{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,28]],"date-time":"2026-01-28T08:02:01Z","timestamp":1769587321923,"version":"3.49.0"},"reference-count":136,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2016,7,9]],"date-time":"2016-07-09T00:00:00Z","timestamp":1468022400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Aquaporins (AQPs) are proteinaceous channels widespread in nature where they allow facilitated permeation of water and uncharged through cellular membranes. AQPs play a number of important roles in both health and disease. This review focuses on the most recent advances and research trends regarding the expression and modulation, as well as physiological and pathophysiological functions of AQPs in hepatocytes and Sertoli cells (SCs). Besides their involvement in bile formation, hepatocyte AQPs are involved in maintaining energy balance acting in hepatic gluconeogenesis and lipid metabolism, and in critical processes such as ammonia detoxification and mitochondrial output of hydrogen peroxide. Roles are played in clinical disorders including fatty liver disease, diabetes, obesity, cholestasis, hepatic cirrhosis and hepatocarcinoma. In the seminiferous tubules, particularly in SCs, AQPs are also widely expressed and seem to be implicated in the various stages of spermatogenesis. Like in hepatocytes, AQPs may be involved in maintaining energy homeostasis in these cells and have a major role in the metabolic cooperation established in the testicular tissue. Altogether, this information represents the mainstay of current and future investigation in an expanding field.<\/jats:p>","DOI":"10.3390\/ijms17071096","type":"journal-article","created":{"date-parts":[[2016,7,11]],"date-time":"2016-07-11T09:47:19Z","timestamp":1468230439000},"page":"1096","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["Hepatocyte and Sertoli Cell Aquaporins, Recent Advances and Research Trends"],"prefix":"10.3390","volume":"17","author":[{"given":"Raquel","family":"Bernardino","sequence":"first","affiliation":[{"name":"Department of Microscopy, Laboratory of Cell Biology, Institute of Biomedical Sciences Abel Salazar (ICBAS) and Unit for Multidisciplinary Research in Biomedicine (UMIB), University of Porto, 4050-313 Porto, Portugal"}]},{"given":"Raul","family":"Marinelli","sequence":"additional","affiliation":[{"name":"Instituto de Fisiolog\u00eda Experimental-CONICET, Facultad de Ciencias Bioqu\u00edmicas y Farmac\u00e9uticas-Universidad Nacional de Rosario, 531 S2002LRK Rosario, Santa Fe, Argentina"}]},{"given":"Anna","family":"Maggio","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Biotechnologies and Biopharnaceutics, University of Bari \u201c<i>Aldo Moro<\/i>\u201d, 70125 Bari, Italy"}]},{"given":"Patrizia","family":"Gena","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Biotechnologies and Biopharnaceutics, University of Bari \u201c<i>Aldo Moro<\/i>\u201d, 70125 Bari, Italy"}]},{"given":"Ilaria","family":"Cataldo","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Biotechnologies and Biopharnaceutics, University of Bari \u201c<i>Aldo Moro<\/i>\u201d, 70125 Bari, Italy"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7635-783X","authenticated-orcid":false,"given":"Marco","family":"Alves","sequence":"additional","affiliation":[{"name":"CICS-UBI, Health Sciences Research Centre, University of Beira Interior, 6201-506 Covilh\u00e3, Portugal"}]},{"given":"Maria","family":"Svelto","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Biotechnologies and Biopharnaceutics, University of Bari \u201c<i>Aldo Moro<\/i>\u201d, 70125 Bari, Italy"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4989-5699","authenticated-orcid":false,"given":"Pedro","family":"Oliveira","sequence":"additional","affiliation":[{"name":"Department of Microscopy, Laboratory of Cell Biology, Institute of Biomedical Sciences Abel Salazar (ICBAS) and Unit for Multidisciplinary Research in Biomedicine (UMIB), University of Porto, 4050-313 Porto, Portugal"},{"name":"Instituto de Investiga\u00e7\u00e3o e Inova\u00e7\u00e3o em Sa\u00fade, Universidade do Porto, 4200-135 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4666-9546","authenticated-orcid":false,"given":"Giuseppe","family":"Calamita","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Biotechnologies and Biopharnaceutics, University of Bari \u201c<i>Aldo Moro<\/i>\u201d, 70125 Bari, Italy"}]}],"member":"1968","published-online":{"date-parts":[[2016,7,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"4278","DOI":"10.1002\/anie.200460804","article-title":"Aquaporin water channels (Nobel Lecture)","volume":"43","author":"Agre","year":"2004","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1126\/science.256.5055.385","article-title":"Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein","volume":"256","author":"Preston","year":"1992","journal-title":"Science"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1111\/eci.12621","article-title":"The power of Science Diplomacy, a lesson from the Nobel Laureate Peter Agre","volume":"46","author":"Calamita","year":"2016","journal-title":"Eur. J. Clin. Investig."},{"key":"ref_4","unstructured":"Soveral, G., Casini, A., and Nielsen, S. (2015). Aquaporins in Health and Disease: New Molecular Targets for Drug Discovery, CRC Press Taylor & Francis Group. Chapter 9."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"2642","DOI":"10.2741\/3877","article-title":"Hepatocyte aquaporins in bile formation and cholestasis","volume":"17","author":"Marinelli","year":"2011","journal-title":"Front. Biosci. (Landmark Ed.)"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1078\/0171-9335-00210","article-title":"Expression and immunolocalization of the aquaporin-8 water channel in rat gastrointestinal tract","volume":"80","author":"Calamita","year":"2001","journal-title":"Eur. J. Cell Biol."},{"key":"ref_7","first-page":"F1047","article-title":"Immunolocalization of aquaporin-8 in rat kidney, gastrointestinal tract, testis, and airways","volume":"281","author":"Elkjaer","year":"2001","journal-title":"Am. J. Physiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"12147","DOI":"10.1074\/jbc.M009403200","article-title":"The water channel aquaporin-8 is mainly intracellular in rat hepatocytes, and its plasma membrane insertion is stimulated by cyclic AMP","volume":"276","author":"Kierbel","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1002\/hep.1840380421","article-title":"Ontogeny, distribution, and possible functional implications of an unusual aquaporin, AQP8, in mouse liver","volume":"38","author":"Ferri","year":"2003","journal-title":"Hepatology"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"17149","DOI":"10.1074\/jbc.C400595200","article-title":"The inner mitochondrial membrane has aquaporin-8 water channels and is highly permeable to water","volume":"280","author":"Calamita","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1053\/jhep.2003.50241","article-title":"Glucagon induces the plasma membrane insertion of functional aquaporin-8 water channels in isolated rat hepatocytes","volume":"37","author":"Gradilone","year":"2003","journal-title":"Hepatology"},{"key":"ref_12","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. Lipid Res."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1002\/hep.21039","article-title":"Isolation and characterization of lipid microdomains from apical and basolateral plasma membranes of rat hepatocytes","volume":"43","author":"Mazzone","year":"2006","journal-title":"Hepatology"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1042\/BC20040115","article-title":"Phosphoinositide 3-kinase is involved in the glucagon-induced translocation of aquaporin-8 to hepatocyte plasma membrane","volume":"97","author":"Gradilone","year":"2005","journal-title":"Biol. Cell"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"R1274","DOI":"10.1152\/ajpregu.90783.2008","article-title":"Glucagon induces the gene expression of aquaporin-8 but not that of aquaporin-9 water channels in the rat hepatocyte","volume":"296","author":"Soria","year":"2009","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.mam.2012.03.010","article-title":"Water channel proteins in bile formation and flow in health and disease: When immiscible becomes miscible","volume":"33","author":"Portincasa","year":"2012","journal-title":"Mol. Asp. Med."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1018","DOI":"10.1016\/j.bbamem.2006.07.008","article-title":"Water permeability of rat liver mitochondria: A biophysical study","volume":"1758","author":"Calamita","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"16202","DOI":"10.1074\/jbc.M601864200","article-title":"Evidence against functionally significant aquaporin expression in mitochondria","volume":"281","author":"Yang","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_19","first-page":"352","article-title":"News and views on mitochondrial water transport","volume":"1","author":"Gena","year":"2009","journal-title":"Front. Biosci."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"5296","DOI":"10.1074\/jbc.M609343200","article-title":"Fast and selective ammonia transport by aquaporin-8","volume":"282","author":"Saparov","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1074\/jbc.M603761200","article-title":"Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes","volume":"282","author":"Bienert","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2061","DOI":"10.1002\/hep.26236","article-title":"Ammonia detoxification via ureagenesis in rat hepatocytes involves mitochondrial aquaporin-8 channels","volume":"57","author":"Soria","year":"2013","journal-title":"Hepatology"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.taap.2012.08.005","article-title":"Mitochondrial aquaporin-8 knockdown in human hepatoma