Peroxiredoxins (Prxs) are a group of thiol containing proteins that participate both in signal transduction and in the breakdown of hydrogen peroxide (H2O2) during oxidative stress. Six distinct Prxs have been characterized in human cells (Prxs I-VI). Prxs I-IV form dimers held together by disulfide bonds, Prx V forms intramolecular bond, but the mechanism of Prx VI, so-called 1-Cys Prx, is still unclear. Here we describe the regulation of all six Prxs in cultured human lung A549 and BEAS-2B cells. The cells were exposed to variable concentrations of H2O2, menadione, tumor necrosis factor-α or transforming growth factor-β. To evoke glutathione depletion, the cells were furthermore treated with buthionine sulfoximine. Only high concentrations (300 μM) of H 2O2 caused a minor increase (<28%, 4 h) in the expression of Prxs I, IV, and VI. Severe oxidant stress (250-500 μM H 2O2) caused a significant increase in the proportion of the monomeric forms of Prxs I-IV; this was reversible at lower H 2O2 concentrations (≤250 μM). This recovery of Prx overoxidation differed among the various Prxs; Prx I was recovered within 24 h, but recovery required 48 h for Prx III. Overall, Prxs are not significantly modulated by mild oxidant stress or cytokines, but there is variable, though reversible, overoxidation in these nroteins durine severe oxidant exposure.
|Journal||American Journal of Physiology - Lung Cellular and Molecular Physiology|
|Issue number||5 32-5|
|State||Published - May 2005|
- Hydrogen peroxide