title: Aquaporins 7 and 11 in boar spermatozoa: detection, localisation and relationship with sperm quality.
abstract: Aquaporins (AQPs) are integral membrane water channels that allow transport of water and small solutes across cell membranes. Although water permeability is known to play a critical role in mammalian cells, including spermatozoa, little is known about their localisation in boar spermatozoa. Two aquaporins, AQP7 and AQP11, in boar spermatozoa were identified by western blotting and localised through immunocytochemistry analyses. Western blot results showed that boar spermatozoa expressed AQP7 (25kDa) and AQP11 (50kDa). Immunocytochemistry analyses demonstrated that AQP7 was localised in the connecting piece of boar spermatozoa, while AQP11 was found in the head and mid-piece and diffuse labelling was also seen along the tail. Despite differences in AQP7 and AQP11 content between boar ejaculates, these differences were not found to be correlated with sperm quality in the case of AQP7. Conversely, AQP11 content showed a significant correlation (P<0.05) with sperm membrane integrity and fluidity and sperm motility. In conclusion, boar spermatozoa express AQP7 and AQP11, and the amounts of AQP11 but not those of AQP7 are correlated with sperm motility and membrane integrity.
authors.affiliation: Biotechnology of Animal and Human Reproduction (TechnoSperm), Department of Biology, Institute of Food and Agricultural Technology, University of Girona, E-17071 Girona, Spain.
authors.forename: Noelia
authors.initials: N
authors.lastname: Prieto-Martínez
authors.affiliation: Biotechnology of Animal and Human Reproduction (TechnoSperm), Department of Biology, Institute of Food and Agricultural Technology, University of Girona, E-17071 Girona, Spain.
authors.forename: Ingrid
authors.initials: I
authors.lastname: Vilagran
authors.affiliation: Biotechnology of Animal and Human Reproduction (TechnoSperm), Department of Biology, Institute of Food and Agricultural Technology, University of Girona, E-17071 Girona, Spain.
authors.forename: Roser
authors.initials: R
authors.lastname: Morató
authors.affiliation: Unit of Animal Reproduction, Department of Animal Medicine and Surgery, Faculty of Veterinary Medicine, Autonomous University of Barcelona, E-08193 Bellaterra (Barcelona), Spain.
authors.forename: Joan E
authors.initials: JE
authors.lastname: Rodríguez-Gil
authors.affiliation: Nuffield Department of Obstetrics and Gynaecology, University of Oxford, Level 3, Women's Centre, John Radcliffe Hospital, Headington, Oxford OX3 9DU, UK.
authors.forename: Marc
authors.initials: M
authors.lastname: Yeste
authors.affiliation: Biotechnology of Animal and Human Reproduction (TechnoSperm), Department of Biology, Institute of Food and Agricultural Technology, University of Girona, E-17071 Girona, Spain.
authors.forename: Sergi
authors.initials: S
authors.lastname: Bonet
mesh_terms: D000818:Animals; D017849:Animals, Inbred Strains; D020346:Aquaporins / Q000378:metabolism*; D055592:Biophysical Phenomena; D015153:Blotting, Western / Q000662:veterinary; D002462:Cell Membrane / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel / Q000662:veterinary; D007150:Immunohistochemistry / Q000662:veterinary; D008297:Male; D008560:Membrane Fluidity; D018613:Microscopy, Confocal / Q000662:veterinary; D025341:Principal Component Analysis; D020033:Protein Isoforms / Q000378:metabolism; D021381:Protein Transport; D055101:Semen Analysis / Q000662:veterinary; D013030:Spain; D013045:Species Specificity; D013081:Sperm Motility; D013094:Spermatozoa / Q000166:cytology / Q000378:metabolism*; D034421:Sus scrofa / Q000502:physiology*
chemical_list: D020346:Aquaporins; D020033:Protein Isoforms