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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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Posted ContentDOI

Hydrogen sulfide maintains redox homeostasis and suppresses ganoderic acids biosynthesis under heat stress via S-sulfhydrating thioredoxin 1 in Ganoderma lucidum

TL;DR: In this article , the role of hydrogen sulfide in maintaining redox homeostasis under heat stress (HS) was determined, and a redox-regulated protein, thioredoxin 1 (Trx1), was selected as a potential target of H 2 S.
Patent

Compositions and methods of modulating gasotransmitter signaling

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Homocysteinylation and Sulfhydration in Diseases

TL;DR: In this article , the role of protein modification by hydrogen sulfide (H2S) and H2S in diseases has been discussed, and the authors make a prediction that H 2S might exert a protective effect on the toxicity of homocysteinylation of target protein via sulfhydration.
Dissertation

The role of intestinal hydrogen sulfide on GLP-1 secretion and downstream metabolism

TL;DR: A direct role for H 2S in the stimulation of GLP-1 and a potential role for sulfur prebiotics to increase the H2S producing SRB as a means to enhance GLP -1 and improve metabolism are demonstrated.
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.
Journal ArticleDOI

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.
Journal ArticleDOI

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.
Journal ArticleDOI

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.
Journal ArticleDOI

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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