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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.

biochemical journal

The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract