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. 1998 Jul 1;333(Pt 1):5–9. doi: 10.1042/bj3330005

The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract.

L Hall 1, K Williams 1, A C Perry 1, J Frayne 1, J A Jury 1
PMCID: PMC1219548  PMID: 9639555

Abstract

An epididymis-specific, secretory glutathione peroxidase (GPX5) has been proposed previously to play a role in protecting mammalian sperm membranes from the deleterious effects of lipid peroxidation, which, if not contained, can lead to reduced fertilizing capacity. Here we report the cDNA cloning of human GPX5 and show that the majority of transcripts contain a 118 nt frame-shifting deletion, arising, most likely, from inappropriate excision of exon 3 during processing. Antisera raised against recombinant human GPX5 cross-reacted with rat and macaque (Macaca fascicularis) epididymal proteins of the size expected for full-length, active GPX5. However, no similar reactivity could be demonstrated in any of the human samples tested.

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Selected References

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  1. Aitken R. J., Clarkson J. S., Fishel S. Generation of reactive oxygen species, lipid peroxidation, and human sperm function. Biol Reprod. 1989 Jul;41(1):183–197. doi: 10.1095/biolreprod41.1.183. [DOI] [PubMed] [Google Scholar]
  2. Cummins J. M., Jequier A. M., Kan R. Molecular biology of human male infertility: links with aging, mitochondrial genetics, and oxidative stress? Mol Reprod Dev. 1994 Mar;37(3):345–362. doi: 10.1002/mrd.1080370314. [DOI] [PubMed] [Google Scholar]
  3. Frayne J., Jury J. A., Barker H. L., Perry A. C., Jones R., Hall L. Macaque MDC family of proteins: sequence analysis, tissue distribution and processing in the male reproductive tract. Mol Hum Reprod. 1998 May;4(5):429–437. doi: 10.1093/molehr/4.5.429. [DOI] [PubMed] [Google Scholar]
  4. Ghyselinck N. B., Dufaure I., Lareyre J. J., Rigaudière N., Mattéi M. G., Dufaure J. P. Structural organization and regulation of the gene for the androgen-dependent glutathione peroxidase-like protein specific to the mouse epididymis. Mol Endocrinol. 1993 Feb;7(2):258–272. doi: 10.1210/mend.7.2.8469239. [DOI] [PubMed] [Google Scholar]
  5. Jones R. Preparation of a plasma membrane-rich fraction from rat spermatozoa. J Reprod Fertil. 1986 Jul;77(2):435–449. doi: 10.1530/jrf.0.0770435. [DOI] [PubMed] [Google Scholar]
  6. Okamura N., Iwaki Y., Hiramoto S., Tamba M., Bannai S., Sugita Y., Syntin P., Dacheux F., Dacheux J. L. Molecular cloning and characterization of the epididymis-specific glutathione peroxidase-like protein secreted in the porcine epididymal fluid. Biochim Biophys Acta. 1997 Jul 19;1336(1):99–109. doi: 10.1016/s0304-4165(97)00016-0. [DOI] [PubMed] [Google Scholar]
  7. Perry A. C., Jones R., Hall L. Isolation and characterization of a rat cDNA clone encoding a secreted superoxide dismutase reveals the epididymis to be a major site of its expression. Biochem J. 1993 Jul 1;293(Pt 1):21–25. doi: 10.1042/bj2930021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Perry A. C., Jones R., Niang L. S., 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. 1992 Aug 1;285(Pt 3):863–870. doi: 10.1042/bj2850863. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Storey B. T. Biochemistry of the induction and prevention of lipoperoxidative damage in human spermatozoa. Mol Hum Reprod. 1997 Mar;3(3):203–213. doi: 10.1093/molehr/3.3.203. [DOI] [PubMed] [Google Scholar]
  10. Vernet P., Faure J., Dufaure J. P., Drevet J. R. Tissue and developmental distribution, dependence upon testicular factors and attachment to spermatozoa of GPX5, a murine epididymis-specific glutathione peroxidase. Mol Reprod Dev. 1997 May;47(1):87–98. doi: 10.1002/(SICI)1098-2795(199705)47:1<87::AID-MRD12>3.0.CO;2-X. [DOI] [PubMed] [Google Scholar]
  11. Vernet P., Rigaudiére N., Ghyselinck N., Dufaure J. P., Drevet J. R. In vitro expression of a mouse tissue specific glutathione-peroxidase-like protein lacking the selenocysteine can protect stably transfected mammalian cells against oxidative damage. Biochem Cell Biol. 1996;74(1):125–131. doi: 10.1139/o96-014. [DOI] [PubMed] [Google Scholar]
  12. Williams K., Frayne J., McLaughlin E. A., Hall L. Expression of extracellular superoxide dismutase in the human male reproductive tract, detected using antisera raised against a recombinant protein. Mol Hum Reprod. 1998 Mar;4(3):235–242. doi: 10.1093/molehr/4.3.235. [DOI] [PubMed] [Google Scholar]

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