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dc.contributor.authorRaldúa, Demetrio-
dc.contributor.authorOtero, David-
dc.contributor.authorFabra, Mercedes-
dc.contributor.authorCerdà, Joan-
dc.date.accessioned2010-02-18T11:44:20Z-
dc.date.available2010-02-18T11:44:20Z-
dc.date.issued2008-03-01-
dc.identifier.citationAmerican Journal Physiology Regulation Integrative and Comparative Physiology 294(3): 993-1003 (2008)en_US
dc.identifier.issn0363-6119-
dc.identifier.urihttp://hdl.handle.net/10261/21304-
dc.description11 pages, 8 figuresen_US
dc.description.abstractDifferential localization and regulation of two aquaporin-1 homologs in the intestinal epithelia of the marine teleost Sparus aurata. Am J Physiol Regul Integr Comp Physiol 294: R993–R1003, 2008. First published January 2, 2008; doi:10.1152/ajpregu.00695.2007.—Aquaporin (AQP)-mediated intestinal water absorption may play a major osmoregulatory role in euryhaline teleosts, although the molecular identity and anatomical distribution of AQPs in the fish gastrointestinal tract is poorly known. Here, we have investigated the functional properties and cellular localization in the intestine of two gilthead seabream (Sparus aurata) homologs of mammalian aquaporin-1 (AQP1), named SaAqp1a and SaAqp1b. Heterologous expression in Xenopus laevis oocytes showed that SaAqp1a and SaAqp1b were water-selective channels. Real-time quantitative RT-PCR and Western blot using specific antisera indicated that abundance of SaAqp1a mRNA and protein was higher in duodenum and hindgut than in the rectum, whereas abundance of SaAqp1b was higher in rectum. In duodenum and hindgut, SaAqp1a localized at the apical brush border and lateral membrane of columnar enterocytes, whereas SaAqp1b was detected occasionally and at very low levels at the apical membrane. In the rectum, however, SaAqp1a was mainly accumulated in the cytoplasm of a subpopulation of enterocytes spread in groups over the surface of the epithelia, including the intervillus pockets, whereas SaAqp1b was detected exclusively at the apical brush border of all rectal enterocytes. Freshwater acclimation reduced the synthesis of SaAqp1a protein in all intestinal segments, but it only reduced SaAqp1b abundance in the rectum. These results show for the first time in teleosts a differential distribution and regulation of two functional AQP1 homologs in the intestinal epithelium, which suggest that they may play specialized functions during water movement across the intestineen_US
dc.description.sponsorshipThis work was supported by Grants from the Spanish Ministry of Education and Science (MEC; AGL2001-0364/ACU and AGL2004-00316) and the European Commission (Q5RS-2002-00784-CRYOCYTE) and by the Reference Center in Aquaculture (Generalitat de Catalunya, Spain) to J. Cerdà. Participation of M. Fabra and D. Raldúa was financed by a fellowship from the Catalan Government (DURSI, Spain) and by a “Ramón y Cajal” contract (MEC), respectivelyen_US
dc.format.extent22195 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherAmerican Physiological Societyen_US
dc.rightsopenAccessen_US
dc.subjectGilthead sea breamen_US
dc.subjectSaAqp1aen_US
dc.subjectSaAqp1ben_US
dc.subjectFunctional expressionen_US
dc.subjectSalinityen_US
dc.subjectGastrointestinal tracten_US
dc.titleDifferential localization and regulation of two aquaporin-1 homologs in the intestinal epithelia of the marine teleost Sparus aurataen_US
dc.typeartículoen_US
dc.identifier.doi10.1152/ajpregu.00695.2007-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttps://doi.org/10.1152/ajpregu.00695.2007en_US
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairetypeartículo-
item.grantfulltextopen-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
item.languageiso639-1en-
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