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Maiorino, M. et al.

Maiorino, Mauri, Roveri, Benazzi, Toppo, Bosello, Ursini,

Primary structure of the nuclear forms of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat spermatozoa.

Phospholipid hydroperoxide glutathione peroxidase is a monomeric Se-peroxidase highly expressed in mammalian male germ cells. Its nuclear form, sperm nuclei glutathione peroxidase (snGPx), has been originally identified in maturating spermatozoa as a transcription product containing an alternative exon within the phospholipid hydroperoxide glutathione peroxidase gene. In this paper, we show that this form is inconstantly detectable in rat spermatozoa where a 20.0 and 25.9 kDa major forms are detected instead. These have been conclusively characterized. The N-terminus sequence of the 20.0 kDa form confirmed that the protein is identical to cytosolic form, suggesting diffusion into the nucleus. The 25.9 kDa protein represented a truncated form of the previously described nuclear snGPx, lacking the basic nuclear localization signal. This protein is present in two forms differing from each other by the presence of an N-terminal methionine. The presence of traces of the larger snGPx form suggests that exhaustive proteolytic processing of the precursor produces the 25.9 kDa enzyme, although the alternate use of a downstream ATG, at least in rodents, could not be unequivocally ruled out.[1]

References

Primary structure of the nuclear forms of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat spermatozoa. Maiorino, M., Mauri, P., Roveri, A., Benazzi, L., Toppo, S., Bosello, V., Ursini, F. FEBS Lett. (2005) [Pubmed]

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