Article abstract
Nature Cell Biology 4, 743 - 749 (2002)
Published online: 16 September 2002 | doi:10.1038/ncb851
There is an Erratum (March 2003) associated with this Article.
Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
Judith Haendeler1, Jörg Hoffmann1, Verena Tischler1, Bradford C. Berk2, Andreas M. Zeiher1 & Stefanie Dimmeler1
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.
- Molecular Cardiology, Department of Internal Medicine IV, University of Frankfurt, Theodor-Stern-Kai 7, 60590 Frankfurt, Germany
- Center for Cardiovascular Research, University of Rochester, 601 Elmwood Ave, Box 679, Rochester, New York, 14642, USA
Correspondence to: Stefanie Dimmeler1 e-mail: Dimmeler@em.uni-frankfurt.de
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