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H2S Signals Through Protein S-Sulfhydration

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TLDR
Ex vivo endogenous H2S physiologically modifies cysteine residues in many proteins, including glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and actin, converting Cysteine -SH groups to -SSH groups in a process the authors call S-sulfhydration.
Abstract
Hydrogen sulfide (H2S), a messenger molecule generated by cystathionine gamma-lyase, acts as a physiologic vasorelaxant. Mechanisms whereby H2S signals have been elusive. We now show that H2S physiologically modifies cysteines in a large number of proteins by S-sulfhydration. About 10 to 25% of many liver proteins, including actin, tubulin, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), are sulfhydrated under physiological conditions. Sulfhydration augments GAPDH activity and enhances actin polymerization. Sulfhydration thus appears to be a physiologic posttranslational modification for proteins.

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Citations
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Analysis and Functional Studies of the Gasotransmitters Hydrogen Sulfide and Nitric Oxide

TL;DR: In this paper, the authors present a list of ABBREVIATIONS/SYMBOLS and ABBEVIATION/ABBEVVIATION symbols for the first time.
Journal ArticleDOI

Binding mechanism of disulfide species to ferric hemeproteins: The case of metmyoglobin.

TL;DR: In this paper , the authors studied the association process for disulfane and its conjugate base hydrodisulfide at different pH conditions and provided free energy profiles for ligand migration for both acid/base species, showing a similar behavior to the previously reported for the related H2S/HS− pair.
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Proteomic and phosphoproteomic analysis reveal threonine deficiency increases hepatic lipid deposition in Pekin ducks via reducing STAT phosphorylation

TL;DR: In this article , the effects of dietary threonine deficiency on the expressions of proteins and phosphoproteins in liver of Pekin ducks were investigated to identify the underlying molecular changes.
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Protective Roles of Hydrogen Sulfide in Alzheimer’s Disease and Traumatic Brain Injury

Bindu D. Paul, +1 more
- 01 May 2023 - 
TL;DR: A review of the latest discoveries on the neuroprotective roles of hydrogen sulfide (H2S) in Alzheimer's disease and traumatic brain injury is presented in this paper . But, it does not address the role of H2S in brain injury.
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H2S- and Redox-State-Mediated PTP1B S-Sulfhydration in Insulin Signaling

TL;DR: In this paper , a feasible PEG-switch method was used to determine the levels of PTP1B S-sulfhydration and cellular redox homeostasis in response to insulin stimulation.
References
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Journal ArticleDOI

H2S as a Physiologic Vasorelaxant: Hypertension in Mice with Deletion of Cystathionine γ-Lyase

TL;DR: It is shown that H2S is physiologically generated by cystathionine γ-lyase (CSE) and that genetic deletion of this enzyme in mice markedly reduces H 2S levels in the serum, heart, aorta, and other tissues.
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Protein S-nitrosylation: purview and parameters.

TL;DR: S-nitrosylation conveys a large part of the ubiquitous influence of nitric oxide on cellular signal transduction, and provides a mechanism for redox-based physiological regulation.
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The vasorelaxant effect of H2S as a novel endogenous gaseous KATP channel opener

TL;DR: It is demonstrated that H2S is an important endogenous vasoactive factor and the first identified gaseous opener of KATP channels in vascular SMCs and production from vascular tissues was enhanced by nitric oxide.
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Hydrogen sulphide and its therapeutic potential

TL;DR: The physiology and biochemistry of H2S is overviews, the effects of H 2S inhibitors or H2s donors in animal models of disease are summarized, the potential options for the therapeutic exploitation of H1S are outlined and they are outlined.
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Protein S-nitrosylation: a physiological signal for neuronal nitric oxide.

TL;DR: Protein S-nitrosylation is established as a physiological signalling mechanism for neuronally generated NO in mice harbouring a genomic deletion of neuronal NO synthase (nNOS).
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