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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Polysulfides Link H2S to Protein Thiol Oxidation
Romy Greiner,Zoltán Pálinkás,Katrin Bäsell,Dörte Becher,Haike Antelmann,Péter Nagy,Tobias P. Dick +6 more
TL;DR: This study suggests that the effects that have been attributed to H2S in previous reports may in fact have been mediated by polysulfides, and supports the notion that sulfane sulfur rather than sulfide is the actual in vivo agent of H 2S signaling.
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A review of hydrogen sulfide (H2S) donors: Chemistry and potential therapeutic applications.
TL;DR: This review examines a variety of H2S donor systems classified by their H 2S‐releasing trigger as well as their H1N1 release profiles, byproducts, and potential therapeutic applications.
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H2S mediates O2 sensing in the carotid body.
Ying-Jie Peng,Jayasri Nanduri,Gayatri Raghuraman,Dangjai Souvannakitti,Moataz M. Gadalla,Ganesh K. Kumar,Solomon H. Snyder,Nanduri R. Prabhakar +7 more
TL;DR: In this paper, it was shown that hydrogen sulfide (H2S) is a physiologic gasotransmitter of the carotid body, enhancing its sensory response to hypoxia.
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SIRT5 Regulates both Cytosolic and Mitochondrial Protein Malonylation with Glycolysis as a Major Target
Yuya Nishida,Matthew J. Rardin,Chris Carrico,Wenjuan He,Alexandria K. Sahu,Philipp Gut,Rami Najjar,Mark Fitch,Marc K. Hellerstein,Bradford W. Gibson,Eric Verdin +10 more
TL;DR: It is demonstrated that SIRT5 is a global regulator of lysine malonylation and provide a mechanism for regulation of energetic flux through glycolysis.
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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