Protein kinase C activity in boar sperm

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dc.creator Teijeiro, Juan Manuel
dc.creator Marini, Patricia Estela
dc.creator Bragado, María Julia
dc.creator García-Marin, Luis
dc.date.accessioned 2017-11-17T01:26:06Z
dc.date.available 2017-11-17T01:26:06Z
dc.date.issued 2017-02-10
dc.identifier.issn 2047-2927 es
dc.identifier.uri http://hdl.handle.net/2133/9294
dc.description Male germ cells undergo different processes within the female reproductive tract to successfully fertilize the oocyte. These processes are triggered by different extracellular stimuli leading to activation of protein phosphorylation. Protein kinase C (PKC) is a key regulatory enzyme in signal transduction mechanisms involved in many cellular processes. Studies in boar sperm demonstrated a role for PKC in the intracellular signaling involved in motility and cellular volume regulation. Experiments using phorbol 12-myristate 13-acetate (PMA) showed increases in the Serine/Threonine phosphorylation of substrates downstream of PKC in boar sperm. In order to gain knowledge about those cellular processes regulated by PKC, we evaluate the effects of PMA on boar sperm motility, lipid organization of plasma membrane, integrity of acrosome membrane and sperm agglutination. Also, we investigate the crosstalk between PKA and PKC intracellular pathways in spermatozoa from this species. The results presented here reveal a participation of PKC in sperm motility regulation and membrane fluidity changes, which is probably associated to acrosome reaction and to agglutination. Also, we show the existence of a hierarchy in the kinases pathway. Previous works on boar sperm suggest a pathway in which PKA is positioned upstream to PKC and this new results support such model. es
dc.description.sponsorship ANPCyT-BID PICT 2012-0342 es
dc.description.sponsorship Government of Extremadura, Spain (JUEX-IBI13121, PCJ1008, GR10125 and GR10156) es
dc.description.sponsorship Programa AVE (Ayuda para Viajes al Exterior) Universidad Nacional de Rosario, 2011 es
dc.format application/pdf
dc.format.extent Volume 5, Issue 2 Pages 381–391 es
dc.language.iso eng es
dc.publisher Wiley es
dc.rights embargoedAccess es
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/2.5/ar/ *
dc.subject Espermatozoides porcinos es
dc.subject Fluidez de membrana es
dc.subject Protein quinasa C es
dc.subject Boar sperm es
dc.subject Membrane fluidity es
dc.subject Protein kinase C es
dc.title Protein kinase C activity in boar sperm es
dc.type article
dc.type artículo
dc.type acceptedVersion
dc.rights.holder Wiley es
dc.relation.publisherversion http://onlinelibrary.wiley.com/doi/10.1111/andr.12312/abstract es
dc.rights.text https://authorservices.wiley.com/asset/photos/licensing-and-open-access-photos/eCTA_sample.pdf es
dc.citation.title Andrology es
dc.citation.volume Volume 5, Issue 2 Pages 381–391 es
dc.description.fil Fil: Teijeiro, Juan Manuel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Laboratorio de Medicina Reproductiva (CONICET); Argentina es
dc.description.fil Fil: Marini, Patricia Estela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Laboratorio de Medicina Reproductiva (CONICET); Argentina es
dc.description.fil Fil: Marini, Patricia Estela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (CONICET); Argentina es
dc.description.fil Fil: Marini, Patricia Estela. Universidad Nacional de Rosario. Consejo de Investigaciones de la Universidad Nacional de Rosario; Argentina es
dc.description.fil Fil: Bragado, María Julia. Universidad de Extremadura. Escuela de Medicina Veterinaria. Grupo de Investigación de Señalización Intracelular y Tecnología de la Reproducción; España es
dc.description.fil Fil: García-Marin, Luis. Universidad de Extremadura. Escuela de Medicina Veterinaria. Grupo de Investigación de Señalización Intracelular y Tecnología de la Reproducción; España es
dc.type.collection articulo
dc.type.version acceptedVersion es


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