dc.creatorTeijeiro, Juan Manuel
dc.creatorMarini, Patricia Estela
dc.creatorBragado, María Julia
dc.creatorGarcía-Marin, Luis
dc.date2017-11-17T01:26:06Z
dc.date2017-11-17T01:26:06Z
dc.date2017-02-10
dc.date2017-11-17T01:26:06Z
dc.date2017-11-17T01:26:06Z
dc.date2017-02-10
dc.date.accessioned2019-05-17T20:22:05Z
dc.date.available2019-05-17T20:22:05Z
dc.identifier2047-2927
dc.identifierhttp://hdl.handle.net/2133/9294
dc.identifierhttp://hdl.handle.net/2133/9294
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/2679599
dc.descriptionMale 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.
dc.descriptionFil: Teijeiro, Juan Manuel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Laboratorio de Medicina Reproductiva (CONICET); Argentina
dc.descriptionFil: Marini, Patricia Estela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Laboratorio de Medicina Reproductiva (CONICET); Argentina
dc.descriptionFil: Marini, Patricia Estela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (CONICET); Argentina
dc.descriptionFil: Marini, Patricia Estela. Universidad Nacional de Rosario. Consejo de Investigaciones de la Universidad Nacional de Rosario; Argentina
dc.descriptionFil: Bragado, María Julia. Universidad de Extremadura. Escuela de Medicina Veterinaria. Grupo de Investigación de Señalización Intracelular y Tecnología de la Reproducción; España
dc.descriptionFil: García-Marin, Luis. Universidad de Extremadura. Escuela de Medicina Veterinaria. Grupo de Investigación de Señalización Intracelular y Tecnología de la Reproducción; España
dc.formatapplication/pdf
dc.languageeng
dc.publisherWiley
dc.relationhttp://onlinelibrary.wiley.com/doi/10.1111/andr.12312/abstract
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.rightsWiley
dc.rightshttps://authorservices.wiley.com/asset/photos/licensing-and-open-access-photos/eCTA_sample.pdf
dc.rightsembargoedAccess
dc.subjectEspermatozoides porcinos
dc.subjectFluidez de membrana
dc.subjectProtein quinasa C
dc.subjectBoar sperm
dc.subjectMembrane fluidity
dc.subjectProtein kinase C
dc.titleProtein kinase C activity in boar sperm
dc.typeArtículos de revistas
dc.typeArtículos de revistas
dc.typeArtículos de revistas


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