The role of thioredoxin in the regulation of cellular processes by S-nitrosylation

S-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of S-nitrosothiols (R-S-N=O or RSNO), has emerged as an important feature of NO biology and pathobiology. Many NO-related biological functions have been directly ass...

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Published inBiochimica et biophysica acta Vol. 1820; no. 6; pp. 689 - 700
Main Authors Sengupta, Rajib, Holmgren, Arne
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.06.2012
Subjects
Animals
biochemical pathways
caspase-3
Cell Physiological Phenomena
cysteine
Cysteine - metabolism
glutathione
Glutathione - metabolism
homeostasis
mammals
Nitric oxide
Nitric Oxide - metabolism
Nitrosation
Oxidation-Reduction
Oxidative Stress
proteins
Proteins - metabolism
Redox regulation
S-Nitrosoglutathione - metabolism
S-Nitrosothiols - metabolism
S-nitrosylation
Selenocysteine - metabolism
Signal Transduction
Thiol
thiols
Thioredoxin
Thioredoxin reductase
Thioredoxin-Disulfide Reductase - chemistry
Thioredoxin-Disulfide Reductase - metabolism
Thioredoxins - chemistry
Thioredoxins - metabolism
Thiol
Thioredoxin
Thioredoxin reductase
Nitric oxide
S-nitrosylation
Redox regulation
Online AccessGet full text
ISSN0304-4165
0006-3002
1872-8006
DOI10.1016/j.bbagen.2011.08.012

