Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1992 Aug 1;285(Pt 3):863–870. doi: 10.1042/bj2850863

Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon.

A C Perry 1, R Jones 1, L S Niang 1, R M Jackson 1, L Hall 1
PMCID: PMC1132876  PMID: 1386734

Abstract

Epididymal glutathione peroxidase (GPX) has been suggested as a major factor in combating loss of fertility of spermatozoa due to lipid peroxidation. We report here the isolation and sequence of putative GPX cDNAs from rat (Rattus rattus) and cynomolgus-monkey (Macaca fascicularis) epididymis, which exhibit marked sequence identity with known GPXs. In both species the cDNAs encode predicted preproteins containing 221 amino acid residues. Unlike other characterized GPX sequences, epididymal GPX mRNA does not contain a selenocysteine codon (UGA). However, sequence comparison and molecular-modelling studies suggest a high degree of structural conservation between epididymal and other GPXs. Transcripts corresponding to epididymal GPX are not detected in a variety of other tissues (liver, spleen, kidney and testis) and appear to be androgen-regulated in the epididymis.

Full text

PDF
863

Images in this article

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. 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. 1987 Nov;81(2):459–469. doi: 10.1530/jrf.0.0810459. [DOI] [PubMed] [Google Scholar]
  2. 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. 1989 May;23(1):77–90. doi: 10.1002/mrd.1120230108. [DOI] [PubMed] [Google Scholar]
  3. Claessens M., Van Cutsem E., Lasters I., Wodak S. Modelling the polypeptide backbone with 'spare parts' from known protein structures. Protein Eng. 1989 Jan;2(5):335–345. doi: 10.1093/protein/2.5.335. [DOI] [PubMed] [Google Scholar]
  4. Craig R. K., Brown P. A., Harrison O. S., McIlreavy D., Campbell P. N. Guinea-pig milk-protein synthesis. Isolation and characterization of messenger ribonucleic acids from lactating mammary gland and identification of caseins and pre-alpha-lactalbumin as translation products in heterologous cell-free systems. Biochem J. 1976 Oct 15;160(1):57–74. doi: 10.1042/bj1600057. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dower W. J., Miller J. F., Ragsdale C. W. High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 1988 Jul 11;16(13):6127–6145. doi: 10.1093/nar/16.13.6127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Epp O., Ladenstein R., Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur J Biochem. 1983 Jun 1;133(1):51–69. doi: 10.1111/j.1432-1033.1983.tb07429.x. [DOI] [PubMed] [Google Scholar]
  7. Faure J., Ghyselinck N. B., Jimenez C., Dufaure J. P. Specific distribution of messenger ribonucleic acids for 24-kilodalton proteins in the mouse epididymis as revealed by in situ hybridization: developmental expression and regulation in the adult. Biol Reprod. 1991 Jan;44(1):13–22. doi: 10.1095/biolreprod44.1.13. [DOI] [PubMed] [Google Scholar]
  8. Feinberg A. P., Vogelstein B. "A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity". Addendum. Anal Biochem. 1984 Feb;137(1):266–267. doi: 10.1016/0003-2697(84)90381-6. [DOI] [PubMed] [Google Scholar]
  9. Ghyselinck N. B., Dufaure J. P. A mouse cDNA sequence for epididymal androgen-regulated proteins related to glutathione peroxidase. Nucleic Acids Res. 1990 Dec 11;18(23):7144–7144. doi: 10.1093/nar/18.23.7144. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Ghyselinck N. B., Jimenez C., Lefrançois A. M., Dufaure J. P. Molecular cloning of a cDNA for androgen-regulated proteins secreted by the mouse epididymis. J Mol Endocrinol. 1990 Feb;4(1):5–12. doi: 10.1677/jme.0.0040005. [DOI] [PubMed] [Google Scholar]
  11. Girotti M., Jones R., Emery D. C., Chia W., Hall L. Structure and expression of the rat epididymal secretory protein I gene. An androgen-regulated member of the lipocalin superfamily with a rare splice donor site. Biochem J. 1992 Jan 1;281(Pt 1):203–210. doi: 10.1042/bj2810203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Grunstein M., Hogness D. S. Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3961–3965. doi: 10.1073/pnas.72.10.3961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Humphries S. E., Whittall R., Minty A., Buckingham M., Williamson R. There are approximately 20 actin gene in the human genome. Nucleic Acids Res. 1981 Oct 10;9(19):4895–4908. doi: 10.1093/nar/9.19.4895. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Jones R., Mann T., Sherins R. Peroxidative breakdown of phospholipids in human spermatozoa, spermicidal properties of fatty acid peroxides, and protective action of seminal plasma. Fertil Steril. 1979 May;31(5):531–537. doi: 10.1016/s0015-0282(16)43999-3. [DOI] [PubMed] [Google Scholar]
  15. Kozak M. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol Rev. 1983 Mar;47(1):1–45. doi: 10.1128/mr.47.1.1-45.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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 Eng. 1988 Sep;2(3):239–246. doi: 10.1093/protein/2.3.239. [DOI] [PubMed] [Google Scholar]
  17. Rao B., Soufir J. C., Martin M., David G. Lipid peroxidation in human spermatozoa as related to midpiece abnormalities and motility. Gamete Res. 1989 Oct;24(2):127–134. doi: 10.1002/mrd.1120240202. [DOI] [PubMed] [Google Scholar]
  18. Schuckelt R., Brigelius-Flohé R., Maiorino M., Roveri A., Reumkens J., Strassburger W., Ursini F., Wolf B., Flohé L. Phospholipid hydroperoxide glutathione peroxidase is a selenoenzyme distinct from the classical glutathione peroxidase as evident from cDNA and amino acid sequencing. Free Radic Res Commun. 1991;14(5-6):343–361. doi: 10.3109/10715769109093424. [DOI] [PubMed] [Google Scholar]
  19. Sukenaga Y., Ishida K., Takeda T., Takagi K. cDNA sequence coding for human glutathione peroxidase. Nucleic Acids Res. 1987 Sep 11;15(17):7178–7178. doi: 10.1093/nar/15.17.7178. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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. 1990 Aug;108(2):145–148. doi: 10.1093/oxfordjournals.jbchem.a123172. [DOI] [PubMed] [Google Scholar]
  21. Twigg A. J., Sherratt D. Trans-complementable copy-number mutants of plasmid ColE1. Nature. 1980 Jan 10;283(5743):216–218. doi: 10.1038/283216a0. [DOI] [PubMed] [Google Scholar]
  22. Walker J. E., Jones R., Moore A., Hamilton D. W., Hall L. Analysis of major androgen-regulated cDNA clones from the rat epididymis. Mol Cell Endocrinol. 1990 Nov 12;74(1):61–68. doi: 10.1016/0303-7207(90)90205-m. [DOI] [PubMed] [Google Scholar]
  23. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983 Jun 1;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES