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Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation

Department of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japan
Author to whom correspondence should be addressed.
Academic Editors: Noriyuki Nagahara and Maria Wróbel
Molecules 2016, 21(12), 1721;
Received: 16 November 2016 / Revised: 8 December 2016 / Accepted: 9 December 2016 / Published: 15 December 2016
(This article belongs to the Special Issue Sulfur Atom: Element for Adaptation to an Oxidative Environment 2016)
For decades, reactive persulfide species including cysteine persulfide (CysSSH) have been known to exist endogenously in organisms. However, the physiological significance of endogenous persulfides remains poorly understood. That cystathionine β-synthase and cystathionine γ-lyase produced CysSSH from cystine was recently demonstrated. An endogenous sulfur transfer system involving CysSSH evidently generates glutathione persulfide (GSSH) that exists at concentrations greater than 100 μM in vivo. Because reactive persulfide species such as CysSSH and GSSH have higher nucleophilicity than parental cysteine (Cys) and glutathione do, these reactive species exhibit strong scavenging activities against oxidants, e.g., hydrogen peroxide, and electrophiles, which contributes to redox signaling regulation. Also, several papers indicated that various proteins and enzymes have Cys polysulfides including CysSSH at their specific Cys residues, which is called protein polysulfidation. Apart from the redox signaling regulatory mechanism, another plausible function of protein polysulfidation is providing protection for protein thiol residues against irreversible chemical modification caused by oxidants and electrophiles. Elucidation of the redox signaling regulatory mechanism of reactive persulfide species including small thiol molecules and thiol-containing proteins should lead to the development of new therapeutic strategies and drug discoveries for oxidative and electrophilic stress-related diseases. View Full-Text
Keywords: reactive persulfide species; protein polysulfidation; thiol modification; redox signaling reactive persulfide species; protein polysulfidation; thiol modification; redox signaling
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MDPI and ACS Style

Kasamatsu, S.; Nishimura, A.; Morita, M.; Matsunaga, T.; Abdul Hamid, H.; Akaike, T. Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation. Molecules 2016, 21, 1721.

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