Phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis nuclei is bound to chromatin

Cristiana Godeas, Federica Tramer, Fulvio Micali, Antonella Roveri, Matilde Maiorino, Carla Nisii, Gabriella Sandri, Enrico Panfili

Research output: Contribution to journalArticlepeer-review


In rat testis nuclei the activity of the selenoenzyme phospholipid hydroperoxide glutathione peroxidase (PHGPx, EC is much higher than in other tissues and subcellular compartments, with the sole exception of mitochondria. In nuclei, the bound enzyme is solubilized by DNase I treatment, thus suggesting a binding to chromatin. Treatment with ionic strength releases about 70% of bound PHGPx, suggesting that electrostatic bonds are involved. Immunogold electron microscopy indicates the association of PHGPx with chromatin structures in isolated nuclei. A possible interpretation of these data is a PHGPx protective role against DNA peroxidative damage. Furthermore, in agreement with kinetic and structural information, PHGPx-chromatin binding could suggest an hypothetical thiol oxidase activity toward specific thiol bearing proteins which could substitute for GSH as alternative donor substrates. Such activity could give to the enzyme a new important function which is not only protective but also has a specific regulatory function in chromatin condensation.

Original languageEnglish
Pages (from-to)118-124
Number of pages7
JournalBiochemical and Molecular Medicine
Issue number2
Publication statusPublished - Dec 1996

ASJC Scopus subject areas

  • Biochemistry


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