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• W2000948604 abstract "Peroxiredoxins (Prxs) are a group of thiol containing proteins that participate both in signal transduction and in the breakdown of hydrogen peroxide (H 2 O 2 ) 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 H 2 O 2 , 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 2 O 2 caused a minor increase (<28%, 4 h) in the expression of Prxs I, IV, and VI. Severe oxidant stress (250–500 μM H 2 O 2 ) caused a significant increase in the proportion of the monomeric forms of Prxs I–IV; this was reversible at lower H 2 O 2 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 proteins during severe oxidant exposure." @default.
• W2000948604 created "2016-06-24" @default.
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• W2000948604 date "2005-05-01" @default.
• W2000948604 modified "2023-10-12" @default.
• W2000948604 title "Variable overoxidation of peroxiredoxins in human lung cells in severe oxidative stress" @default.
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• W2000948604 doi "https://doi.org/10.1152/ajplung.00432.2004" @default.
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