Assessment of redox changes to hydrogen peroxide-sensitive proteins during EGF signaling.
Hydrogen peroxide acts as a second messenger in growth factor signaling where it can oxidize and modify the function of redox-sensitive proteins. While selective thiol oxidation has been measured, there has been no global assessment of protein oxidation following growth factor activation. Significant changes to the abundant and widely distributed redox sensitive thiol proteins were observed in A431 epidermoid carcinoma cells exposed to hydrogen peroxide, but no changes were observed following treatment with epidermal growth factor (EGF). This included members of the peroxiredoxin family, which were also monitored in the presence of the thioredoxin reductase inhibitor auranofin to limit their capacity to recycle to the reduced form. We conclude that widespread thiol oxidation does not occur in cells during EGF signaling, and that hydrogen peroxide must act in a highly localized or selective manner.
Free Radical Research Group, National Research Centre for Growth and Development, Department of Pathology, University of Otago, Christchurch, New Zealand.
Sarah L
SL
Cuddihy
Christine C
CC
Winterbourn
Mark B
MB
Hampton
D015153:Blotting, Western; D045744:Cell Line, Tumor; D015180:Electrophoresis, Gel, Two-Dimensional; D004815:Epidermal Growth Factor / Q000494:pharmacology*; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D010084:Oxidation-Reduction / Q000187:drug effects*; D054464:Peroxiredoxins / Q000378:metabolism; D013879:Thioredoxins / Q000378:metabolism
D013879:Thioredoxins; D004815:Epidermal Growth Factor; D006861:Hydrogen Peroxide; D054464:Peroxiredoxins