Medical Journals

Sperm Nuclei Glutathione Peroxidases and Their Occurrence in Animal Species with Cysteine-containing Protamines.

Authors:
  • Bertelsmann Holger
  • Kuehbacher Markus
  • Weseloh Gundolf
  • Kyriakopoulos Antonios
  • Behne Dietrich

From: Hahn-Meitner-Institut Berlin, Department Molecular Trace Element Research in the Life Sciences, Glienickerstr.100, 14109 Berlin, Germany. bertelsmann@hmi.de

Biochimica et biophysica acta

  • Publish Date: Oct 2007
  • ISSN: 0006-3002
  • Volume: 1770
  • Issue: 10
  • Pages: 1459-67
  • Medium: Print
  • Language: English
  • Citation (JAMA): Bertelsmann Holger, Kuehbacher Markus, Weseloh Gundolf, et al. Sperm Nuclei Glutathione Peroxidases and Their Occurrence in Animal Species with Cysteine-containing Protamines.. Biochim. Biophys. Acta Oct 2007;1770:1459-67

Abstract

The selenoenzyme sperm nuclei glutathione peroxidase (snGPx), also called the nuclear form of phospholipid hydroperoxide glutathione peroxidase (n-PHGPx), was found to be involved in the stabilization of condensed sperm chromatin, most likely by thiol to disulfide oxidation of the cysteine residues of the mammalian protamines, small nuclear basic proteins in the nuclei of sperm cells. By applying Acidic Urea-PAGE in combination with SDS-PAGE, snGPx with an apparent molecular mass of 34 kDa and a 24-kDa protein were purified from rat sperm nuclei. The 24-kDa protein was identified by means of mass spectrometry as a truncated form of snGPx produced by cleavage at the N-terminal end. After defined processing of spermatozoa and detergent treatment of the sperm nuclei fraction, snGPx and its truncated form were shown to be the only selenoproteins present in mature mammalian sperm nuclei. Both forms were found in mature rat and horse sperm nuclei but in man only snGPx was detected. In trout and chicken, species with sperm cells which likewise undergo chromatin condensation but do not contain cysteine in their protamines, the snGPx proteins were missing. This can be taken as an indirect proof of the function of snGPx to act as protamine cysteine thiol peroxidase in the mammalian species with cysteine-containing protamines.

Mesh Headings (Keywords): Animals, Cell Nucleus, Chickens, Cysteine, Electrophoresis, Polyacrylamide Gel, Glutathione Peroxidase, Horses, Humans, Male, Oncorhynchus mykiss, Protamines, Selenium, Selenoproteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spermatozoa


Check for Full Text / PubMed Unique Identifier (PMID): 17714875


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