scispace - formally typeset
Open AccessJournal ArticleDOI

H2S Signals Through Protein S-Sulfhydration

Reads0
Chats0
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
More filters
Journal ArticleDOI

H2S and polysulfide metabolism: Conventional and unconventional pathways

TL;DR: This review summarizes the current knowledge of both the conventional and unconventional pathways for hydrogen sulfide regulation, and describes a number of standard “conventional” pathways that have been described and well characterized.
Journal ArticleDOI

Measurement and meaning of markers of reactive species of oxygen, nitrogen and sulfur in healthy human subjects and patients with inflammatory joint disease

TL;DR: The concept that ROS/RNS-mediated protein damage creates neoepitopes, resulting in autoantibody formation against proteins, e.g. type-II collagen and the complement component, C1q, have been detected in inflammatory autoimmune diseases are highlighted.
Journal ArticleDOI

Hydrogen sulfide regulates inward-rectifying K+ channels in conjunction with stomatal closure.

TL;DR: The selective inactivation of current carried by inward-rectifying K+ channels of tobacco (Nicotiana tabacum) guard cells is reported and its close parallel with stomatal closure evoked by submicromolar concentrations of H2S is shown.
Journal ArticleDOI

Modulation of Ion Channels by Hydrogen Sulfide

TL;DR: This article reviews the numerous, yet diverse, types of ion channels now reported to be regulated by H(2)S, and determines the mechanisms by which H( 2)S regulates ion channels, as well as other target proteins.
Journal ArticleDOI

Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is inactivated by S-sulfuration in vitro

TL;DR: Questions about the reported ability of H2S to activate GAPDH by the sulfuration of its active site thiol are raised, and polysulfide is a stronger protein S-sulfurating agent than sulfide is indicated.
References
More filters
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).
Related Papers (5)