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
Citations
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Cytoprotective actions of hydrogen sulfide in ischaemia-reperfusion injury.
Adrienne L. King,David J. Lefer +1 more
TL;DR: It has been demonstrated that the administration of H2S either prior to ischaemia or at reperfusion significantly ameliorates myocardial and hepatic ischaia–reperfusion injury and the review provides a summary of several known molecular targets of H 2S protection.
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Hydrogen sulfide in physiology and pathogenesis of bacteria and viruses.
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Quantitative Persulfide Site Identification (qPerS-SID) Reveals Protein Targets of H2S Releasing Donors in Mammalian Cells.
Sebastian Longen,Florian Richter,Yvette Köhler,Ilka Wittig,Karl-Friedrich Beck,Josef Pfeilschifter +5 more
TL;DR: In this article, a mass spectrometry-based method was used to identify persulfide-containing peptides in the mammalian proteome and showed that negative charged amino acids appeared more frequently adjacent to cysteines forming persulfides.
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Sodium thiosulfate attenuates angiotensin II-induced hypertension, proteinuria and renal damage
Pauline M. Snijder,Anne-Roos S. Frenay,Anne M. Koning,Matthias Bachtler,Andreas Pasch,Arjan J. Kwakernaak,Else van den Berg,Eelke M. Bos,Jan-Luuk Hillebrands,Gerjan Navis,Henri G. D. Leuvenink,Harry van Goor +11 more
TL;DR: Investigating the protective properties of H(2)S in angiotensin II (Ang II)-induced hypertensive renal disease in rats suggests that intervention in H( 2)S production pathways has potential therapeutic benefit and might be a valuable addition to the already existing antihypertensive and renoprotective therapies.
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Physiological roles of hydrogen sulfide and polysulfides.
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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
Protein S-nitrosylation: purview and parameters.
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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