Metamorphosis of the selenoprotein PHGPx during spermatogenesis

The selenoprotein phospholipid hydroperoxide glutathione peroxidase in spermatogenic cells and spermatozoa accounts for almost the entire selenium content of mammal testis. A particular relevance of PHGPx to male fertility was first suggested by gonadotropin-dependent synthesis in rat testis and further corroborated by in situ hybridazation studies demostrating abundant expression in round spermatids. In testicular tissue, PHGPx, by alternate use of initiation codons, is targeted either to mitochondria or to the cytosol. Also, alternate splicing of the pre mRNA directs part of the PHGPx to the nucleus