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Open AccessJournal ArticleDOI

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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Journal ArticleDOI

Esterase-Activated Perthiocarbonate Persulfide Donors Provide Insights into Persulfide Persistence and Stability.

TL;DR: The synthesis of esterase-activated perthiocarbonate persulfide donors are reported and the effects of structural modifications on persulfides release are investigated and it is found that the steric bulk and identity of the thiol significantly impact Persulfide persistence.
Journal ArticleDOI

H2S-mediated blockage of protein acetylation and oxidative stress attenuates lipid overload-induced cardiac senescence.

TL;DR: In this paper, the role of the cystathionine gamma-lyase (CSE) and hydrogen sulphide (H2S) system on lipid overload-induced lipotoxicity and cardiac senescence was investigated.
Book ChapterDOI

Oxidant-Dependent and Oxidant-Independent Proangiogenic and Vasomotor Signaling in Coronary Vascular Endothelium

TL;DR: Vascular endothelial growth factor (VEGF), a major growth factor involved in the maintenance of EC health, vasomotor tone, and angiogenesis, will also be discussed, including the structures of oxidant-producing enzymes, their agonists, and their related signaling pathways in EC.
Posted ContentDOI

Dietary methionine restriction impairs anti-tumor immunity through gut microbiota

TL;DR: This paper showed that methionine restriction exacerbates cancer growth and influences the outcomes of anti-tumor immunotherapy through gut microbiota and immune suppression in immunocompetent settings.
Journal ArticleDOI

Hydrogen sulfide: A new therapeutic target in vascular diseases

TL;DR: The role of H2S in vascular diseases, including hypertension, atherosclerosis, inflammation and angiogenesis is systemically summarized and a novel therapeutic perspective comprising crosstalk between H 2S and smooth muscle cell function is outlined.
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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