Original ContributionCatalytic activity of selenomethionine in removing amino acid, peptide, and protein hydroperoxides
Graphical abstract
Highlights
► Peptide and protein hydroperoxides are key intermediates in protein oxidation. ► These peroxides are poorly detoxified by classical peroxidases and protective enzymes. ► Selenomethionine reacts stoichiometrically with hydroperoxides to give a selenoxide ► The selenoxide is re-reduced by GSH or thioredoxin reductase/thioredoxin /NADPH. ► Cells supplemented with selenomethionine have greater peroxide reduction capacity.
Section snippets
Materials
SeMet, Met, GSH, l-ascorbic acid, bovine lactalbumin, and soybean trypsin inhibitor were obtained from Sigma–Aldrich (Australia). N-Ac-Trp-OMe, Gly-His-Gly, and Gly-Tyr-Gly were from Bachem (Bubendorf, Switzerland). H2O2, bovine serum albumin (BSA; Cohn faction V, essentially fatty acid free), and NADPH were obtained from Roche (Castle Hill, Australia). Escherichia coli Trx and TrxR, and rat recombinant TrxR, were obtained from IMCO Corp. (Stockholm, Sweden). Blood was obtained from multiple
SeMet reduces H2O2 and amino acid, peptide, and protein hydroperoxides in a dose- and time-dependent manner
Incubation of H2O2 or hydroperoxides present on N-Ac-Trp-OMe, Gly-His-Gly, Gly-Tyr-Gly, or BSA with varying molar excesses of SeMet for 3 min at 22 °C resulted in a significant loss of hydroperoxides (Fig. 1). The extent of hydroperoxide loss was markedly affected by the structure of these species, with the overall order of reactivity being Gly-His-Gly hydroperoxides > Gly-Tyr-Gly hydroperoxides ≥ N-Ac-Trp-OMe hydroperoxides > BSA hydroperoxides > H2O2. The extent of hydroperoxide removal was
Discussion
Selenium is an essential micronutrient, with a deficiency in this element reported to increase the sensitivity of tissues and cells to oxidative damage [26]. One major mechanism through which selenium may afford protection is via up-regulation of the expression and activity of seleno-antioxidants such as glutathione peroxidase and thioredoxin reductase [13], [14], [27]. Both sodium selenite and SeMet have been widely used in in vitro and animal studies to assess the antioxidant benefit of
Acknowledgments
The authors are grateful to Dr. Philip E. Morgan for assistance with the HPLC experiments in this study. This work was supported financially by the Australian Research Council, through the Centres of Excellence (CE0561607) and Discovery (DP0988311) Programs, and the National Heart Foundation (Grant in Aid: G09S4313).
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