Startseite Testis-Specific Expression of the Nuclear Form of Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx)
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Testis-Specific Expression of the Nuclear Form of Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx)

  • S. G. Moreno , G. Laux , M. Brielmeier , G. W. Bornkamm und M. Conrad
Veröffentlicht/Copyright: 1. Juni 2005
Biological Chemistry
Aus der Zeitschrift Band 384 Heft 4

Abstract

The selenoprotein phospholipid hydroperoxide glutathione peroxidase (PHGPx) is present in at least three different isoforms in testis: as a cytosolic, as a mitochondrial, and as a nuclear protein. We have recently shown that a sperm nucleus-specific glutathione peroxidase (snGPx) is identical to the mitochondrial and cytosolic forms of PHGPx apart from its N-terminus. This arginine-rich N-terminus of snGPx, reminiscent of protamines, is encoded by an alternative exon located in the first intron of the PHGPx gene and is responsible for nuclear localisation and chromatin binding of snGPx [Pfeifer et al., FASEB J. 15 (2001), pp. 1236-1238]. By using a combination of techniques including selective cloning of mRNA 5' ends, RT-PCR, and S1 analyses, we provide evidence that the transcript encoding the nuclear form is generated by transcription initiation at an alternative promoter and not by alternative splicing. We show that the major transcription start region is located at 12 to 14 upstream of the AUG translation initiation site of the sperm nucleus-specific exon and lacks a TATA box. Two minor TATA-less transcription initiation sites are located at around -30 and -45. We have shown by in situ hybridisation that snGPx expression in testis, like protamine expression, is restricted to late stages of spermatogenesis whereas PHGPx expression is only found in spermatocytes and early spermatids. These findings have to be taken into account when studying either the differential regulation of PHGPx and snGPx expression in testis or the impact of putative mutations in snGPx on male fertility in man.

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Published Online: 2005-06-01
Published in Print: 2003-04-10

Copyright © 2003 by Walter de Gruyter GmbH & Co. KG

Artikel in diesem Heft

  1. Glutathione, Related Enzymology, and Leopold Flohé
  2. 'Lest I Forget Thee, Glutathione...'
  3. Glutathione Pathways in the Brain
  4. The Role of Glutathione Peroxidases in Trypanosomatids
  5. Cytoprotection against Oxidative Stress and the Regulation of Glutathione Synthesis
  6. The Parasite-Specific Trypanothione Metabolism of Trypanosoma and Leishmania
  7. Glutathione – Functions and Metabolism in the Malarial Parasite Plasmodium falciparum
  8. Oxidative Stress Caused by Inactivation of Glutathione Peroxidase and Adaptive Responses
  9. Versatility of Selenium Catalysis in PHGPx Unraveled by LC/ESI-MS/MS
  10. Modulation of the Chymotrypsin-Like Activity of the 20S Proteasome by Intracellular Redox Status: Effects of Glutathione Peroxidase-1 Overexpression and Antioxidant Drugs
  11. Microflora Trigger Colitis in Mice Deficient in Selenium-Dependent Glutathione Peroxidase and Induce Gpx2 Gene Expression
  12. Recruitment of the Interleukin-1 Receptor (IL-1RI)-Associated Kinase IRAK to the IL-1RI Is Redox Regulated
  13. Kinetics and Redox-Sensitive Oligomerisation Reveal Negative Subunit Cooperativity in Tryparedoxin Peroxidase of Trypanosoma brucei brucei
  14. Testis-Specific Expression of the Nuclear Form of Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx)
  15. Selective Recognition of Peptide Sequences by Glutathione Transferases: A Possible Mechanism for Modulation of Cellular Stress-Induced Signaling Pathways
  16. Biosynthesis of Trypanothione in Trypanosoma brucei brucei
  17. Transcriptional Regulation of Cytosol and Membrane Alanyl-Aminopeptidase in Human T Cell Subsets
  18. Regulation of Gene Transcription by a Constitutively Active Mutant of Activating Transcription Factor 2 (ATF2)
  19. Solvent Isotope Effect on the Reaction Catalysed by the Pyruvate Dehydrogenase Complex from Escherichia coli
  20. Selective Induction of Liver Parenchymal Cell Heme Oxygenase-1 in Selenium-Deficient Rats
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