Mitochondrial respiratory chain involvement in peroxiredoxin 3 oxidation by phenethyl isothiocyanate and auranofin |
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Authors: | Kristin K. Brown Mark B. Hampton |
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Affiliation: | Free Radical Research Group and National Research Centre for Growth and Development, Department of Pathology, University of Otago, Christchurch, New Zealand |
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Abstract: | Mitochondrial peroxiredoxin 3 (Prx 3) is rapidly oxidized in cells exposed to phenethyl isothiocyanate (PEITC) and auranofin (AFN), but the mechanism of oxidation is unclear. Using HL-60 cells deplete of mitochondrial DNA we show that peroxiredoxin 3 oxidation and cytotoxicity requires a functional respiratory chain. Thioredoxin reductase (TrxR) could be inhibited by up to 90% by auranofin without direct oxidation of peroxiredoxin 3. However, inhibition of thioredoxin reductase promoted peroxiredoxin 3 oxidation and cytotoxicity in combination with phenethyl isothiocyanate or antimycin A. We conclude that rapid peroxiredoxin 3 oxidation occurs as a consequence of increased oxidant production from the mitochondrial respiratory chain. |
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Keywords: | AFN, auranofin NEM, N-ethylmaleimide PEITC, phenethyl isothiocyanate Prx, peroxiredoxin ρ0, mitochondrial DNA deplete TrxR, thioredoxin reductase |
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