Phospholipid Hydroperoxide Glutathione Peroxidase Is The Major Selenoperoxidase In Nuclei and Mitochondria Of Rat Testis

Abstract

This paper reports the identification of the selenoenzyme Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPX) in rat testis. PHGPX specific activity in the testis was the highest so far measured in mammalian tissues, and the activity distribution pattern was just the opposite of that found in the liver. In fact, while liver PHGPX is essentially a soluble cytosolic protein, in the testis, the highest specific activity was detected in the nuclear and mitochondrial membranes. The identity of PHGPX with the previously-described 15-20 Kd selenoprotein (Wallace et al., 1983), involved in the maturation of spermatozoa, is proposed. The observation that PHGPX is the preponderant selenoprotein in rat testis throws some light on the complex relationship between selenium and spermatogenesis, and suggests that the effects of selenium deficiency may reasonably be produced by the absence of this enzyme.