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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Competition of Reactive Signals and Thiol Modifications of Proteins
TL;DR: In this paper, it was argued that all these molecules are not acting in the same manner, and that H2S was acting in a role which moderated the effects of ROS and NO.
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S-desulfurization: A different covalent modification mechanism from persulfidation by GSH.
TL;DR: In this article, GSH is bound to active cysteine sites of protein by S-desulfurization, which is a new covalent modification mechanism of protein, thus regulating catalytic activity.
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From Primordial Gas to the Medicine Cabinet.
TL;DR: This article is part of a themed section on Hydrogen Sulfide in Biology & Medicine, which highlights the importance of knowing the carrier and removal status of hydrogen sulfide in the animal kingdom.
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The interaction of disulfiram and H2S metabolism in inhibition of aldehyde dehydrogenase activity and liver cancer cell growth
TL;DR: In this article, the potential of combining Disulfiram (DSF) and H2S for inhibition of cancer cell growth and tumor development by targeting aldehyde dehydrogenase (ALDH).
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H2S signaling and extracellular matrix remodeling in cardiovascular diseases: A tale of tense relationship.
Jiechun Zhu,Guangdong Yang +1 more
TL;DR: The potential of hydrogen sulfide (H2S) in the prevention and treatment of cardiovascular diseases through attenuating adverse ECM remodeling has been discussed in this paper, where the implications and mechanisms of H2S in the regulation of extracellular matrix remodeling in cardiovascular diseases have been discussed.
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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