Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-09-16

AUTHORS

Judith Haendeler, Jörg Hoffmann, Verena Tischler, Bradford C. Berk, Andreas M. Zeiher, Stefanie Dimmeler

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. More... »

PAGES

743-749

References to SciGraph publications

  • 2001-02. Export by red blood cells of nitric oxide bioactivity in NATURE
  • 2001-01-19. Protein S-nitrosylation: a physiological signal for neuronal nitric oxide in NATURE CELL BIOLOGY
  • 1998-04. Oxidative modifications in nitrosative stress in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 1997-07. S-nitrosylation regulates apoptosis in NATURE
  • 1999-10-20. Nitric oxide–an endothelial cell survival factor in CELL DEATH & DIFFERENTIATION
  • 1999-10-20. NO: an inhibitor of cell death in CELL DEATH & DIFFERENTIATION
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ncb851

    DOI

    http://dx.doi.org/10.1038/ncb851

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1022075458

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/12244325


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