Mitochondrial peroxiredoxin 3 is rapidly oxidized in cells treated with isothiocyanates

In this study we investigated the effect of several different isothiocyanates on the redox states of the cysteine-dependent peroxiredoxins in Jurkat T lymphoma cells, and compared this to known effects on the selenoprotein thioredoxin reductase, glutathione reductase and intracellular GSH levels

Kristin K. Brown; Sofi E. Eriksson; Elias S.J. Arnér; Mark B. Hampton

2008

Scholarcy highlights

  • Isothiocyanates are phytochemicals with anti-cancer properties that include the ability to trigger apoptosis
  • A substantial body of evidence suggests that reaction of the electrophilic isothiocyanate moiety with cysteine residues in cellular proteins and glutathione accounts for their biological activity
  • In this study we investigated the effect of several different isothiocyanates on the redox states of the cysteine-dependent peroxiredoxins in Jurkat T lymphoma cells, and compared this to known effects on the selenoprotein thioredoxin reductase, glutathione reductase and intracellular GSH levels
  • Oxidation of mitochondrial Prx could be detected as early as 5 min after exposure of cells to phenethyl isothiocyanate, with complete oxidation occurring at doses that only had small inhibitory effects on total cellular thioredoxin reductase and glutathione reductase activities
  • Peroxiredoxin oxidation was specific to the mitochondrial isoform with cytoplasmic Prx and Prx maintained in their reduced forms at all analyzed time points and concentrations of isothiocyanate
  • We propose that pro-apoptotic isothiocyanates selectively disrupt mitochondrial redox homeostasis, as indicated by Prx oxidation, and that this contributes to their pro-apoptotic activity

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