORITY JOURNAL; RAT; SELENIUM DEFICIENCY; SERUM;

ANIMALS; GLUTATHIONE PEROXIDASE; IMMUNOBLOTTING; IMMUNOELECTROPHORESIS; IMMUNOHISTOCHEMISTRY; ISOENZYMES; KIDNEY; LIVER; MALE; RATS; RATS, SPRAGUE-DAWLEY; RNA, MESSENGER; SELENIUM;

ANIMALIA; HESPERIS;

EID: 0032171220     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(98)00078-1     Document Type: Article

References (34)

1. Takahashi K., Avissar N., Whitin J., Cohen H. Purification and characterization of human plasma glutathione peroxidase a selenoglycoprotein distinct from the known cellular enzyme . Arch. Biochem. Biophys. 256:1987;677-686.
2. Ursini F., Mariorino M., Gregolin C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochim. Biophys. Acta. 839:1985;62-70.
3. Chu F.F., Doroshow J.H., Esworthy R.S. Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSH-Px-GI. J. Biol. Chem. 268:1993;2571-2578.
4. Esworthy R.S., Chu F.F., Geiger P., Girotti A.W., Doroshow J.H. Reactivity of plasma glutathione peroxidase with hydroperoxide substrates and glutathione. Arch. Biochem. Biophys. 307:1993;29-34.
5. Roveri A., Casasco A., Maiorino M., Dalan P., Calligaro A., Ursini F. Phospholipid hydroperoxide glutathione peroxidase of rat testis. J. Biol. Chem. 267:1992;6142-6146.
6. 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. J. Biochem. 109:1991;918-923.
7. Avissar N., Ornt D.B., Yagil Y., Horowitz S., Watkins R.H., Kerl E.A., Takahashi K., Palmer I.S., Cohen H.J. Human kidney proximal tubules are the main source of plasma glutathione peroxidase. Am. J. Physiol. 266:(2 Pt 1):1994;C367-C375.
8. 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. 79:1992;3233-3238.
9. Hafeman D.G., Sunde R.A., Hoekstra W.G. Effect of dietary selenium on erythrocyte and liver glutathione peroxidase in the rat. J. Nutr. 104:1974;580-587.
10. Lei X.G., Evenson J.K., Thompson K.M., Sunde R.A. Glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase are differentially regulated in rats by dietary selenium. J. Nutr. 125:1995;1438-1446.
11. Hill K.E., Burk R.F., Lane J.M. Effect of selenium depletion and repletion on plasma glutathione and glutathione-dependent enzymes in the rat. J. Nutr. 117:1987;99-104.
12. Waschulewski I.H., Sunde R.A. Effect of dietary methionine on utilization of tissue selenium from dietary selenomethionine for glutathione peroxidase in the rat. J. Nutr. 118:1988;367-374.
13. Asayama K., Yokota 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. 102:1994;213-219.
14. Weeke B. Rocket immunoelectrophoresis. Axelsen N.H., Krφll J., Weeke B. A manual of quantitative immunoelectrophoresis methods and applications. 1973;37-46 Universitetsforlaget, Oslo.
15. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
16. Yoshimura S., Takekoshi S., Watanabe K., Fujii-Kuriyama Y. Determination of nucleotide sequence of cDNA coding rat glutathione peroxidase and diminished expression of mRNA in selenium deficient rats. Biochem. Biophys. Res. Commun. 154:1988;1024-1028.
17. Shimura H., Okajima F., Ikuyama S., Shimura Y., Kimura S., Saji M., Kohn L.D. Thyroid-specific expression and cyclic adenosine 3′, 5′-monophosphate autoregulation of the thyrotropin receptor gene involves thyroid transcription factor-1. Mol. Endocrinol. 8:1994;1049-1069.
18. Sambrook J., Fritsch E.F., Maniatis T. Molecular cloning: A laboratory manual. 2nd ed. 1989;7.26-7.29 Cold Spring Harbor Laboratory Press, New York.
19. Asayama K., Dettbarn W.D., Burr I.M. Differential effect of denervation on free radical scavenging enzymes in slow and fast muscle of rat. J. Neurochem. 46:1986;604-609.
20. Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Chem. 72:1976;248-254.
21. Weiss S.L., Evenson J.K., Thompson K.M., Sunde R.A. The selenium requirement for glutathione peroxidase mRNA level is half of the selenium requirement for glutathione peroxidase activity in female rats. J. Nutr. 126:1996;2260-2267.
22. Bermano G., Nicol F., Dyer J.A., Sunde R.A., Baccate G.J., Arthur J.R., Hesketh J.E. Tissue-specific regulation of selenoenzyme gene expression during selenium deficiency in rats. Biochem. J. 311:(Pt 2):1995;425-430.
23. Bermano G., Nicol F., Dyer J.A., Sunde R.A., Baccate G.J., Arthur J.R., Hesketh J.E. Selenoprotein gene expression during selenium-repletion of selenium-deficient rats. Biol. Trace Element Res. 51:1996;211-223.
24. Knight S.A., Sunde R.A. The effect of progressive selenium deficiency on anti-glutathione peroxidase antibody reactive protein in rat liver. J. Nutr. 117:1987;732-738.
25. Avissar N., Kerl E.A., Baker S.S., Cohen H.J. Extracellular glutathione peroxidase mRNA and protein in human cell lines. Arch. Biochem. Biophys. 309:1994;239-246.
26. Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H. Structure and function of the 5′-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J. Biol. Chem. 267:1992;5949-5958.
27. Christensen M.J., Burgener K.W. Dietary selenium stabilizes glutathione peroxidase mRNA in rat liver. J. Nutr. 122:1992;1620-1626.
28. Hubert N., Walczak R., Carbon P., Krol A. A protein binds the selenocysteine insertion element in the 3′-UTR of mammalian selenoprotein mRNAs. Nucleic Acids Res. 24:1996;464-469.
29. Shen Q., Chu F.F., Newburger P.E. Sequences in the 3′-untranslated region of the human cellular glutathione peroxidase gene are necessary and sufficient for selenocysteine incorporation at the UGA codon. J. Biol. Chem. 268:1993;11463-11469.
30. Shen Q., McQuilkin P.A., Newburger P.E. RNA-binding proteins that specifically recognize the selenocysteine insertion sequence of human cellular glutathione peroxidase mRNA. J. Biol. Chem. 270:1995;30448-30452.
31. Baron C., Heider J., Bock A. Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA. Proc. Natl. Acad. Sci. USA. 90:1993;4181-4185.
32. Ringquist S., Schneider D., Gibson T., Baron C., Bock A., Gold L. Recognition of the mRNA selenocysteine insertion sequence by the specialized translational elongation factor SELB. Gen. Dev. 8:1994;376-385.
33. Hawkes W.C., Lyons D.E., Tappel A.L. Identification of a selenocysteine-specific aminoacyl transfer RNA from rat liver. Biochim. Biophys. Acta. 699:1982;183-191.
34. Hill K.E., Lloyd R.S., Burk R.F. Conserved nucleotide sequences in the open reading frame and 3′ untranslated region of selenoprotein P mRNA. Proc. Natl. Acad. Sci. USA. 90:1993;537-541.