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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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Endogenously produced hydrogen sulfide supports tumor cell growth and proliferation.

TL;DR: A new concept is formulated, which implicates tumor-produced CBS-derived H2S as a combined autocrine and paracrine-signaling molecule that promotes tumor angiogenesis and peritumoral vasodilation and reduces intratumoral neovessel density.
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Impaired Redox Signaling in Huntington’s Disease: Therapeutic Implications

TL;DR: This review will focus on the current understanding of aberrant redox homeostasis in HD and potential therapeutic interventions.
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Platelet‐derived growth factor‐BB induces cystathionine γ‐lyase expression in rat mesangial cells via a redox‐dependent mechanism

TL;DR: Evaluated the redox‐dependent signalling events that regulate the expression of the H2S synthesising enzyme cystathionine‐γ‐lyase in rat mesangial cells to evaluate the regulation of the endogenous synthesis of hydrogen sulfide.
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Old and New Gasotransmitters in the Cardiovascular System: Focus on the Role of Nitric Oxide and Hydrogen Sulfide in Endothelial Cells and Cardiomyocytes

TL;DR: This review would like to explore the recent literature on NO and H2S roles on cardiovascular system and to elucidate potential outcomes in the use of pharmacological drugs interfering with their metabolism.
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Interaction between the signaling molecules hydrogen sulfide and hydrogen peroxide and their role in vacuolar H+ -ATPase regulation in cadmium-stressed cucumber roots.

TL;DR: The results suggest the existence of two pathways of H2 S generation in Cd-stressed cucumber roots, one involves desulfhydrase activity, as was previously demonstrated in different plant species, and the other, the desulfHydrase-independent pathway induced by H2 O2 /NADPH oxidase, may protect V-ATPase from inhibition by Cd.
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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