Hepatocyte aquaporins in bile physiology and disease

Autores
Marinelli, Raúl A.; Marrone, Julieta; Soria, Leandro R.
Año de publicación
2016
Idioma
inglés
Tipo de recurso
reseña artículo
Estado
versión publicada
Descripción
Bile formation by hepatocytes is an osmotic secretory process resulting from the canalicular secretion of water in response to osmotic gradients created by the active transport of solutes, primarily bile salts, and other organic anions. Thus bile secretion would be ultimately dependent on the canalicular expression of bile salt and organic anion transporters as well as the osmotic water permeability of the canalicular plasma membrane domain, mainly determined by aquaporin-8 (AQP8) water channels. Compelling experimental evidence suggests that canalicular AQP8 facilitates the osmotically-coupled transport of solute and water during the formation of bile. Downregulation of AQP8-mediated hepatocyte canalicular water permeability is found in rat models of hepatocellular cholestasis suggesting that defective hepatocyte AQP8 expression is involved in the molecular mechanisms of bile secretory failure. The study of AQP function in liver has provided new insights into normal bile physiology and disease mechanisms, and may yield novel therapies to improve certain cholestatic conditions.
Sociedad Argentina de Fisiología
Materia
Ciencias Médicas
Aquaporin water channels
Hepatocytes
Bile secretion
Cholestasis
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/127642
Acceder
id SEDICI_2448a0c5bb50c193ea680c3e6b7cb411
oai_identifier_str oai:sedici.unlp.edu.ar:10915/127642
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Hepatocyte aquaporins in bile physiology and diseaseMarinelli, Raúl A.Marrone, JulietaSoria, Leandro R.Ciencias MédicasAquaporin water channelsHepatocytesBile secretionCholestasisBile formation by hepatocytes is an osmotic secretory process resulting from the canalicular secretion of water in response to osmotic gradients created by the active transport of solutes, primarily bile salts, and other organic anions. Thus bile secretion would be ultimately dependent on the canalicular expression of bile salt and organic anion transporters as well as the osmotic water permeability of the canalicular plasma membrane domain, mainly determined by aquaporin-8 (AQP8) water channels. Compelling experimental evidence suggests that canalicular AQP8 facilitates the osmotically-coupled transport of solute and water during the formation of bile. Downregulation of AQP8-mediated hepatocyte canalicular water permeability is found in rat models of hepatocellular cholestasis suggesting that defective hepatocyte AQP8 expression is involved in the molecular mechanisms of bile secretory failure. The study of AQP function in liver has provided new insights into normal bile physiology and disease mechanisms, and may yield novel therapies to improve certain cholestatic conditions.Sociedad Argentina de Fisiología2016-02info:eu-repo/semantics/reviewinfo:eu-repo/semantics/publishedVersionRevisionhttp://purl.org/coar/resource_type/c_dcae04bcinfo:ar-repo/semantics/resenaArticuloapplication/pdf1-8http://sedici.unlp.edu.ar/handle/10915/127642enginfo:eu-repo/semantics/altIdentifier/url/https://pmr.safisiol.org.ar/archive/id/82info:eu-repo/semantics/altIdentifier/issn/1669-5410info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-10T12:33:31Zoai:sedici.unlp.edu.ar:10915/127642Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-10 12:33:31.835SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Hepatocyte aquaporins in bile physiology and disease
title Hepatocyte aquaporins in bile physiology and disease
spellingShingle Hepatocyte aquaporins in bile physiology and disease
Marinelli, Raúl A.
Ciencias Médicas
Aquaporin water channels
Hepatocytes
Bile secretion
Cholestasis
title_short Hepatocyte aquaporins in bile physiology and disease
title_full Hepatocyte aquaporins in bile physiology and disease
title_fullStr Hepatocyte aquaporins in bile physiology and disease
title_full_unstemmed Hepatocyte aquaporins in bile physiology and disease
title_sort Hepatocyte aquaporins in bile physiology and disease
dc.creator.none.fl_str_mv Marinelli, Raúl A.
Marrone, Julieta
Soria, Leandro R.
author Marinelli, Raúl A.
author_facet Marinelli, Raúl A.
Marrone, Julieta
Soria, Leandro R.
author_role author
author2 Marrone, Julieta
Soria, Leandro R.
author2_role author
author
dc.subject.none.fl_str_mv Ciencias Médicas
Aquaporin water channels
Hepatocytes
Bile secretion
Cholestasis
topic Ciencias Médicas
Aquaporin water channels
Hepatocytes
Bile secretion
Cholestasis
dc.description.none.fl_txt_mv Bile formation by hepatocytes is an osmotic secretory process resulting from the canalicular secretion of water in response to osmotic gradients created by the active transport of solutes, primarily bile salts, and other organic anions. Thus bile secretion would be ultimately dependent on the canalicular expression of bile salt and organic anion transporters as well as the osmotic water permeability of the canalicular plasma membrane domain, mainly determined by aquaporin-8 (AQP8) water channels. Compelling experimental evidence suggests that canalicular AQP8 facilitates the osmotically-coupled transport of solute and water during the formation of bile. Downregulation of AQP8-mediated hepatocyte canalicular water permeability is found in rat models of hepatocellular cholestasis suggesting that defective hepatocyte AQP8 expression is involved in the molecular mechanisms of bile secretory failure. The study of AQP function in liver has provided new insights into normal bile physiology and disease mechanisms, and may yield novel therapies to improve certain cholestatic conditions.
Sociedad Argentina de Fisiología
description Bile formation by hepatocytes is an osmotic secretory process resulting from the canalicular secretion of water in response to osmotic gradients created by the active transport of solutes, primarily bile salts, and other organic anions. Thus bile secretion would be ultimately dependent on the canalicular expression of bile salt and organic anion transporters as well as the osmotic water permeability of the canalicular plasma membrane domain, mainly determined by aquaporin-8 (AQP8) water channels. Compelling experimental evidence suggests that canalicular AQP8 facilitates the osmotically-coupled transport of solute and water during the formation of bile. Downregulation of AQP8-mediated hepatocyte canalicular water permeability is found in rat models of hepatocellular cholestasis suggesting that defective hepatocyte AQP8 expression is involved in the molecular mechanisms of bile secretory failure. The study of AQP function in liver has provided new insights into normal bile physiology and disease mechanisms, and may yield novel therapies to improve certain cholestatic conditions.
publishDate 2016
dc.date.none.fl_str_mv 2016-02
dc.type.none.fl_str_mv info:eu-repo/semantics/review
info:eu-repo/semantics/publishedVersion
Revision
http://purl.org/coar/resource_type/c_dcae04bc
info:ar-repo/semantics/resenaArticulo
format review
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/127642
url http://sedici.unlp.edu.ar/handle/10915/127642
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://pmr.safisiol.org.ar/archive/id/82
info:eu-repo/semantics/altIdentifier/issn/1669-5410
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
1-8
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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