Dual Function of the Selenoprotein PHGPx During Sperm Maturation

Fulvio Ursini(University of Padua), Sabina Heim(Helmholtz Centre for Infection Research), Michael Kieß(Helmholtz Centre for Infection Research), Matilde Maiorino(University of Padua), Antonella Roveri(University of Padua), Josef Wissing(Helmholtz Centre for Infection Research), Leopold Flohé(Technische Universität Braunschweig)
Science
August 27, 1999
Cited by 903

Abstract

The selenoprotein phospholipid hydroperoxide glutathione peroxidase (PHGPx) changes its physical characteristics and biological functions during sperm maturation. PHGPx exists as a soluble peroxidase in spermatids but persists in mature spermatozoa as an enzymatically inactive, oxidatively cross-linked, insoluble protein. In the midpiece of mature spermatozoa, PHGPx protein represents at least 50 percent of the capsule material that embeds the helix of mitochondria. The role of PHGPx as a structural protein may explain the mechanical instability of the mitochondrial midpiece that is observed in selenium deficiency.


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