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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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Journal ArticleDOI

Biological Functions of Hydrogen Sulfide in Plants

TL;DR: In this paper , the authors summarize the specific ways in which hydrogen sulfide is endogenously synthesized and metabolized in plants, along with the agents and methods used for H2S research, and outline the progress of research on the regulation of H 2S on plant metabolism and morphogenesis, abiotic stress tolerance, and the series of different post-translational modifications (PTMs) in which H 2 s is involved.
Journal ArticleDOI

H2S contributed from CSE during cellular senescence suppresses inflammation and nitrosative stress.

TL;DR: In this paper , the role of hydrogen sulfide (H2S) in the regulation of inflammatory phenotype and nitrosative stress during cellular senescence has been investigated using a combination of direct measurements with fluorescent reporter dye (WSP-5) and protein sulfhydration analysis.
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Salen, salan and salalen zinc(II) complexes in the interaction with HS-: time-resolved fluorescence applications.

TL;DR: In this article , a computational analysis on the time dependent density functional theory (TD-DFT) level explored the overall fluorescence properties of the title complexes and their different fluorescence responses to HS-.
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Hypertension and renal disease programming: focus on the early postnatal period

- 01 Sep 2022 - 
TL;DR: In this paper , the authors highlight the great number of studies performed in animal models, showing the broad range of stressors involved in hypertension and renal disease programming, with a particular focus on the stressors that occur during the early postnatal period.
Book ChapterDOI

From Nitric Oxide Toward S-Nitrosylation: Expanding Roles in Gametes and Embryos

TL;DR: This chapter summarizes, in a nonexhaustive manner, research that explores the role of NO in gametes and embryos.
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.
Journal ArticleDOI

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.
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.

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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