Protein S-nitrosylation: purview and parameters

Hess, Douglas T.; Matsumoto, Akio; Kim, Sung Oog; Marshall, Hiram W.; Stamler, Jonathan S.

doi:10.1038/nrm1569

Cited by 1,955 publications

(1,975 citation statements)

References 151 publications

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“…S-nitrosylation of specific cysteine residues (which will be discussed further below) has been detected in well over 100 proteins of all classes and is arguably the principal mechanism by which NO signals [1]. Much like phosphorylation by kinases, S-nitrosylation by NOSs influences protein activity, protein-protein interactions and protein location.…”

Section: Oxidants As Modulators Of Signal Transductionmentioning

confidence: 99%

“…It is important to note that NO signalling by guanylate cyclase and S-nitrosylation are not necessarily mutually exclusive [12,13]. S-nitrosylation has been implicated in transmitting signals downstream of all classes of receptors, including GPCRs, RTKs, TNF, Toll, glutaminergic and other [1,[14][15][16]--acting locally within subcellular signaling domains as well conveying signals from the cell surface to intracellular compartments, including the mitrochondria and the nucleus (e.g. by modification of transcription factors).…”

Section: Oxidants As Modulators Of Signal Transductionmentioning

confidence: 99%

“…S-nitrosylation exhibits a number of essential features that are prototypic of biological signals and may be useful when considering the possibility that additional reactive oxidants subserve signaling roles: I) temporal regulation on physiological timescales (S-nitrosylation is stimuluscoupled and rapid), II) the existence of motifs within proteins that facilitate S-nitrosylation and/or provide specificity [1,17], III) co-localization of target proteins with a source of NO (e.g. NOS enzyme) [18], IV) reversibility; and V) enzymatic control (e.g.…”

Section: Oxidants As Modulators Of Signal Transductionmentioning

confidence: 99%

“…Compelling data also indicates that oxidants are produced and employed in physiological settings as signaling molecules in control of cell and tissue homeostasis, cell division, migration, contraction, and mediator production [1][2][3][4]. Collectively, these signaling oxidants--which include nitric oxide (NO), S-nitrosothiols (SNO, in particular Snitrosoglutathione; GSNO) and hydrogen peroxide (H 2 O 2 )--are produced mainly by NADPHdependent enzymes (NO synthases and NADPH oxidases) whose expression is tightly controlled, compartmentalized and tissue-specific.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Redox-based regulation of signal transduction: Principles, pitfalls, and promises

Janssen–Heininger¹,

Mossman²,

Heintz³

et al. 2008

Free Radical Biology and Medicine

Self Cite

705

652

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Section: Oxidants As Modulators Of Signal Transductionmentioning

confidence: 99%

Section: Oxidants As Modulators Of Signal Transductionmentioning

confidence: 99%

Section: Oxidants As Modulators Of Signal Transductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Redox-based regulation of signal transduction: Principles, pitfalls, and promises

Janssen–Heininger¹,

Mossman²,

Heintz³

et al. 2008

Free Radical Biology and Medicine

Self Cite

705

652

View full text Add to dashboard Cite

“…The modification of cysteine residues on peptides and proteins via reaction with nitrogen oxides has been examined extensively and is considered to be an important aspect of nitrogen oxide signaling (104)(105)(106)(107). The basic chemistry of thiol modification by nitrogen oxides has also been examined in detail and there are numerous mechanisms by which endogenously generated nitrogen oxides can react with and modify thiols.…”

Section: Interaction Of Nitrogen Oxides With Thiols: S-nitrosylation mentioning

confidence: 99%

The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

Forman

Fukuto

Miller

et al. 2008

Archives of Biochemistry and Biophysics

219

165

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During the past several years, major advances have been made in understanding how reactive oxygen species (ROS) and nitrogen species (RNS) participate in signal transduction. Identification of the specific targets and the chemical reactions involved still remains to be resolved with many of the signaling pathways in which the involvement of reactive species has been determined. Our understanding is that ROS and RNS have second messenger roles. While cysteine residues in the thiolate (ionized) form found in several classes of signaling proteins can be specific targets for reaction with H 2 O 2 and RNS, better understanding of the chemistry, particularly kinetics, suggests that for many signaling events in which ROS and RNS participate, enzymatic catalysis is more likely to be involved than non-enzymatic reaction. Due to increased interest in how oxidation products, particularly lipid peroxidation products, also are involved with signaling, a review of signaling by 4-hydroxy-2-nonenal (HNE) is included. This article focuses on the chemistry of signaling by ROS, RNS, and HNE and will describe reactions with selected target proteins as representatives of the mechanisms rather attempt to comprehensively review the many signaling pathways in which the reactive species are involved. Keywords signaling; glutathione; thioredoxin; oxidants; reactive oxygen species; thiols; peroxide; nitric oxide; peroxynitrite; 4-hydroxynonenal; cysteine; hydrogen peroxide; protein tyrosine phosphatase; reactive nitrogen species; eNOS; iNOS; nNOS; soluble guanylate cyclase; cGMP; tyrosine nitration; fatty acid nitration; NO-heme; NO-metal complexes; nitrite; protein kinase C; ERK; JNK; p38MAPK; tyrosine kinase receptors; calcium OVERVIEW OF SIGNALING BY REACTIVE SPECIESUnderstanding of the roles of reactive oxygen species (ROS), reactive nitrogen species (RNS) and the lipid peroxidation product, 4-hydroxy-2-nonenal (HNE) in signaling has evolved rapidly during the last decade. This has been markedly helped by identification of the specific targets in signaling pathways. In previous reviews, we defined how ROS, H 2 O 2 in particular,

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Messenger Molecules and Cell Death

Sedlak¹,

Snyder²

2006

JAMA

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Programmed cell death, also called apoptosis, participates not only in normal physiologic processes such as development of the immune system, but also in many diseases. A loss of normal cell death may occur in cancer, and excessive cell death is found in a variety of neurodegenerative conditions. We describe 3 distinct pathways that regulate cell death. First, bilirubin, often thought to be a toxic end product of heme metabolism, serves as a physiologic cytoprotectant that may attenuate multiple forms of morbidity. In a second pathway, the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mediates a novel cell death cascade. Cytotoxic stimuli, via nitric oxide generation, lead to the binding of GAPDH to the protein Siah1, translocation of GAPDH-Siah1 to the nucleus, and ultimately cell death. Third, cytochrome c, released from mitochondria early in apoptosis, synergizes with inositol-1,4,5-triphosphate (IP3) to elicit massive cellular calcium release, resulting in cell death. These pathways may regulate cell survival in a variety of pathologic states and represent fertile targets for novel therapies.

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Protein S-nitrosylation: purview and parameters

Cited by 1,955 publications

References 151 publications

Redox-based regulation of signal transduction: Principles, pitfalls, and promises

Redox-based regulation of signal transduction: Principles, pitfalls, and promises

The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

Messenger Molecules and Cell Death

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