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Abstract S-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of S-nitrosothiols (R-S-N=O or RSNO), has emerged as an important feature of NO biology and pathobiology. Many NO-related biological functions have been directly associated with the S-nitrosothiols and a considerable number of S-nitrosylated proteins have been identified which can positively or negatively regulate various cellular processes including signaling and metabolic pathways. Taking account of the recent progress in the field of research, this review focuses on the regulation of cellular processes by S-nitrosylation and Trx-mediated cellular homeostasis of S-nitrosothiols. Thioredoxin (Trx) system in mammalian cells utilizes thiol and selenol groups to maintain a reducing intracellular environment to combat oxidative/nitrosative stress. Reduced glutathione (GSH) and Trx system perform the major role in denitrosylation of S-nitrosylated proteins. However, under certain conditions, oxidized form of mammalian Trx can be S-nitrosylated and then it can trans-S-nitrosylate target proteins, such as caspase 3. Investigations on the role of thioredoxin system in relation to biologically relevant RSNOs, their functions, and the mechanisms of S-denitrosylation facilitate the development of drugs and therapies. This article is part of a Special Issue entitled Regulation of Cellular Processes. ► S-nitrosylation is an important feature of NO biology and pathobiology. ► Many S-nitrosylated proteins regulate various cellular processes. ► Thioredoxin system plays an important role to combat oxidative/nitrosative stress. ► GSH and Trx system perform the major role in denitrosylation of RSNOs.
AbstractList S-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of S-nitrosothiols (R-S-N=O or RSNO), has emerged as an important feature of NO biology and pathobiology. Many NO-related biological functions have been directly associated with the S-nitrosothiols and a considerable number of S-nitrosylated proteins have been identified which can positively or negatively regulate various cellular processes including signaling and metabolic pathways. Taking account of the recent progress in the field of research, this review focuses on the regulation of cellular processes by S-nitrosylation and Trx-mediated cellular homeostasis of S-nitrosothiols. Thioredoxin (Trx) system in mammalian cells utilizes thiol and selenol groups to maintain a reducing intracellular environment to combat oxidative/nitrosative stress. Reduced glutathione (GSH) and Trx system perform the major role in denitrosylation of S-nitrosylated proteins. However, under certain conditions, oxidized form of mammalian Trx can be S-nitrosylated and then it can trans-S-nitrosylate target proteins, such as caspase 3. Investigations on the role of thioredoxin system in relation to biologically relevant RSNOs, their functions, and the mechanisms of S-denitrosylation facilitate the development of drugs and therapies. This article is part of a Special Issue entitled Regulation of Cellular Processes.
BACKGROUND: S-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of S-nitrosothiols (R-S-N=O or RSNO), has emerged as an important feature of NO biology and pathobiology. Many NO-related biological functions have been directly associated with the S-nitrosothiols and a considerable number of S-nitrosylated proteins have been identified which can positively or negatively regulate various cellular processes including signaling and metabolic pathways. SCOPE OF THE REVIEW: Taking account of the recent progress in the field of research, this review focuses on the regulation of cellular processes by S-nitrosylation and Trx-mediated cellular homeostasis of S-nitrosothiols. MAJOR CONCLUSIONS: Thioredoxin (Trx) system in mammalian cells utilizes thiol and selenol groups to maintain a reducing intracellular environment to combat oxidative/nitrosative stress. Reduced glutathione (GSH) and Trx system perform the major role in denitrosylation of S-nitrosylated proteins. However, under certain conditions, oxidized form of mammalian Trx can be S-nitrosylated and then it can trans-S-nitrosylate target proteins, such as caspase 3. GENERAL SIGNIFICANCE: Investigations on the role of thioredoxin system in relation to biologically relevant RSNOs, their functions, and the mechanisms of S-denitrosylation facilitate the development of drugs and therapies. This article is part of a Special Issue entitled Regulation of Cellular Processes.
S-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of S-nitrosothiols (R-S-N=O or RSNO), has emerged as an important feature of NO biology and pathobiology. Many NO-related biological functions have been directly associated with the S-nitrosothiols and a considerable number of S-nitrosylated proteins have been identified which can positively or negatively regulate various cellular processes including signaling and metabolic pathways.BACKGROUNDS-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of S-nitrosothiols (R-S-N=O or RSNO), has emerged as an important feature of NO biology and pathobiology. Many NO-related biological functions have been directly associated with the S-nitrosothiols and a considerable number of S-nitrosylated proteins have been identified which can positively or negatively regulate various cellular processes including signaling and metabolic pathways.Taking account of the recent progress in the field of research, this review focuses on the regulation of cellular processes by S-nitrosylation and Trx-mediated cellular homeostasis of S-nitrosothiols.SCOPE OF THE REVIEWTaking account of the recent progress in the field of research, this review focuses on the regulation of cellular processes by S-nitrosylation and Trx-mediated cellular homeostasis of S-nitrosothiols.Thioredoxin (Trx) system in mammalian cells utilizes thiol and selenol groups to maintain a reducing intracellular environment to combat oxidative/nitrosative stress. Reduced glutathione (GSH) and Trx system perform the major role in denitrosylation of S-nitrosylated proteins. However, under certain conditions, oxidized form of mammalian Trx can be S-nitrosylated and then it can trans-S-nitrosylate target proteins, such as caspase 3.MAJOR CONCLUSIONSThioredoxin (Trx) system in mammalian cells utilizes thiol and selenol groups to maintain a reducing intracellular environment to combat oxidative/nitrosative stress. Reduced glutathione (GSH) and Trx system perform the major role in denitrosylation of S-nitrosylated proteins. However, under certain conditions, oxidized form of mammalian Trx can be S-nitrosylated and then it can trans-S-nitrosylate target proteins, such as caspase 3.Investigations on the role of thioredoxin system in relation to biologically relevant RSNOs, their functions, and the mechanisms of S-denitrosylation facilitate the development of drugs and therapies. This article is part of a Special Issue entitled Regulation of Cellular Processes.GENERAL SIGNIFICANCEInvestigations on the role of thioredoxin system in relation to biologically relevant RSNOs, their functions, and the mechanisms of S-denitrosylation facilitate the development of drugs and therapies. This article is part of a Special Issue entitled Regulation of Cellular Processes.
S-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of S-nitrosothiols (R-S-N=O or RSNO), has emerged as an important feature of NO biology and pathobiology. Many NO-related biological functions have been directly associated with the S-nitrosothiols and a considerable number of S-nitrosylated proteins have been identified which can positively or negatively regulate various cellular processes including signaling and metabolic pathways. Taking account of the recent progress in the field of research, this review focuses on the regulation of cellular processes by S-nitrosylation and Trx-mediated cellular homeostasis of S-nitrosothiols. Thioredoxin (Trx) system in mammalian cells utilizes thiol and selenol groups to maintain a reducing intracellular environment to combat oxidative/nitrosative stress. Reduced glutathione (GSH) and Trx system perform the major role in denitrosylation of S-nitrosylated proteins. However, under certain conditions, oxidized form of mammalian Trx can be S-nitrosylated and then it can trans-S-nitrosylate target proteins, such as caspase 3. Investigations on the role of thioredoxin system in relation to biologically relevant RSNOs, their functions, and the mechanisms of S-denitrosylation facilitate the development of drugs and therapies. This article is part of a Special Issue entitled Regulation of Cellular Processes. ► S-nitrosylation is an important feature of NO biology and pathobiology. ► Many S-nitrosylated proteins regulate various cellular processes. ► Thioredoxin system plays an important role to combat oxidative/nitrosative stress. ► GSH and Trx system perform the major role in denitrosylation of RSNOs.
Author Sengupta, Rajib
Holmgren, Arne
Author_xml – sequence: 1
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  fullname: Holmgren, Arne
  email: arne.holmgren@ki.se
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Keywords Thiol
Thioredoxin
Thioredoxin reductase
Nitric oxide
S-nitrosylation
Redox regulation
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Snippet S-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of S-nitrosothiols...
BACKGROUND: S-nitrosylation (or S-nitrosation) by Nitric Oxide (NO), i.e., the covalent attachment of a NO group to a cysteine thiol and formation of...
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SubjectTerms Animals
biochemical pathways
caspase-3
Cell Physiological Phenomena
cysteine
Cysteine - metabolism
glutathione
Glutathione - metabolism
homeostasis
mammals
Nitric oxide
Nitric Oxide - metabolism
Nitrosation
Oxidation-Reduction
Oxidative Stress
proteins
Proteins - metabolism
Redox regulation
S-Nitrosoglutathione - metabolism
S-Nitrosothiols - metabolism
S-nitrosylation
Selenocysteine - metabolism
Signal Transduction
Thiol
thiols
Thioredoxin
Thioredoxin reductase
Thioredoxin-Disulfide Reductase - chemistry
Thioredoxin-Disulfide Reductase - metabolism
Thioredoxins - chemistry
Thioredoxins - metabolism
Title The role of thioredoxin in the regulation of cellular processes by S-nitrosylation
URI https://dx.doi.org/10.1016/j.bbagen.2011.08.012
https://www.ncbi.nlm.nih.gov/pubmed/21878369
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