HepG2 cells causes ROS-induced mitochondrial depolarization and loss of viability","volume":"264","author":"Marchissio","year":"2012","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1089\/ars.2013.5505","article-title":"Mitochondrial aquaporin-8: A functional peroxiporin?","volume":"19","author":"Marinelli","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1006\/bbrc.2000.3505","article-title":"Immunolocalization of AQP9 in liver, epididymis, testis, spleen, and brain","volume":"276","author":"Elkjaer","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2945","DOI":"10.1073\/pnas.0437994100","article-title":"Aquaglyceroporin AQP9: Solute permeation and metabolic control of expression in liver","volume":"100","author":"Carbrey","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_27","first-page":"1","article-title":"Sexual Dimorphism of Adipose and Hepatic Aquaglyceroporins in Health and Metabolic Disorders","volume":"6","author":"Marinelli","year":"2015","journal-title":"Front. Endocrinol. (Lausanne)"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1177\/002215540104901208","article-title":"Tissue distribution and membrane localization of aquaporin-9 water channel: Evidence for sex-linked differences in liver","volume":"49","author":"Nicchia","year":"2001","journal-title":"J. Histochem. Cytochem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"G365","DOI":"10.1152\/ajpgi.00437.2011","article-title":"Estrogen prevents increased hepatic aquaporin-9 expression and glycerol uptake during starvation","volume":"302","author":"Lebeck","year":"2012","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"44319","DOI":"10.1074\/jbc.M111.297002","article-title":"Aquaporin-9 protein is the primary route of hepatocyte glycerol uptake for glycerol gluconeogenesis in mice","volume":"286","author":"Jelen","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1111\/boc.201100061","article-title":"Biophysical assessment of aquaporin-9 as principal facilitative pathway in mouse liver import of glucogenetic glycerol","volume":"104","author":"Calamita","year":"2012","journal-title":"Biol. Cell"},{"key":"ref_32","first-page":"G1279","article-title":"Aquaporin-9 and urea transporter-A gene deletions affect urea transmembrane passage in murine hepatocytes","volume":"303","author":"Jelen","year":"2012","journal-title":"Am. J. Physiol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"15956","DOI":"10.1073\/pnas.0908108106","article-title":"Reduced arsenic clearance and increased toxicity in aquaglyceroporin-9-null mice","volume":"106","author":"Carbrey","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.bbrc.2016.01.153","article-title":"Aquaporin-9 facilitates membrane transport of hydrogen peroxide in mammalian cells","volume":"471","author":"Watanabe","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1016\/j.bbagen.2013.10.039","article-title":"The role of mammalian superaquaporins inside the cell","volume":"1840","author":"Ishibashi","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"30413","DOI":"10.1074\/jbc.R300017200","article-title":"Glyceroneogenesis and the triglyceride\/fatty acid cycle","volume":"278","author":"Reshef","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/j.cam.2015.01.036","article-title":"A model for the hepatic glucose metabolism based on Hill and step functions","volume":"292","author":"Gena","year":"2016","journal-title":"J. Comput. Appl. Math."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1172\/JCI200420468","article-title":"PPAR\u03b1 governs glycerol metabolism","volume":"114","author":"Patsouris","year":"2004","journal-title":"J. Clin. Investig."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"G198","DOI":"10.1152\/ajpgi.00407.2013","article-title":"Hepatic AQP9 expression in male rats is reduced in response to PPAR\u03b1 agonist treatment","volume":"308","author":"Lebeck","year":"2015","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"3609","DOI":"10.1073\/pnas.0610894104","article-title":"Defective glycerol metabolism in aquaporin 9 (AQP9) knockout mice","volume":"104","author":"Rojek","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2915","DOI":"10.2337\/diabetes.51.10.2915","article-title":"Coordinated regulation of fat-specific and liver-specific glycerol channels, aquaporin adipose and aquaporin 9","volume":"51","author":"Kuriyama","year":"2002","journal-title":"Diabetes"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1038\/ijo.2013.234","article-title":"Reduced hepatic aquaporin-9 and glycerol permeability are related to insulin resistance in non-alcoholic fatty liver disease","volume":"38","author":"Gena","year":"2014","journal-title":"Int. J. Obes."