{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T23:27:13Z","timestamp":1787614033083,"version":"build-2736575974"},"reference-count":28,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,9,1]],"date-time":"2021-09-01T00:00:00Z","timestamp":1630454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,9,1]],"date-time":"2021-09-01T00:00:00Z","timestamp":1630454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100002923","name":"Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003074","name":"Agencia Nacional de Promoci\u00f3n Cient\u00edfica y Tecnol\u00f3gica","doi-asserted-by":"publisher","award":["PICT 2015\u20130439"],"award-info":[{"award-number":["PICT 2015\u20130439"]}],"id":[{"id":"10.13039\/501100003074","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003074","name":"Agencia Nacional de Promoci\u00f3n Cient\u00edfica y Tecnol\u00f3gica","doi-asserted-by":"publisher","award":["PICT2017-3393"],"award-info":[{"award-number":["PICT2017-3393"]}],"id":[{"id":"10.13039\/501100003074","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2021,9]]},"DOI":"10.1016\/j.biochi.2021.03.016","type":"journal-article","created":{"date-parts":[[2021,3,31]],"date-time":"2021-03-31T22:30:50Z","timestamp":1617229850000},"page":"12-15","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"special_numbering":"C","title":["Aquaporin gene transfer for hepatocellular cholestasis"],"prefix":"10.1016","volume":"188","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2934-8863","authenticated-orcid":false,"given":"Julieta","family":"Marrone","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mauro","family":"Danielli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C\u00e9sar I.","family":"Gaspari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alejo M.","family":"Capiglioni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ra\u00fal A.","family":"Marinelli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2021.03.016_bib1","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1002\/j.2040-4603.2013.tb00519.x","article-title":"Bile formation and secretion","volume":"3","author":"Boyer","year":"2013","journal-title":"Comp. Physiol."},{"key":"10.1016\/j.biochi.2021.03.016_bib2","series-title":"Aquaporins in Health and Disease: New Molecular Targets for Drug Discovery","first-page":"183","article-title":"Hepatobiliary, salivary glands and pancreatic aquaporins in health and disease","author":"Calamita","year":"2016"},{"key":"10.1016\/j.biochi.2021.03.016_bib3","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1124\/jpet.119.261115","article-title":"Hepatic bile formation: canalicular osmolarity and paracellular and transcellular water flow","volume":"371","author":"Marinelli","year":"2019","journal-title":"J.\u00a0Pharmacol. Exp. Therapeut."},{"key":"10.1016\/j.biochi.2021.03.016_bib4","first-page":"2642","article-title":"Hepatocyte aquaporins in bile formation and cholestasis","author":"Marinelli","year":"2012","journal-title":"Front. Biosci."},{"key":"10.1016\/j.biochi.2021.03.016_bib5","doi-asserted-by":"crossref","first-page":"G905","DOI":"10.1152\/ajpgi.00386.2006","article-title":"Defective hepatocyte aquaporin-8 expression and reduced canalicular membrane water permeability in estrogen-induced cholestasis","author":"Carreras","year":"2007","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"10.1016\/j.biochi.2021.03.016_bib6","doi-asserted-by":"crossref","first-page":"G567","DOI":"10.1152\/ajpgi.00232.2007","article-title":"LPS induces the TNF-mediated down-regulation of rat liver aquaporin-8: role in sepsis-associated cholestasis","volume":"294","author":"Lehmann","year":"2008","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"10.1016\/j.biochi.2021.03.016_bib7","doi-asserted-by":"crossref","first-page":"1426","DOI":"10.1194\/jlr.M400412-JLR200","article-title":"Membrane microdomains in hepatocytes: potential target areas for proteins involved in canalicular bile secretion","volume":"46","author":"Tietz","year":"2005","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.biochi.2021.03.016_bib8","doi-asserted-by":"crossref","first-page":"1673","DOI":"10.1002\/hep.22807","article-title":"ABC-transporters are localized in caveolin-1-positive and reggie-1-negative and reggie-2-negative microdomains of the canalicular membrane in rat hepatocytes","author":"Ismair","year":"2009","journal-title":"Hepatology"},{"key":"10.1016\/j.biochi.2021.03.016_bib9","doi-asserted-by":"crossref","first-page":"1072","DOI":"10.1016\/j.bbadis.2018.01.015","article-title":"Mechanisms of canalicular transporter endocytosis in the cholestatic rat liver","volume":"1864","author":"Miszczuk","year":"2018","journal-title":"Biochim. Biophys. Acta (BBA) - Mol. Basis Dis."},{"key":"10.1016\/j.biochi.2021.03.016_bib10","doi-asserted-by":"crossref","first-page":"1878","DOI":"10.1124\/dmd.108.024778","article-title":"Effect of membrane cholesterol on BSEP\/ABCB11 activity: species specificity studiesfor substrates and inhibitors","volume":"37","author":"Kis","year":"2009","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.biochi.2021.03.016_bib11","doi-asserted-by":"crossref","first-page":"9947","DOI":"10.1074\/jbc.M808667200","article-title":"Activity of the bile salt export pump (ABCB11) is critically dependent on canalicular membrane cholesterol content","author":"Paulusma","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2021.03.016_bib12","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1124\/mol.114.092262","article-title":"Differential effects of membrane cholesterol content on the transport activity of multidrug resistance-associated protein 2 (ABCC2) and of the bile salt export pump (ABCB11)","volume":"85","author":"Guyot","year":"2014","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.biochi.2021.03.016_bib13","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1038\/gt.2014.78","article-title":"Adenoviral transfer of human aquaporin-1 gene to rat liver improves bile flow in estrogen-induced cholestasis","volume":"21","author":"Marrone","year":"2014","journal-title":"Gene Ther."