The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts

Water homeostasis and the structural integrity of the vertebrate lens is partially mediated by AQP0 channels. Emerging evidence indicates that external pH may be involved in channel gating. Here we show that a tetraploid teleost, the Atlantic salmon, retains 4 aqp0 genes (aqp0a1, -0a2, -0b1, and -0b...

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Detalles Bibliográficos
Autores: Chauvigné, François, Zapater, Cinta, Stavang, Jon Anders, Taranger, Geir Lasse, Cerdà, Joan, Finn, Roderick Nigel
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:20.500.12327/2239
Acceso en línea:http://hdl.handle.net/20.500.12327/2239
https://doi.org/10.1096/fj.14-267625
Access Level:acceso abierto
Palabra clave:639
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oai_identifier_str oai:recercat.cat:20.500.12327/2239
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repository_id_str
spelling The pH sensitivity of Aqp0 channels in tetraploid and diploid teleostsChauvigné, FrançoisZapater, CintaStavang, Jon AndersTaranger, Geir LasseCerdà, JoanFinn, Roderick Nigel639Water homeostasis and the structural integrity of the vertebrate lens is partially mediated by AQP0 channels. Emerging evidence indicates that external pH may be involved in channel gating. Here we show that a tetraploid teleost, the Atlantic salmon, retains 4 aqp0 genes (aqp0a1, -0a2, -0b1, and -0b2), which are highly, but not exclusively, expressed in the lens. Functional characterization reveals that,although each paralog permeateswater efficiently, the permeability is respectively shifted to the neutral, alkaline, or acidic pH in Aqp0a1, -0a2, and -0b1, whereas that of Aqp0b2 is not regulated by external pH. Mutagenesis studies demonstrate that Ser38, His39, and His40 residues in the extracellular transmembrane domain of a-helix 2 facing the water pore are critical for the pH modulation of water transport. To validate these findings, we show that both zebrafish Aqp0a and -0b are functional water channels with respective pH sensitivities toward alkaline or acid pH ranges and that an N-terminal allelic variant (Ser19) of Aqp0b exists that abolishes water transport in Xenopus laevis oocytes. The data suggest that the alkaline pH sensitivity is a conserved trait in teleost Aqp0 a-type channels, whereas mammalian AQP0 and some teleost Aqp0 b-type channels display an acidic pH permeation preference.info:eu-repo/semantics/publishedVersionWiley Open AccessProducció AnimalAqüicultura2015info:eu-repo/semantics/article13http://hdl.handle.net/20.500.12327/2239https://doi.org/10.1096/fj.14-267625reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésFASEB JournalMICINN/Programa Nacional de Proyectos de Investigación Fundamental/AGL2010-15597/ES/AQUAPORINAS TESTICULARES DURANTE LA ESPERMATOGENESIS DE PECES MARINOS Y LA ACTIVACION Y PERMEABILIDAD ESPERMATICA/Attribution-NonCommercial 4.0 Internationalhttp://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccessoai:recercat.cat:20.500.12327/22392026-05-29T05:05:01Z
dc.title.none.fl_str_mv The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts
title The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts
spellingShingle The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts
Chauvigné, François
639
title_short The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts
title_full The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts
title_fullStr The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts
title_full_unstemmed The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts
title_sort The pH sensitivity of Aqp0 channels in tetraploid and diploid teleosts
dc.creator.none.fl_str_mv Chauvigné, François
Zapater, Cinta
Stavang, Jon Anders
Taranger, Geir Lasse
Cerdà, Joan
Finn, Roderick Nigel
author Chauvigné, François
author_facet Chauvigné, François
Zapater, Cinta
Stavang, Jon Anders
Taranger, Geir Lasse
Cerdà, Joan
Finn, Roderick Nigel
author_role author
author2 Zapater, Cinta
Stavang, Jon Anders
Taranger, Geir Lasse
Cerdà, Joan
Finn, Roderick Nigel
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Producció Animal
Aqüicultura
dc.subject.none.fl_str_mv 639
topic 639
description Water homeostasis and the structural integrity of the vertebrate lens is partially mediated by AQP0 channels. Emerging evidence indicates that external pH may be involved in channel gating. Here we show that a tetraploid teleost, the Atlantic salmon, retains 4 aqp0 genes (aqp0a1, -0a2, -0b1, and -0b2), which are highly, but not exclusively, expressed in the lens. Functional characterization reveals that,although each paralog permeateswater efficiently, the permeability is respectively shifted to the neutral, alkaline, or acidic pH in Aqp0a1, -0a2, and -0b1, whereas that of Aqp0b2 is not regulated by external pH. Mutagenesis studies demonstrate that Ser38, His39, and His40 residues in the extracellular transmembrane domain of a-helix 2 facing the water pore are critical for the pH modulation of water transport. To validate these findings, we show that both zebrafish Aqp0a and -0b are functional water channels with respective pH sensitivities toward alkaline or acid pH ranges and that an N-terminal allelic variant (Ser19) of Aqp0b exists that abolishes water transport in Xenopus laevis oocytes. The data suggest that the alkaline pH sensitivity is a conserved trait in teleost Aqp0 a-type channels, whereas mammalian AQP0 and some teleost Aqp0 b-type channels display an acidic pH permeation preference.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12327/2239
https://doi.org/10.1096/fj.14-267625
url http://hdl.handle.net/20.500.12327/2239
https://doi.org/10.1096/fj.14-267625
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv FASEB Journal
MICINN/Programa Nacional de Proyectos de Investigación Fundamental/AGL2010-15597/ES/AQUAPORINAS TESTICULARES DURANTE LA ESPERMATOGENESIS DE PECES MARINOS Y LA ACTIVACION Y PERMEABILIDAD ESPERMATICA/
dc.rights.none.fl_str_mv Attribution-NonCommercial 4.0 International
http://creativecommons.org/licenses/by-nc/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv Attribution-NonCommercial 4.0 International
http://creativecommons.org/licenses/by-nc/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 13
dc.publisher.none.fl_str_mv Wiley Open Access
publisher.none.fl_str_mv Wiley Open Access
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869413406540300288
score 15.811543

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