Abstract
An epididymis-specific, secretory glutathione peroxidase (GPX5) has been proposed previously to play a role in protecting mammalian sperm membranes from the deleterious effects of lipid peroxidation, which, if not contained, can lead to reduced fertilizing capacity. Here we report the cDNA cloning of human GPX5 and show that the majority of transcripts contain a 118 nt frame-shifting deletion, arising, most likely, from inappropriate excision of exon 3 during processing. Antisera raised against recombinant human GPX5 cross-reacted with rat and macaque (Macaca fascicularis) epididymal proteins of the size expected for full-length, active GPX5. However, no similar reactivity could be demonstrated in any of the human samples tested.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ATP-Binding Cassette Transporters*
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Adult
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Aged
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Amino Acid Sequence
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Animals
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Base Sequence
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Blotting, Western
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Carrier Proteins / genetics
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Cloning, Molecular
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DNA, Complementary / genetics
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Epididymis / enzymology
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Escherichia coli Proteins*
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Glutathione Peroxidase / biosynthesis
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Glutathione Peroxidase / genetics*
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Glutathione Peroxidase / immunology
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Humans
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Immune Sera / immunology
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Isoenzymes / biosynthesis
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Isoenzymes / genetics*
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Isoenzymes / immunology
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Macaca fascicularis
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Male
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Maltose-Binding Proteins
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Middle Aged
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Molecular Sequence Data
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Monosaccharide Transport Proteins*
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Periplasmic Binding Proteins*
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Polymerase Chain Reaction
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RNA Splicing*
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Rats
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / immunology
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Sequence Alignment
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Testis / enzymology*
Substances
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ATP-Binding Cassette Transporters
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Carrier Proteins
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DNA, Complementary
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Escherichia coli Proteins
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Immune Sera
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Isoenzymes
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MalE protein, E coli
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Maltose-Binding Proteins
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Monosaccharide Transport Proteins
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Periplasmic Binding Proteins
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Recombinant Fusion Proteins
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maltose transport system, E coli
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Glutathione Peroxidase
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selenium-independent glutathione peroxidase