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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence / physiology
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Apoptosis / physiology*
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Cells, Cultured
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Cysteine / metabolism*
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Down-Regulation / drug effects
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Down-Regulation / physiology
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Endothelium / cytology
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Endothelium / enzymology*
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Enzyme Inhibitors / pharmacology
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Free Radical Scavengers / metabolism
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Gene Expression Regulation, Enzymologic / physiology
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Genetic Vectors / genetics
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Humans
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Mutation / genetics
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Nitric Oxide / biosynthesis*
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Nitric Oxide Synthase / antagonists & inhibitors
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Nitric Oxide Synthase / metabolism
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Nitrogen Compounds / metabolism
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Oxidation-Reduction
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Reactive Oxygen Species / metabolism
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Sulfur / metabolism
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Thioredoxins / genetics
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Thioredoxins / metabolism*
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Tumor Necrosis Factor-alpha / antagonists & inhibitors
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Tumor Necrosis Factor-alpha / metabolism
Substances
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Enzyme Inhibitors
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Free Radical Scavengers
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Nitrogen Compounds
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Reactive Oxygen Species
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Tumor Necrosis Factor-alpha
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Nitric Oxide
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Thioredoxins
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Sulfur
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Nitric Oxide Synthase
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Cysteine