Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation
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 fro...
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| Format: | Article |
| Language: | English |
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MDPI AG
2016-12-01
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| Series: | Molecules |
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| Online Access: | http://www.mdpi.com/1420-3049/21/12/1721 |
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| author | Shingo Kasamatsu Akira Nishimura Masanobu Morita Tetsuro Matsunaga Hisyam Abdul Hamid Takaaki Akaike |
| author_facet | Shingo Kasamatsu Akira Nishimura Masanobu Morita Tetsuro Matsunaga Hisyam Abdul Hamid Takaaki Akaike |
| author_sort | Shingo Kasamatsu |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-21T14:03:24Z |
| format | Article |
| id | doaj.art-bab528fd83134415801f61f3b868d531 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-12-21T14:03:24Z |
| publishDate | 2016-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-bab528fd83134415801f61f3b868d5312022-12-21T19:01:18ZengMDPI AGMolecules1420-30492016-12-012112172110.3390/molecules21121721molecules21121721Redox Signaling Regulated by Cysteine Persulfide and Protein PolysulfidationShingo Kasamatsu0Akira Nishimura1Masanobu Morita2Tetsuro Matsunaga3Hisyam Abdul Hamid4Takaaki Akaike5Department of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, JapanDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, JapanDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, JapanDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, JapanDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, JapanDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, JapanFor 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.http://www.mdpi.com/1420-3049/21/12/1721reactive persulfide speciesprotein polysulfidationthiol modificationredox signaling |
| spellingShingle | Shingo Kasamatsu Akira Nishimura Masanobu Morita Tetsuro Matsunaga Hisyam Abdul Hamid Takaaki Akaike Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation Molecules reactive persulfide species protein polysulfidation thiol modification redox signaling |
| title | Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation |
| title_full | Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation |
| title_fullStr | Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation |
| title_full_unstemmed | Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation |
| title_short | Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation |
| title_sort | redox signaling regulated by cysteine persulfide and protein polysulfidation |
| topic | reactive persulfide species protein polysulfidation thiol modification redox signaling |
| url | http://www.mdpi.com/1420-3049/21/12/1721 |
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