Abstract
Thioredoxin 1 (Trx) is a known redox regulator that is implicated in the redox control of cell growth and apoptosis inhibition. Here we show that Trx is essential for maintaining the content of S-nitrosylated molecules in endothelial cells. Trx itself is S-nitrosylated at cysteine 69 under basal conditions, and this S-nitrosylation is required for scavenging reactive oxygen species and for preserving the redox regulatory activity of Trx. S-nitrosylation of Trx also contributes to the anti-apoptotic function of Trx. Thus, Trx can exert its complete redox regulatory and anti-apoptotic functions in endothelial cells only when cysteine 69 is S-nitrosylated.
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Acknowledgements
We thank C. Goy for technical assistance. This work was supported by a grant to S.D. from the Deutsche Forschungsgesellschaft, Sonderforschungsbereich. J. Haendeler was supported by a grant from the Deutsche Forschungsgesellschaft. J. Hoffmann was supported by a stipendium from Boehringer Ingelheim Fonds.
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Haendeler, J., Hoffmann, J., Tischler, V. et al. Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat Cell Biol 4, 743–749 (2002). https://doi.org/10.1038/ncb851
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DOI: https://doi.org/10.1038/ncb851
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