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Related Experiment Videos

PHGPx and spermatogenesis.

A Roveri1, F Ursini, L Flohé

  • 1Department of Biological Chemistry, University of Padova, Viale G. Colombo 3, I-35121 Padova, Italy.

Biofactors (Oxford, England)
|September 25, 2001
PubMed
Summary

Phospholipid hydroperoxide glutathione peroxidase (PHGPx) cross-links proteins in rat sperm capsules, inactivating the enzyme. This activity, dependent on selenium, is crucial for sperm development and function.

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Area of Science:

  • Biochemistry
  • Reproductive Biology
  • Enzymology

Background:

  • Phospholipid hydroperoxide glutathione peroxidase (PHGPx) is essential for spermatogenesis.
  • PHGPx in the rat sperm mitochondrial capsule is cross-linked and inactive, but can be partially released in an active form.

Purpose of the Study:

  • To investigate the role of PHGPx activity in cross-linking proteins within the mammalian sperm capsule.
  • To elucidate the mechanism of PHGPx inactivation and cross-linking.

Main Methods:

  • Treatment of reduced and solubilized capsule proteins with hydrogen peroxide (H2O2).
  • Monitoring H2O2 consumption and protein thiol oxidation.
  • SDS-PAGE analysis of monobromobimane-labeled proteins to identify cross-linked bands.

Main Results:

  • H2O2 consumption was dependent on both PHGPx activity and protein thiols.
  • Protein thiols were oxidized with a stoichiometry of 2 thiol equivalents per mole of hydroperoxide.
  • PHGPx was inactivated and cross-linked, with oxidation occurring in specific ~20 kDa protein bands.

Conclusions:

  • The protein thiol peroxidase activity of PHGPx is responsible for cross-linking proteins in the mammalian sperm capsule.
  • This cross-linking mechanism explains the selenium dependency of spermatogenesis.

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