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"E586","DOI":"10.1210\/jc.2010-1408","article-title":"Insulin- and leptin-mediated control of aquaglyceroporins in human adipocytes and hepatocytes is mediated via the PI3K\/Akt\/mTOR signaling cascade","volume":"96","author":"Catalan","year":"2011","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.abb.2011.08.002","article-title":"AMP-activated protein kinase modulates the gene expression of aquaporin 9 via forkhead box a2","volume":"515","author":"Yokoyama","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1762","DOI":"10.1016\/j.metabol.2009.06.004","article-title":"Gene expression of paired abdominal adipose AQP7 and liver AQP9 in patients with morbid obesity: relationship with glucose abnormalities","volume":"58","author":"Miranda","year":"2009","journal-title":"Metabolism"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.mce.2014.06.017","article-title":"Aquaglyceroporins and caveolins in energy and metabolic homeostasis","volume":"397","author":"Balaguer","year":"2014","journal-title":"Mol. Cell. Endocrinol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.4161\/cc.10.10.15672","article-title":"Aquaglyceroporins serve as metabolic gateways in adiposity and insulin resistance control","volume":"10","year":"2011","journal-title":"Cell Cycle"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"R165","DOI":"10.1530\/JME-13-0268","article-title":"Metabolic impact of the glycerol channels AQP7 and AQP9 in adipose tissue and liver","volume":"52","author":"Lebeck","year":"2014","journal-title":"J. Mol. Endocrinol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1007\/s00424-005-1399-1","article-title":"NH3 and NH4 permeability in aquaporin-expressing Xenopus oocytes","volume":"450","author":"Holm","year":"2005","journal-title":"Pflugers Arch."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.febslet.2004.08.004","article-title":"Aquaporin homologues in plants and mammals transport ammonia","volume":"574","author":"Jahn","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1042\/BC20050026","article-title":"Purification and functional characterization of aquaporin-8","volume":"98","author":"Liu","year":"2006","journal-title":"Biol. Cell"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"C417","DOI":"10.1152\/ajpcell.00057.2006","article-title":"Evidence from knockout mice against physiologically significant aquaporin 8-facilitated ammonia transport","volume":"291","author":"Yang","year":"2006","journal-title":"Am. J. Physiol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.bbrc.2010.01.104","article-title":"Aquaporin-8-facilitated mitochondrial ammonia transport","volume":"393","author":"Soria","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1677\/JOE-06-0058","article-title":"Triiodothyronine modulates the expression of aquaporin-8 in rat liver mitochondria","volume":"192","author":"Calamita","year":"2007","journal-title":"J. Endocrinol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1016\/j.febslet.2014.03.012","article-title":"Lipopolysaccharide impairs hepatocyte ureagenesis from ammonia: Involvement of mitochondrial aquaporin-8","volume":"588","author":"Soria","year":"2014","journal-title":"FEBS Lett."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1002\/cphy.c120027","article-title":"Bile formation and secretion","volume":"3","author":"Boyer","year":"2013","journal-title":"Compr. Physiol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"22710","DOI":"10.1074\/jbc.M202394200","article-title":"Expression and localization of aquaporin water channels in rat hepatocytes. Evidence for a role in canalicular bile secretion","volume":"277","author":"Huebert","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"G93","DOI":"10.1152\/ajpgi.90410.2008","article-title":"Knockdown of hepatocyte aquaporin-8 by RNA interference induces defective bile canalicular water transport","volume":"296","author":"Larocca","year":"2009","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"43157","DOI":"10.1074\/jbc.M305899200","article-title":"Water transporting properties of hepatocyte basolateral and canalicular plasma membrane domains","volume":"278","author":"Marinelli","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1042\/CS20120633","article-title":"Endothelin-1 and -3 induce choleresis in the rat through ETB receptors coupled to nitric oxide and vagovagal reflexes","volume":"125","author":"Rodriguez","year":"2013","journal-title":"Clin. Sci. (Lond.)"