English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/22430
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 36 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Título

Evidence for the Involvement of Aquaporins in Sperm Motility Activation of the Teleost Gilthead Sea Bream (Sparus aurata)

AutorZilli, Loredana; Schiavone, Roberta; Chauvigné, François ; Cerdà, Joan ; Storelli, Carlo; Vilella, Sebastiano
Palabras claveAquaporin
Fish sperm
Gamete biology
Sperm
Sperm motility and transpor
Teleost
Fecha de publicación1-may-2009
EditorSociety for the Study of Reproduction
CitaciónBiology of Reproduction 81(5): 880–888 (2009)
ResumenThe expression of aquaporins in the spermatozoa of the marine teleost gilthead sea bream (Sparus aurata) and their involvement in the motility activation process were investigated. Sperm motility was activated by a hyperosmotic shock, but it was completely inhibited by 10 lM HgCl2, such inhibition being partially recovered by beta-mercaptoethanol (ME). Conventional RT-PCR using primers specific for S. aurata aquaglyceroporin (glp) and aquaporin 1a (aqp1a) demonstrated the presence of both mRNAs in spermatozoa. Heterologous expression in Xenopus laevis oocytes showed that 10 and 100 lM HgCl2 equally inhibited water and solute transport through S. aurata aquaporin 1a and S. aurata aquaglyceroporin, but treatment with ME only recovered aquaporin 1a-mediated water permeability. Western blot analysis using isoform-specific antisera on protein extracts from spermatozoa revealed bands that corresponded to the predicted molecular mass of S. aurata aquaglyceroporin (31 kDa) and S. aurata aquaporin 1a (28 kDa). The antisera also demonstrated that both aquaporins were localized in the head and flagellum of the spermatozoa. However, the immunoreaction at the plasma membrane of the spermatozoa head was more intense after the hyperosmotic activation, suggesting the translocation of both aquaporin 1a and aquaglyceroporin into the plasma membrane after the osmotic shock. This study therefore provides the first direct demonstration for the presence of aquaporins in fish sperm. The different sensitivities of S. aurata aquaporin 1a and S. aurata aquaglyceroporin to ME may explain the failure of this reducing agent to fully recover the mercurial inhibition of sperm motility, suggesting that these aquaporins may play different physiological roles during the activation and maintenance of sperm motility in sea bream.
Descripción9 pages,5 figures, 1a table
Versión del editorhttp://dx.doi.org/10.1095/biolreprod.109.077933
URIhttp://hdl.handle.net/10261/22430
DOI10.1095/biolreprod.109.077933
ISSN0006-3363
Aparece en las colecciones: (ICM) Artículos
Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.