Identificador persistente para citar o vincular este elemento:
http://hdl.handle.net/10662/19496
Registro completo de Metadatos
Campo DC | Valor | idioma |
---|---|---|
dc.contributor.author | Hurtado de Llera, Ana | - |
dc.contributor.author | Martín Hidalgo, David | - |
dc.contributor.author | Gil Anaya, María Cruz | - |
dc.contributor.author | García Marín, Luis Jesús | - |
dc.contributor.author | Bragado González, María Julia | - |
dc.date.accessioned | 2024-01-30T13:13:39Z | - |
dc.date.available | 2024-01-30T13:13:39Z | - |
dc.date.issued | 2014-02-13 | - |
dc.identifier.uri | http://hdl.handle.net/10662/19496 | - |
dc.description.abstract | Spermatozoa successfully fertilize oocytes depending on cell energy-sensitive processes. We recently showed that the cell energy sensor, the AMP-activated protein kinase (AMPK), plays a relevant role in spermatozoa by regulating motility as well as plasma membrane organization and acrosomal integrity, and contributes to the maintenance of mitochondrial membrane potential. As the signaling pathways that control AMPK activity have been studied exclusively in somatic cells, our aim is to investigate the intracellular pathways that regulate AMPK phosphorylation at Thr(172) (activity) in male germ cells. Boar spermatozoa were incubated under different conditions in the presence or absence of Ca(2+), 8Br-cAMP, IBMX, PMA, the AMPK activator A769662, or inhibitors of PKA, PKC, or CaMKKalpha/beta. AMPK phosphorylation was evaluated by Western blot using anti-phospho-Thr(172)-AMPK antibody. Data show that AMPK phosphorylation in spermatozoa is potently stimulated by an elevation of cAMP levels through the activation of PKA, as the PKA inhibitor H89 blocks phospho-Thr(172)-AMPK. Another mechanism to potently activate AMPK is Ca(2+) that acts through two pathways, PKA (blocked by H89) and CaMKKalpha/beta (blocked by STO-609). Moreover, phospho-Thr(172)-AMPK levels greatly increased upon PKC activation induced by PMA, and the PKC inhibitor Ro-32-0432 inhibits TCM-induced AMPK activation. Different stimuli considered as cell stresses (rotenone, cyanide, sorbitol, and complete absence of intracellular Ca(2+) by BAPTA-AM) also cause AMPK phosphorylation in spermatozoa. In summary, AMPK activity in boar spermatozoa is regulated upstream by different kinases, such as PKA, CaMKKalpha/beta, and PKC, as well as by the essential intracellular messengers for spermatozoan function, Ca(2+) and cAMP levels | es_ES |
dc.description.sponsorship | Supported by Ministerio de Ciencia e Innovacion grant AGL2010-15188 and by Government of Extremadura grants PRI09A077 and GR10156. D.M.-H. is a recipient of a Ph.D. grant from the Government of Extremadura, Spain | es_ES |
dc.format.extent | 10 p. | es_ES |
dc.format.mimetype | application/pdf | en_US |
dc.language.iso | eng | es_ES |
dc.publisher | Oxford Academic | es_ES |
dc.subject | Espermatozoide | es_ES |
dc.subject | Sperm | es_ES |
dc.subject | Semen | es_ES |
dc.subject | Semen | es_ES |
dc.subject | Cerdo | es_ES |
dc.subject | Pig | es_ES |
dc.subject | Ampk | es_ES |
dc.title | The calcium/CaMKKalpha/beta and the cAMP/PKA pathways are essential upstream regulators of AMPK activity in boar spermatozoa | es_ES |
dc.type | article | es_ES |
dc.description.version | peerReviewed | es_ES |
europeana.type | TEXT | en_US |
dc.rights.accessRights | embargoedAccess | es_ES |
dc.subject.unesco | 2401 Biología Animal (Zoología) | es_ES |
dc.date.embargoEndDate | 2025-01-30 | es_ES |
europeana.dataProvider | Universidad de Extremadura. España | es_ES |
dc.identifier.bibliographicCitation | Ana Hurtado de Llera, David Martin-Hidalgo, Maria Cruz Gil, Luis J. Garcia-Marin, Maria Julia Bragado, The Calcium/CaMKKalpha/beta and the cAMP/PKA Pathways Are Essential Upstream Regulators of AMPK Activity in Boar Spermatozoa, Biology of Reproduction, Volume 90, Issue 2, 1 February 2014, 29, 1–10, https://doi.org/10.1095/biolreprod.113.112797 | es_ES |
dc.type.version | publishedVersion | es_ES |
dc.contributor.affiliation | Universidad de Extremadura. Departamento de Fisiología | es_ES |
dc.relation.publisherversion | https://academic.oup.com/biolreprod/article/90/2/29,%201-10/2514071?login=true | es_ES |
dc.identifier.doi | 10.1095/biolreprod.113.112797 | - |
dc.identifier.publicationtitle | Biology of Reproduction | es_ES |
dc.identifier.publicationfirstpage | 1 | es_ES |
dc.identifier.publicationlastpage | 10 | es_ES |
dc.identifier.publicationvolume | 90 | es_ES |
dc.identifier.orcid | 0000-0002-6787-0006 | es_ES |
dc.identifier.orcid | 0000-0002-6782-9783 | es_ES |
dc.identifier.orcid | 0000-0001-7041-9673 | 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 | |
---|---|---|---|---|
Hurtado-CaMKK-AMPK-BOR-2014.pdf | Manuscrito original | 589,56 kB | Adobe PDF | Descargar |
BOR-2-Copyright-2014.pdf | Autorización de la revista para publicar el artículo en abierto en el repositorio por un año | 135,25 kB | Adobe PDF | Descargar |
Este elemento está sujeto a una licencia Licencia Creative Commons