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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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Selective Irreversible Inhibition of Neuronal and Inducible Nitric-oxide Synthase in the Combined Presence of Hydrogen Sulfide and Nitric Oxide.

TL;DR: The results suggest that nNOS and inducible NOS but not endothelial NOS are irreversibly inhibited by H2S/NO at modest concentrations of H1N1 in a reaction that may allow feedback inhibition of NO production under conditions of excessive NO/H2S formation.
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A redox cycle with complex II prioritizes sulfide quinone oxidoreductase-dependent H2S oxidation

TL;DR: In this article , a new redox cycle is established between SQOR and complex II, operating in reverse, under high H2S concentrations, which are known to inhibit complex IV, and the purine nucleotide cycle and the malate aspartate shuttle furnish fumarate, which leads to succinate accumulation.
Journal ArticleDOI

Exogenous H2S enhances mice gastric smooth muscle tension through S‐sulfhydration of KV4.3, mediating the inhibition of the voltage‐dependent potassium current

TL;DR: This study aimed to investigate the possible targets of H2S and determine how H 2S affects its target proteins during H1N1‐induced contraction.
Journal ArticleDOI

Age-Dependent Allergic Asthma Development and Cystathionine Gamma-Lyase Deficiency.

TL;DR: Whether the age-dependent development of allergic asthma is caused by age- dependent expression of cystathionine gamma-lyase (CSE), a key enzyme that catalyzes the production of hydrogen sulfide (H2S), is examined.
Journal ArticleDOI

Engineering macromolecular nanocarriers for local delivery of gaseous signaling molecules.

TL;DR: In this article, the authors focus on the recent development of macromolecular nanocarriers for the local delivery of various endogenous gaseous signaling molecules (GSMs).
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.
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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.
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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