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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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Sulfhydration of AKT triggers Tau-phosphorylation by activating glycogen synthase kinase 3β in Alzheimer’s disease

TL;DR: It is found that if phosphorylated AKT is sulfhydrated, it will be unable to inactivate GSK3β and subsequently increases Tau phosphorylation, which primarily contributes to synaptic dysfunction in AD.
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Reductive potential - a savior turns stressor in protein aggregation cardiomyopathy.

TL;DR: The role of RS is discussed as a causal or contributing factor in relevant pathophysiology of a major cardiac disease of human origin and constitutive activation of pathways that enable sustained generation of reducing equivalents of glutathione, reduced nicotinamide adenine dinucleotide phosphate will cause RS.
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Discoveries of Hydrogen Sulfide as a Novel Cardiovascular Therapeutic

TL;DR: The cytoprotective and cardioprotective effects of H2S therapy are discussed, analysis on the molecular alterations that lead to these enhancements are provided, and recently developed therapeutics that may bring this gasotransmitter into the clinic in the near future are explored.
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Using resonance synchronous spectroscopy to characterize the reactivity and electrophilicity of biologically relevant sulfane sulfur

TL;DR: Sulfane sulfur showed species-specific RS2 spectra and intensities at physiological pH, which may reveal the relative abundance of a reactive sulfane sulfur species inside cells.
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Exogenous hydrogen sulfide attenuates the development of diabetic cardiomyopathy via the FoxO1 pathway.

TL;DR: This study investigated the interactions between hydrogen sulfide (H2S) and nuclear FoxO1 in DCM by inhibiting oxidative stress, inflammation, and apoptosis and found that the former can alleviate the development of diabetic cardiomyopathy.
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.
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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