Abstract
At appropriate concentrations, hydrogen sulfide, a well-known gasotransmitter, plays important roles in both physiology and pathophysiology. Increasing evidence suggests that modifying thiol groups of specific cysteines in target proteins via sulfhydration or persulfidation is one of the important mechanisms responsible for the biological functions of hydrogen sulfide. A variety of key proteins of different cellular pathways in mammals have been reported to be sulfhydrated by hydrogen sulfide to participate and regulate the processes of cell survival/death, cell differentiation, cell proliferation/hypertrophy, cellular metabolism, mitochondrial bioenergetics/biogenesis, endoplasmic reticulum stress, vasorelaxtion, inflammation, oxidative stress, etc. Moreover, S-sulfhydration also exerts many biological functions through the cross-talk with other post-translational modifications including phosphorylation, S-nitrosylation and tyrosine nitration. This review summarizes recent studies of hydrogen sulfide-induced sulfhydration as a posttranslational modification, an important biological function of hydrogen sulfide, and sulfhydrated proteins are introduced. Additionally, we discuss the main methods of detecting sulfhydration of proteins.
Highlights
Hydrogen sulfide, a “superstar” gasotransmitter in the gaseous signal molecule family, has been found involved in various physiologic and pathophysiologic processes since the end of the last century
We showed some main formation processes of S-sulfhydrated modification which is believed to occur possibly in the following cases: (1) protein thiols do not react with hydrogen sulfide (H2S) directly, it can react with sulfenic acids; (2) H2S can react with S-nitrosated cysteines leading to the formation of thionitrous acid (HSNO) or nitroxyl (HNO); (3) H2S can react with cysteine disulfides (-S-S) for sulfhydration formation; (4) reaction between oxidized sulfide species such as polysulfides and cysteine thiols; (5) persulfides play as carriers and engage in “trans-S-sulfhydration” reaction (Figure 1)
With increasing studies concerning the effect of H2S on phenotype in physiological and pathological processes, the mechanism by which H2S functions in different signaling pathways via S-sulfhydration has gradually been recognized
Summary
Specialty section: This article was submitted to Experimental Pharmacology and Drug. Citation: Zhang D, Du J, Tang C, Huang Y and Jin H (2017) H2S-Induced Sulfhydration: Biological Function and Detection Methodology. Increasing evidence suggests that modifying thiol groups of specific cysteines in target proteins via sulfhydration or persulfidation is one of the important mechanisms responsible for the biological functions of hydrogen sulfide. A variety of key proteins of different cellular pathways in mammals have been reported to be sulfhydrated by hydrogen sulfide to participate and regulate the processes of cell survival/death, cell differentiation, cell proliferation/hypertrophy, cellular metabolism, mitochondrial bioenergetics/biogenesis, endoplasmic reticulum stress, vasorelaxtion, inflammation, oxidative stress, etc. S-sulfhydration exerts many biological functions through the cross-talk with other post-translational modifications including phosphorylation, S-nitrosylation and tyrosine nitration. This review summarizes recent studies of hydrogen sulfide-induced sulfhydration as a posttranslational modification, an important biological function of hydrogen sulfide, and sulfhydrated proteins are introduced. We discuss the main methods of detecting sulfhydration of proteins
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