Dual function of the selenoprotein PHGPx during sperm maturation
F Ursini, S Heim, M Kiess, M Maiorino, A Roveri… - Science, 1999 - science.org
F Ursini, S Heim, M Kiess, M Maiorino, A Roveri, J Wissing, L Flohé
Science, 1999•science.orgThe 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 …
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 …
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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