},{"key":"10.1016\/j.biochi.2021.03.016_bib14","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1002\/hep.28564","article-title":"Hepatic gene transfer of human aquaporin-1 improves bile acid secretory failure in rats with estrogen-induced cholestasis","volume":"64","author":"Marrone","year":"2016","journal-title":"Hepatology"},{"key":"10.1016\/j.biochi.2021.03.016_bib15","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1002\/iub.1689","article-title":"Adenovirus-mediated human aquaporin-1 expression in hepatocytes improves lipopolysaccharide-induced cholestasis","volume":"69","author":"Marrone","year":"2017","journal-title":"IUBMB Life"},{"key":"10.1016\/j.biochi.2021.03.016_bib16","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.biochi.2019.07.027","article-title":"Improved hepatic MRP2\/ABCC2 transport activity in LPS-induced cholestasis by aquaporin-1 gene transfer","volume":"165","author":"Marrone","year":"2019","journal-title":"Biochimie"},{"key":"10.1016\/j.biochi.2021.03.016_bib17","doi-asserted-by":"crossref","first-page":"3268","DOI":"10.1073\/pnas.94.7.3268","article-title":"Increased fluid secretion after adenoviral-mediated transfer of the aquaporin-1cDNA to irradiated rat salivary glands","volume":"94","author":"Delporte","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.biochi.2021.03.016_bib18","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.ymthe.2004.11.007","article-title":"Increased fluid secretion after adenoviral-mediated transfer of the human aquaporin-1 cDNA to irradiated miniature pig parotid glands","volume":"11","author":"Shan","year":"2005","journal-title":"Mol. Ther."},{"key":"10.1016\/j.biochi.2021.03.016_bib19","doi-asserted-by":"crossref","first-page":"19403","DOI":"10.1073\/pnas.1210662109","article-title":"Early responses to adenoviral-mediated transfer of the aquaporin-1 cDNA for radiation-induced salivary hypofunction","volume":"109","author":"Baum","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.biochi.2021.03.016_bib20","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1016\/j.molmed.2016.08.007","article-title":"Caveolin-1 function in liver physiology and disease","volume":"22","author":"Fernandez-Rojo","year":"2016","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.biochi.2021.03.016_bib21","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1016\/j.bbalip.2014.02.002","article-title":"Caveolin-1 interacts with ATP binding cassette transporter G1 (ABCG1) and regulates ABCG1-mediated cholesterol efflux","volume":"1841","author":"Gu","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2021.03.016_bib22","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1042\/BC20040131","article-title":"The potential role of caveolin-1 inhibition of aquaporins during the AVD","volume":"98","author":"Jablonski","year":"2006","journal-title":"Biol. Cell."},{"key":"10.1016\/j.biochi.2021.03.016_bib23","doi-asserted-by":"crossref","first-page":"6525","DOI":"10.1074\/jbc.272.10.6525","article-title":"Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins","volume":"272","author":"Couet","year":"1997","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2021.03.016_bib24","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1016\/j.hep.2003.09.011","article-title":"Hepatic overexpression of caveolins increases bile salt secretion in mice","volume":"38","author":"Moreno","year":"2003","journal-title":"Hepatology"},{"key":"10.1016\/j.biochi.2021.03.016_bib25","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1124\/jpet.107.122994","article-title":"Localization of the human breast cancer resistance protein (BCRP\/ABCG2) inlipid rafts\/caveolae and modulation of its activity by cholesterol in\u00a0vitro","volume":"323","author":"Storch","year":"2007","journal-title":"J.\u00a0Pharmacol. Exp. Therapeut."},{"key":"10.1016\/j.biochi.2021.03.016_bib26","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1080\/15216540500104750","article-title":"Evidence for rat organic anion transporter 3 association with caveolin-1 in rat kidney","volume":"57","author":"Kwak","year":"2005","journal-title":"IUBMB Life"},{"key":"10.1016\/j.biochi.2021.03.016_bib27","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1016\/j.bbrc.2008.05.012","article-title":"Regulation of brain endothelial cells migration and angiogenesis by P-glycoprotein\/caveolin-1 interaction","author":"Barakat","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2021.03.016_bib28","doi-asserted-by":"crossref","first-page":"3255","DOI":"10.1113\/jphysiol.2010.194779","article-title":"Interaction with caveolin-1 modulates vascular ATP-sensitive potassium (KATP) channel activity","volume":"588","author":"Davies","year":"2010","journal-title":"J.\u00a0Physiol."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908421000869?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908421000869?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:18:35Z","timestamp":1759540715000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908421000869"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,9]]},"references-count":28,"alternative-id":["S0300908421000869"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2021.03.016","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2021,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Aquaporin gene transfer for hepatocellular cholestasis","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2021.03.016","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier B.V. and Soci\u00e9t\u00e9 Fran\u00e7aise de Biochimie et Biologie Mol\u00e9culaire (SFBBM). All rights reserved.","name":"copyright","label":"Copyright"}]}}