H2S Signals Through Protein S-Sulfhydration
Asif K. Mustafa,Moataz M. Gadalla,Nilkantha Sen,Seyun Kim,Weitong Mu,Sadia K. Gazi,Roxanne K. Barrow,Guangdong Yang,Rui Wang,Solomon H. Snyder +9 more
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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.read more
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Journal ArticleDOI
Gas Signaling Molecules and Mitochondrial Potassium Channels.
TL;DR: This review focuses on the molecular mechanisms underlying the action of H2S, NO, and CO on potassium channels present within mitochondria, which are believed to induce cytoprotection and facilitate cell death.
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Application of redox proteomics to skeletal muscle aging and exercise.
TL;DR: How redox proteomics can be applied to identify and quantify the reversible modifications on susceptible cysteine residues within those redox-sensitive proteins, and the integration of oxidative and non-oxidative protein modifications in relation to the functional proteome is discussed.
Journal ArticleDOI
Methylene blue counteracts H2S toxicity-induced cardiac depression by restoring L-type Ca channel activity.
Annick Judenherc-Haouzi,Xue-Qian Zhang,Takashi Sonobe,Jianliang Song,Matthew D. Rannals,JuFang Wang,Nicole Tubbs,Joseph Y. Cheung,Philippe Haouzi +8 more
TL;DR: The present results offer a new approach for counteracting H2S toxicity and potentially other conditions associated with acute inhibition of L-type Ca(2+) channels.
Journal ArticleDOI
Enrichments of post-translational modifications in proteomic studies.
Luisa Pieroni,Federica Iavarone,Federica Iavarone,Alessandra Olianas,Viviana Greco,Viviana Greco,Claudia Desiderio,Claudia Martelli,Barbara Manconi,Maria Teresa Sanna,Irene Messana,Massimo Castagnola,Tiziana Cabras +12 more
TL;DR: In this review the state of art of the platforms applied for the enrichment of specific and most common post-translational modifications, such as glycosylation and glycation, phosphorylation, sulfation, redox modifications (i.e. sulphydration and nitrosylation), methylation, acetylations and ubiquitinylation, are described.
Journal ArticleDOI
Endogenous hydrogen sulfide sulfhydrates IKKβ at cysteine 179 to control pulmonary artery endothelial cell inflammation.
Da Zhang,Xiuli Wang,Siyao Chen,Selena Chen,Wen Yu,Xin Liu,Guosheng Yang,Yinghong Tao,Xinjing Tang,Dingfang Bu,Heng Zhang,Wei Kong,Wei Kong,Chaoshu Tang,Chaoshu Tang,Yaqian Huang,Junbao Du,Junbao Du,Hongfang Jin,Hongfang Jin +19 more
TL;DR: In vivo and in vitro findings demonstrated, for the first time, that endogenous H2S directly inactivated IKKβ via sulfhydrating IKK β at Cys179 to inhibit nuclear factor-κB (NF-κBs) pathway activation and thereby control PAEC inflammation in PAH.
References
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Journal ArticleDOI
H2S as a Physiologic Vasorelaxant: Hypertension in Mice with Deletion of Cystathionine γ-Lyase
Guangdong Yang,Guangdong Yang,Lingyun Wu,Bo Jiang,Wei Yang,Jiansong Qi,Kun Cao,Qinghe Meng,Asif K. Mustafa,Weitong Mu,Shengming Zhang,Solomon H. Snyder,Rui Wang,Rui Wang +13 more
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
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Douglas T. Hess,Akio Matsumoto,Sung Oog Kim,Harvey E. Marshall,Jonathan S. Stamler,Jonathan S. Stamler +5 more
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.
Samie R. Jaffrey,Hediye Erdjument-Bromage,Christopher D. Ferris,Paul Tempst,Solomon H. Snyder +4 more
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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