Evidence of endogenously produced hydrogen sulfide (H2S) and persulfidation in male reproduction
Abstract Persulfidation contributes to a group of redox post-translational modifications (PTMs), which arise exclusively on the sulfhydryl group of cysteine as a result of hydrogen sulfide (H2S) action. Redox-active molecules, including H2S, contribute to sperm development; therefore, redox PTMs rep...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2022-07-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-022-15360-x |
| _version_ | 1811224261959876608 |
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| author | Hedvika Řimnáčová Jiří Moravec Miriama Štiavnická Jiřina Havránková Ladan Monsef Petr Hošek Šárka Prokešová Tereza Žalmanová Tereza Fenclová Jaroslav Petr Milena Králíčková Jan Nevoral |
| author_facet | Hedvika Řimnáčová Jiří Moravec Miriama Štiavnická Jiřina Havránková Ladan Monsef Petr Hošek Šárka Prokešová Tereza Žalmanová Tereza Fenclová Jaroslav Petr Milena Králíčková Jan Nevoral |
| author_sort | Hedvika Řimnáčová |
| collection | DOAJ |
| description | Abstract Persulfidation contributes to a group of redox post-translational modifications (PTMs), which arise exclusively on the sulfhydryl group of cysteine as a result of hydrogen sulfide (H2S) action. Redox-active molecules, including H2S, contribute to sperm development; therefore, redox PTMs represent an extremely important signalling pathway in sperm life. In this path, persulfidation prevents protein damage caused by irreversible cysteine hyperoxidation and thus maintains this signalling pathway. In our study, we detected both H2S and its production by all H2S-releasing enzymes (cystathionine γ-lyase (CTH), cystathionine β-synthase (CBS), and 3-mercaptopyruvate sulfurtransferase (MPST)) in male reproduction, including spermatozoa. We provided evidence that sperm H2S leads to persulfidation of proteins, such as glyceraldehyde-3-phosphate dehydrogenase, tubulin, and anchor protein A-kinase. Overall, this study suggests that persulfidation, as a part of the redox signalling pathway, is tightly regulated by enzymatic H2S production and is required for sperm viability. |
| first_indexed | 2024-04-12T08:45:28Z |
| format | Article |
| id | doaj.art-c5538e31a580498f8c07324946063117 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-12T08:45:28Z |
| publishDate | 2022-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-c5538e31a580498f8c073249460631172022-12-22T03:39:43ZengNature PortfolioScientific Reports2045-23222022-07-0112111210.1038/s41598-022-15360-xEvidence of endogenously produced hydrogen sulfide (H2S) and persulfidation in male reproductionHedvika Řimnáčová0Jiří Moravec1Miriama Štiavnická2Jiřina Havránková3Ladan Monsef4Petr Hošek5Šárka Prokešová6Tereza Žalmanová7Tereza Fenclová8Jaroslav Petr9Milena Králíčková10Jan Nevoral11Biomedical Center in Pilsen, Faculty of Medicine in Pilsen, Charles UniversityBiomedical Center in Pilsen, Faculty of Medicine in Pilsen, Charles UniversityBiomedical Center in Pilsen, Faculty of Medicine in Pilsen, Charles UniversityBiomedical Center in Pilsen, Faculty of Medicine in Pilsen, Charles UniversityBiomedical Center in Pilsen, Faculty of Medicine in Pilsen, Charles UniversityBiomedical Center in Pilsen, Faculty of Medicine in Pilsen, Charles UniversityInstitute of Animal ScienceInstitute of Animal ScienceBiomedical Center in Pilsen, Faculty of Medicine in Pilsen, Charles UniversityInstitute of Animal ScienceBiomedical Center in Pilsen, Faculty of Medicine in Pilsen, Charles UniversityBiomedical Center in Pilsen, Faculty of Medicine in Pilsen, Charles UniversityAbstract Persulfidation contributes to a group of redox post-translational modifications (PTMs), which arise exclusively on the sulfhydryl group of cysteine as a result of hydrogen sulfide (H2S) action. Redox-active molecules, including H2S, contribute to sperm development; therefore, redox PTMs represent an extremely important signalling pathway in sperm life. In this path, persulfidation prevents protein damage caused by irreversible cysteine hyperoxidation and thus maintains this signalling pathway. In our study, we detected both H2S and its production by all H2S-releasing enzymes (cystathionine γ-lyase (CTH), cystathionine β-synthase (CBS), and 3-mercaptopyruvate sulfurtransferase (MPST)) in male reproduction, including spermatozoa. We provided evidence that sperm H2S leads to persulfidation of proteins, such as glyceraldehyde-3-phosphate dehydrogenase, tubulin, and anchor protein A-kinase. Overall, this study suggests that persulfidation, as a part of the redox signalling pathway, is tightly regulated by enzymatic H2S production and is required for sperm viability.https://doi.org/10.1038/s41598-022-15360-x |
| spellingShingle | Hedvika Řimnáčová Jiří Moravec Miriama Štiavnická Jiřina Havránková Ladan Monsef Petr Hošek Šárka Prokešová Tereza Žalmanová Tereza Fenclová Jaroslav Petr Milena Králíčková Jan Nevoral Evidence of endogenously produced hydrogen sulfide (H2S) and persulfidation in male reproduction Scientific Reports |
| title | Evidence of endogenously produced hydrogen sulfide (H2S) and persulfidation in male reproduction |
| title_full | Evidence of endogenously produced hydrogen sulfide (H2S) and persulfidation in male reproduction |
| title_fullStr | Evidence of endogenously produced hydrogen sulfide (H2S) and persulfidation in male reproduction |
| title_full_unstemmed | Evidence of endogenously produced hydrogen sulfide (H2S) and persulfidation in male reproduction |
| title_short | Evidence of endogenously produced hydrogen sulfide (H2S) and persulfidation in male reproduction |
| title_sort | evidence of endogenously produced hydrogen sulfide h2s and persulfidation in male reproduction |
| url | https://doi.org/10.1038/s41598-022-15360-x |
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