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dc.contributor.author
Marinelli, Raul Alberto
dc.contributor.author
Lehmann, Guillermo Luis
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Soria, Leandro Raul
dc.contributor.author
Marchissio, Maria Julia
dc.date.available
2017-04-18T17:57:10Z
dc.date.issued
2011-06
dc.identifier.citation
Marinelli, Raul Alberto; Lehmann, Guillermo Luis; Soria, Leandro Raul; Marchissio, Maria Julia; Hepatocyte aquaporins in bile formation and cholestasis; Frontiers In Bioscience Inc; Frontiers In Bioscience-landmark; 16; 7; 6-2011; 2642-2652
dc.identifier.issn
1093-9946
dc.identifier.uri
http://hdl.handle.net/11336/15378
dc.description.abstract
Bile formation by hepatocytes is an osmotic secretory process that is ultimately dependent on the biliary secretion of osmotically-active solutes (mainly bile salts) via specialized canalicular transporters as well as on the water permeability of the canalicular plasma membrane domain. Hepatocytes express aquaporins, a family of membrane channel proteins that facilitate the osmotically-driven movement of water molecules. Aquaporin-8 (AQP8), localized to canalicular membranes, modulates membrane water permeability providing a molecular mechanism for the osmotically-coupled transport of solute and water during bile formation. There is experimental evidence suggesting that defective hepatocyte AQP8 expression leads to alterations in normal bile physiology. Thus, AQP8 protein is downregulated (and canalicular water permeability decreased), in established rat models of cholestasis, such as sepsis-associated cholestasis, estrogen-induced cholestasis and extrahepatic obstructive cholestasis. Moreover, AQP8 gene silencing in the human hepatocyte-derived cell line HepG2 inhibits canalicular water secretion. Based on current knowledge, it is conceivable that cholestasis results from a mutual occurrence of impaired solute transport and AQP8-mediated decrease of canalicular water permeability.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Frontiers In Bioscience Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Aquaporins
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Water Channels
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Aquaporin-8
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Membrane Water Permeability
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Hepatocyte
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Bile Secretion
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Fisiología
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Medicina Básica
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CIENCIAS MÉDICAS Y DE LA SALUD
dc.title
Hepatocyte aquaporins in bile formation and cholestasis
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-04-18T14:03:07Z
dc.identifier.eissn
1093-4715
dc.journal.volume
16
dc.journal.number
7
dc.journal.pagination
2642-2652
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Irvine
dc.description.fil
Fil: Marinelli, Raul Alberto. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Fisiología Experimental (i); Argentina
dc.description.fil
Fil: Lehmann, Guillermo Luis. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Fisiología Experimental (i); Argentina
dc.description.fil
Fil: Soria, Leandro Raul. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Fisiología Experimental (i); Argentina
dc.description.fil
Fil: Marchissio, Maria Julia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Fisiología Experimental (i); Argentina
dc.journal.title
Frontiers In Bioscience-landmark
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.2741/3877
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.bioscience.org/2011/v16/af/3877/list.htm
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