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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Electrophoresis, Gel, Two-Dimensional
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Electrophoresis, Polyacrylamide Gel
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Glutathione Peroxidase / chemistry
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Glutathione Peroxidase / isolation & purification
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Glutathione Peroxidase / physiology*
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Infertility, Male / metabolism
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Male
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Mitochondria / chemistry
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Mitochondria / enzymology
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Oxidation-Reduction
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Phospholipid Hydroperoxide Glutathione Peroxidase
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Proteins / chemistry
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Proteins / isolation & purification
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Proteins / physiology*
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Rats
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Rats, Wistar
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Selenium / deficiency
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Selenium / physiology*
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Selenoproteins
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Solubility
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Spermatids / chemistry
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Spermatids / enzymology
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Spermatogenesis*
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Spermatozoa / chemistry
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Spermatozoa / enzymology
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Spermatozoa / physiology*
Substances
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Proteins
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Selenoproteins
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Phospholipid Hydroperoxide Glutathione Peroxidase
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Glutathione Peroxidase
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Selenium