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.
Pubmed ID: 10464096 RIS Download
Mesh terms: Animals | Electrophoresis, Gel, Two-Dimensional | Electrophoresis, Polyacrylamide Gel | Glutathione Peroxidase | Infertility, Male | Male | Mitochondria | Oxidation-Reduction | Proteins | Rats | Rats, Wistar | Selenium | Selenoproteins | Solubility | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Spermatids | Spermatogenesis | Spermatozoa
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