Male Fertility Is Linked to the Selenoprotein Phospholipid Hydroperoxide Glutathione Peroxidase1

@inproceedings{Foresta2002MaleFI,
  title={Male Fertility Is Linked to the Selenoprotein Phospholipid Hydroperoxide Glutathione Peroxidase1},
  author={Carlo Foresta and Leopold Floh{\'e} and Andrea Garolla and Antonella Roveri and Fulvio Ursini and Matilde Maiorino},
  booktitle={Biology of reproduction},
  year={2002}
}
Abstract The selenoprotein phospholipid hydroperoxide glutathione peroxidase (PHGPx) accounts for almost the entire selenium content of mammalian testis. PHGPx is abundantly expressed in spermatids as active peroxidase but is transformed to an oxidatively inactivated protein in mature sperm, where it is a major constituent of the mitochondrial capsule in the midpiece. Male infertility in selenium-deficient animals, which is characterized by impaired sperm motility and morphological midpiece… 
Selenium in mammalian spermiogenesis
TLDR
Circumstantial evidence and ongoing experimental genetics indicate that the mitochondrially expressed form of the GPx4 gene is the most relevant one in spermiogenesis, with the nuclear form being dispensable for fertility and the role of cytosolic GPx 4 remaining unclear.
Immunocytochemical Localisation of Phospholipid Hydroperoxide Glutathione Peroxidase in Bull’s Spermatogenic Cells
TLDR
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Selenium, a key element in spermatogenesis and male fertility.
TLDR
Clinical data have pointed to a correlation between abnormal PHGPx content in sperm and disturbance of human male fertility, however, additional evidence is still required to draw any definitive conclusions about therapeutical strategies for improving fertility by selenium administration.
Failure of phospholipid hydroperoxide glutathione peroxidase expression in oligoasthenozoospermia and mutations in the PHGPx gene
TLDR
It can be concluded that oligoasthenozoospermia is associated with a decrease in the level of expression of PHGPx in the spermatozoa of some infertile men, but is not linked to mutations inPHGPx gene.
Selenoprotein P in seminal fluid is a novel biomarker of sperm quality.
Depletion of Selenoprotein GPx4 in Spermatocytes Causes Male Infertility in Mice*
TLDR
It is demonstrated that the depletion of GPx4 in spermatocytes causes severe abnormalities in spermatozoa, which may be one of the causes of male infertility in mice and humans.
Genetic Variations of gpx-4 and Male Infertility in Humans1
TLDR
The results indicate that gpx-4 polymorphism cannot generally account for the correlation of PHGPx content of sperm and fertility-related parameters, but further examination of this gene as a potential cause of infertility in particular cases is warranted.
Phospholipid hydroperoxide glutathione peroxidase: expression pattern during testicular development in mouse and evolutionary conservation in spermatozoa
TLDR
Results indicate a conserved crucial role of PHGPx during sperm function and male fertility.
Peroxiredoxin 6: The Protector of Male Fertility
TLDR
The role of PRDX6 is focused on as the primary antioxidant enzyme that protects the spermatozoon from oxidative-stress-associated damages to protect the paternal genome and assure fertility.
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References

SHOWING 1-10 OF 30 REFERENCES
Failure of the Expression of Phospholipid Hydroperoxide Glutathione Peroxidase in the Spermatozoa of Human Infertile Males1
TLDR
The results suggest that failure of the expression of mitochondrial PHGPx in spermatozoa might be one of the causes of oligoasthenozoospermia in infertile men.
Dual function of the selenoprotein PHGPx during sperm maturation.
TLDR
The role of PHGPx as a structural protein may explain the mechanical instability of the mitochondrial midpiece that is observed in selenium deficiency.
Phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis nuclei is bound to chromatin.
TLDR
In rat testis nuclei the activity of the selenoenzyme phospholipid hydroperoxide glutathione peroxidase (PHGPx) is much higher than in other tissues and subcellular compartments, with the sole exception of mitochondria, thus suggesting a binding to chromatin.
Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross‐linking during sperm maturation
  • H. Pfeifer, M. Conrad, D. Behne
  • Biology, Chemistry
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2001
TLDR
Evidence is provided that snGPx acts as a protamine thiol peroxidase responsible for disulfide cross‐linking by reduction of reactive oxygen species and its dual function in chromatin condensation and the protection of sperm DNA against oxidation is necessary to ensure male fertility and sperm quality.
Rat Phospholipid-hydroperoxide Glutathione Peroxidase
TLDR
The results suggest that the use of alternative transcription and translation start sites determines the subcellular localization of PhGPx in different tissues.
Testosterone mediates expression of the selenoprotein PHGPx by induction of spermatogenesis and not by direct transcriptional gene activation
  • M. Maiorino, J. Wissing, L. Flohé
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1998
TLDR
The data show that the age or gonadotropin‐dependent expression of PHGPx in testis does not result from direct transcriptional gene activation by testosterone, but is due to differentiation stage‐specific expression in late spermatids, which are under the control of Leydig cell‐derived testosterone.
Selenoenzymes regulate the activity of leukocyte 5-lipoxygenase via the peroxide tone.
Phospholipid hydroperoxide glutathione peroxidase.
TLDR
The kinetic comparison betweenPHGPX and GPX in the presence of different substrates and detergents indicates that, while GPX is more active on soluble hydrophilic substrates, PHGPX isMore active on the hydroperoxides in the membranes.
Expression pattern of phospholipid hydroperoxide glutathione peroxidase messenger ribonucleic acid in mouse testis.
TLDR
Findings suggest that PHGPx in testes may be closely involved in spermatogenesis as well as having a general antioxidant function.
Developmental expression, intracellular localization, and selenium content of the cysteine‐rich protein associated with the mitochondrial capsules of mouse sperm
TLDR
The experiments in the present study were designed to resolve a controversy surrounding the intracellular localization, developmental expression, and selenium‐content of a cysteine‐rich 17–20 kD protein that has been reported to constitute the major structural protein in the mitochondrial capsule of mammals.
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