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http://hdl.handle.net/10662/20129
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Campo DC | Valor | idioma |
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dc.contributor.author | Martín Hidalgo, David | - |
dc.contributor.author | Solar Málaga, Soraya | - |
dc.contributor.author | González Fernández, Lauro | - |
dc.contributor.author | Zamorano Quirantes, José | - |
dc.contributor.author | García Marín, Luis Jesús | - |
dc.contributor.author | Bragado González, María Julia | - |
dc.date.accessioned | 2024-02-07T08:31:04Z | - |
dc.date.available | 2024-02-07T08:31:04Z | - |
dc.date.issued | 2023 | - |
dc.identifier.issn | 0165-7380 | es_ES |
dc.identifier.uri | http://hdl.handle.net/10662/20129 | - |
dc.description.abstract | Before fertilization of the oocyte, the spermatozoa must undergo through a series of biochemical changes in the female reproductive tract named sperm capacitation. Spermatozoa regulates its functions by post-translational modifications, being historically the most studied protein phosphorylation. In addition to phosphorylation, recently, protein acetylation has been described as an important molecular mechanism with regulatory roles in several reproductive processes. However, its role on the mammal's sperm capacitation process remains unraveled. Sirtuins are a deacetylase protein family with 7 members that regulate protein acetylation. Here, we investigated the possible role of SIRT1 on pig sperm capacitation-related events by using YK 3-237, a commercial SIRT1 activator drug. SIRT1 is localized in the midpiece of pig spermatozoa. Protein tyrosine phosphorylation (focused at p32) is an event associated to pig sperm capacitation that increases when spermatozoa are in vitro capacitated in presence of YK 3-237. Eventually, YK 3-237 induces acrosome reaction in capacitated spermatozoa: YK 3-237 treatment tripled (3.40 ± 0.40 fold increase) the percentage of acrosome-reacted spermatozoa compared to the control. In addition, YK 3-237 induces sperm intracellular pH alkalinization and raises the intracellular calcium levels through a CatSper independent mechanism. YK 3-237 was not able to bypass sAC inhibition by LRE1. In summary, YK 3-237 promotes pig sperm capacitation by a mechanism upstream of sAC activation and independent of CatSper calcium channel | es_ES |
dc.description.sponsorship | David Martin-Hidalgo was supported by “Stop Fuga de Cerebros” funded by Roche Farma S.A and implemented by Fundación para la Formación y la Investigación de los Profesionales de la Salud de Extremadura (Spain, FS P20-34). Lauro González-Fernández was granted by Ministerio de Ciencia e Innovación: RYC2020-028915-I, MCIN/AEI/10.13039/50110 0 011033 and by “ESF Investing in your future”. This work was also supported by “Junta de Extremadura” (Spain); References: IB20154, IB20078 and GR18094. | es_ES |
dc.format.extent | 14 p. | es_ES |
dc.format.mimetype | application/pdf | en_US |
dc.language.iso | eng | es_ES |
dc.publisher | Springer | es_ES |
dc.rights | Attribution 4.0 International | * |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | Espermatozoide | es_ES |
dc.subject | Sperm | es_ES |
dc.subject | Cerdo | es_ES |
dc.subject | Pig | es_ES |
dc.subject | Reacción acrosómica | es_ES |
dc.subject | Acrosome reaction | es_ES |
dc.subject | Fosforilación tirosina | es_ES |
dc.subject | Phosphorylation tyrosine | es_ES |
dc.title | The compound YK 3-237 promotes pig sperm capacitation-related events | es_ES |
dc.type | article | es_ES |
dc.description.version | peerReviewed | es_ES |
europeana.type | TEXT | en_US |
dc.rights.accessRights | openAccess | es_ES |
dc.subject.unesco | 3104.08 Porcinos | es_ES |
dc.subject.unesco | 3104.11 Reproducción | es_ES |
europeana.dataProvider | Universidad de Extremadura. España | es_ES |
dc.identifier.bibliographicCitation | Martín-Hidalgo, D., Solar-Málaga, S., González-Fernández, L.; Zamorano, J.; García Marín, L. J.; Bragado González, M. J. (2023). The compound YK 3-237 promotes pig sperm capacitation-related events. Vet Res Commun (2023). https://doi.org/10.1007/s11259-023-10243-6 | es_ES |
dc.type.version | publishedVersion | es_ES |
dc.contributor.affiliation | N/A | es_ES |
dc.contributor.affiliation | Universidad de Extremadura. Departamento de Bioquímica, Biología Molecular y Genética | es_ES |
dc.contributor.affiliation | Universidad de Extremadura. Departamento de Fisiología | es_ES |
dc.relation.publisherversion | https://link.springer.com/article/10.1007/s11259-023-10243-6 | es_ES |
dc.relation.publisherversion | https://doi.org/10.1007/s11259-023-10243-6 | es_ES |
dc.identifier.doi | 10.1007/s11259-023-10243-6 | - |
dc.identifier.publicationtitle | Veterinary Research Communications | es_ES |
dc.identifier.publicationfirstpage | 1 | es_ES |
dc.identifier.publicationlastpage | 14 | es_ES |
dc.identifier.e-issn | 1573-7446 | es_ES |
dc.identifier.orcid | 0000-0002-6787-0006 | es_ES |
dc.identifier.orcid | 0000-0003-2463-5978 | es_ES |
dc.identifier.orcid | 0000-0001-5568-548X | es_ES |
dc.identifier.orcid | 0000-0002-1795-7381 | es_ES |
dc.identifier.orcid | 0000-0001-7770-0775 | es_ES |
Colección: | DFSIO - Artículos |
Archivos
Archivo | Descripción | Tamaño | Formato | |
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s11259_023_10243_6.pdf | 2,08 MB | Adobe PDF | Descargar |
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