41
Views
107
CrossRef citations to date
0
Altmetric
Original Article

Phospholipid Hydroperoxide Glutathione Peroxidase is a Seleno-Enzyme Distinct from the Classical Glutathione Peroxidase as Evident from Cdna and Amino Acid Sequencing

, , , , , , , & show all
Pages 343-361 | Received 28 Nov 1990, Accepted 09 Jan 1991, Published online: 07 Jul 2009

References

  • Mills G. C. Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. Journal of Biological Chemistry 1957; 229: 189–197
  • Flohé L. The selenoprotein glutathione peroxidase. Glutathion, D. Dolphin, R. Poulson, O. Avramovic. John Wiley & Sons, New York 1989; 643–731
  • Flohé L., Günzler W. A., Schock H. H. Glutathione peroxidase: a selenoenzyme. FEBS Lettes 1973; 32: 132–134
  • Forstrom J. W., Zakowski J. J., Tappel A. L. Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine. Biochemistry 1978; 17: 2639–2644
  • Wendel A., Kerner B., Graupe K. The selenium moiety of glutathione peroxidase. Hoppe-Seyler's Z. Physiol. Chem. 1978; 359: 1035–1036
  • Günzler W. A., Steffens G. J., Grossmann A., Kim S.-M. A., Ötting F., Wendel A., Flohé L. The amino-acid sequence of bovine glutathione peroxidase. Hoppe-Seyler's Z. Physiol. Chem. 1984; 365: 195–212
  • Mullenbach G. T., Tabrizi A., Irvine B. D., Bell G. I., Tainer J. A., Hallewell R. A. Selenocysteine's mechanism of incorporation and evolution revealed in cDNAs of three glutathione peroxidases. Protein Engineering 1988; 2: 239–246
  • Ladenstein R., Epp O., Bartels K., Jones A., Huber R., Wendel A. Structure analysis and molecular model of the selenoenzyme glutathione peroxidase at 2.8 å resolution. Journal of Molecular Biology 1979; 134: 199–218
  • Ladenstein R., Epp O., Günzler W. A., Flohé L. Glutathione peroxidase on approval. Life Chemistry Reports 1986; 4: 37–55
  • Takahashi K., Newburger P. E., Cohen H. J. Glutathione peroxidase protein. Absence in selenium deficiency states and correlation with enzymatic activity. Journal of Clinical Investigation 1986; 77: 1402–1404
  • Takahashi K., Cohen H. J. Selenium-dependent glutathione peroxidase protein and activity: immunological investigations on cellular and plasma enzymes. Blood 1986; 68: 640–645
  • Takahashi K., Akasaka M., Yamamoto Y., Kobayashi C., Mizoguchi J., Koyama J. Primary structure of human plasma glutathione peroxidase deduced from cDNA sequences. Journal of Biochemistry 1990; 108: 145–148
  • Grossman A., Wendel A. Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids. European Journal of Biochemistry 1983; 135: 549–552
  • Sevanian A., Muakkassah-Kelly S. F., Montestruque S. The influence of phospholipase A2 and glutathione peroxidase on the elimination of membrane lipid peroxides. Archies in Biochemistry and Biophysics 1983; 223: 441–452
  • Ursini F., Maiorino M., Valente M., Ferri L., 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. Biochimica et Biophysica Acta 1982; 710: 197–211
  • Ursini F., Maiorino M., Gregolin C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochimica et Biophysica Acta 1985; 839: 62–70
  • Laemli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
  • Crestfield A. M., Moore S., Stein W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. Journal of Biological Chemistry 1963; 238: 622–627
  • Gross E., Witkop B. Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide. Journal of American Chemistry 1961; 83: 1510–1511
  • Machleidt W., Wachter E. New supports in solid-phase sequencing. Methods in Enzymology 1977; 47: 263–377
  • Laursen R. A. Solid-phase Edman degradation. European Journal of Biochemistry 1979; 20: 89–102
  • Lottspeich F. Identification of the phenylthiohydantoin derivatives of amino acids by high pressure liquid chromatography. Using a ternary, isocratic solvent system. Hoppe-Seyler's Z. Physiol. Chem. 1980; 361: 1829–1834
  • Saiki R. K., Gelfand D. H., Stoffel S., Scharf S. J., Higuchi R., Horn G. T., Mullis K. B., Erlich H. A. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 1988; 239: 487–491
  • Maniatis T., Fritsch E. F., Sambrook J. Molecular Cloning, A Laboratory Manual. Cold Spring Harbor Laboratory. 1982
  • Ausubel F. M., Brent R., Kingston R. E., Moore D. D., Seidman J. G., Smith J. A., Struhl K. Current Protocols In Molecular Biology. John Wiley & Sons, New York 1987
  • Dumais M. M., Nochumson S. In-gel ligation and transformation of double-stranded DNA (dsDNA). Bio Techniques 1987; 5: 62
  • Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences USA 1977; 74: 5463–5467
  • Adams S. P., Kavka K. S., Wykes E. J., Holder S. B., Galluppi G. R. Hindered dialkylamino nucleoside phosphite reagents in the synthesis of two DNA 51-mers. Journal of the American Chemistry Society 1983; 105: 661–663
  • Sukenaga Y., Ishida K., Takeda T., Takagi K. cDNA sequence coding for human glutathione peroxidase. Nucleic Acids Research 1987; 15: 7178
  • Akasaka M., Mizoguchi J., Yoshimura S., Watanabe K. Nucleotide sequence of cDNA for rabbit glutathione peroxidase. Nucleic Acids Research 1989; 17: 2136
  • Ho Y.-S., Howard A. J., Crapo J. D. Nucleotide sequence of a rat glutathione peroxidase cDNA. Nucleic Acids Research 1988; 16: 5207
  • Chambers I., Frampton J., Goldfarb 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 Journal 1986; 5: 1221–1227
  • Stadtman T. C. Specific occurrence of selenium in enzymes and amino acid tRNAs. FASEB Journal 1987; 1: 375–379
  • Leinfelder W., Zehelein E., Mandrand-Berthelot M. A., Böck A. Gene for a novel tRNA species that accepts L-serine and cotranslationally inserts selenocysteine. Nature 1988; 331: 723–725
  • Weitzel F., Ursini F., Wendel A. Phospholipid hydroperoxide glutathione peroxidase in various mouse organs during selenium deficiency and repletion. Biochimica et Biophysica Acta 1990; 1036: 88–94
  • Steffens G. J., Bannister J. V., Bannister W. H., Flohé L., Günzler W. A., Kim S.-M. A., Ötting F. The primary structure of Cu-Zn superoxide dismutase from Photobacterium leiognathi: ecidence for a separate evolution of Cu-Zn superoxide dismutase in bacteria. Hoppe-Seyler's Z. Physiol. Chem. 1983; 364: 675–690
  • Epp O., Ladenstein R., Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. European Journal of Biochemistry 1983; 133: 51–69
  • Kemp B. E., Pearson R. B. Protein kinase recognition sequence motifs. TIBS 1990; 15: 342–346

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.