Journal
FREE RADICAL RESEARCH
Volume 48, Issue 9, Pages 996-1010Publisher
TAYLOR & FRANCIS LTD
DOI: 10.3109/10715762.2014.942842
Keywords
nitrosylation; nitric oxide; superoxide; hydrogen peroxide; peroxinitrite; redox signaling
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Funding
- National Medical Research council of Singapore [NMRC/1196/2008]
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In the present study, the formation of whole cellular S-nitrosylated proteins (protein-SNOs) by the reactive oxygen species (ROS), hydrogen peroxide (H2O2), and superoxide (O-2(center dot-)) is demonstrated. A spectrum of protein cysteine oxidative modifications was detected upon incubation of serum-starved mouse embryonic fibroblasts with increasing concentrations of exogenous H2O2, ranging from exclusive protein-SNOs at low concentrations to a mixture of protein-SNOs and other protein oxidation at higher concentrations to exclusively non-SNO protein oxidation at the highest concentrations of the oxidant used. Furthermore, formation of protein-SNOs was also detected upon inhibition of the antioxidant protein Cu/Zn superoxide dismutase that results in an increase in intracellular concentration of O-2(center dot-). These results were further validated using the phosphatase and tensin homologue, PTEN, as a model of a protein sensitive to oxidative modifications. The formation of protein-SNOs by H2O2 and O-2(center dot-) was prevented by the NO scavenger, c-PTIO, as well as the peroxinitrite decomposition catalyst, FETPPS, and correlated with the production or the consumption of nitric oxide (NO), respectively. These data suggest that the formation of protein-SNOs by H2O2 or O-2(center dot-) requires the presence or the production of NO and involves the formation of the nitrosylating intermediate, peroxinitrite.
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