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1089\/ars.2010.3363","article-title":"Mitochondrial ROS generation and its regulation: Mechanisms involved in H2O2 signaling","volume":"14","author":"Rigoulet","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"15681","DOI":"10.1073\/pnas.1005776107","article-title":"Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signalling","volume":"107","author":"Miller","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"8735","DOI":"10.1074\/jbc.R113.544635","article-title":"Role of metabolic H2O2 generation: Redox signaling and oxidative stress","volume":"289","author":"Sies","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1007\/s10495-014-0966-3","article-title":"Evidence for necrosis, but not apoptosis, in human hepatoma cells with knockdown of mitochondrial aquaporin-8","volume":"19","author":"Marchissio","year":"2014","journal-title":"Apoptosis"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1053\/j.gastro.2012.04.001","article-title":"The diagnosis and management of non-alcoholic fatty liver disease: Practice guideline by the American Gastroenterological Association, American Association for the Study of Liver Diseases, and American College of Gastroenterology","volume":"142","author":"Chalasani","year":"2012","journal-title":"Gastroenterology"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1146\/annurev-pathol-121808-102132","article-title":"Nonalcoholic fatty liver disease: Pathology and pathogenesis","volume":"5","author":"Tiniakos","year":"2010","journal-title":"Annu. Rev. Pathol."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Gena, P., Mastrodonato, M., Portincasa, P., Fanelli, E., Mentino, D., Rodr\u00edguez, A., Marinelli, R.A., Brenner, C., Fr\u00fchbeck, G., and Svelto, M. (2013). Liver glycerol permeability and aquaporin-9 are dysregulated in a murine model of non-alcoholic fatty liver disease. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0078139"},{"key":"ref_68","first-page":"1121","article-title":"Perturbation of glycerol metabolism in hepatocytes from n3-PUFA-depleted rats","volume":"29","author":"Portois","year":"2012","journal-title":"Int. J. Mol. Med."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1016\/j.intimp.2013.01.020","article-title":"Knockdown of hepatic aquaglyceroporin-9 alleviates high fat diet-induced non-alcoholic fatty liver disease in rats","volume":"15","author":"Cai","year":"2013","journal-title":"Int. Immunopharmacol."},{"key":"ref_70","first-page":"200","article-title":"The relationship between aquaglyceroporin expression and development of fatty liver in diet-induced obesity and ob\/ob mice","volume":"S1871\u2013403X","author":"Hirako","year":"2015","journal-title":"Obes. Res. Clin. Pract."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1055\/s-2000-9390","article-title":"Molecular alterations in hepatocyte transport mechanisms in acquired cholestatic liver disorders","volume":"20","author":"Lee","year":"2000","journal-title":"Semin. Liver Dis."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1053\/jhep.2003.50170","article-title":"Rat hepatocyte aquaporin-8 water channels are down-regulated in extrahepatic cholestasis","volume":"37","author":"Carreras","year":"2003","journal-title":"Hepatology"},{"key":"ref_73","first-page":"G905","article-title":"Defective hepatocyte aquaporin-8 expression and reduced canalicular membrane water permeability in estrogen-induced cholestasis","volume":"292","author":"Carreras","year":"2007","journal-title":"Am. J. Physiol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"G567","DOI":"10.1152\/ajpgi.00232.2007","article-title":"LPS induces the TNF-\u03b1-mediated downregulation 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":"ref_75","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1111\/j.1478-3231.2008.01824.x","article-title":"Peritoneal sepsis downregulates liver expression of Aquaporin-8: A water channel involved in bile secretion","volume":"29","author":"Lehmann","year":"2009","journal-title":"Liver Int."},{"key":"ref_76","first-page":"G682","article-title":"Altered Expression and Distribution of Aquaporin-9 in the Liver of Rat with Obstructive Extrahepatic Cholestasis","volume":"295","author":"Calamita","year":"2008","journal-title":"Am. J. Physiol."},{"key":"ref_77","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-1 cDNA to irradiated rat salivary glands","volume":"94","author":"Delporte","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_78","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. USA"},{"key":"ref_79","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":"ref_80","doi-asserted-by":"crossref","unstructured":"Marrone, J., Soria, L.R., Danielli, M., Lehmann, G.L., Larocca, M.C., and Marinelli, R.A. (2016). Hepatic gene transfer of human aquaporin-1 improves bile salt secretory failure in rats with estrogen-induced cholestasis. Hepatology.","DOI":"10.1002\/hep.28564"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1254\/jphs.FMJ04004X7","article-title":"Molecular mechanisms and drug development in aquaporin water channel diseases: Aquaporin superfamily (superaquaporins): Expansion of aquaporins restricted to multicellular organisms","volume":"96","author":"Morishita","year":"2004","journal-title":"J. Pharmacol. Sci."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"G501","DOI":"10.1152\/ajpgi.00208.2012","article-title":"Liver-specific Aquaporin 11 knockout mice show rapid vacuolization of the rough endoplasmic reticulum in periportal hepatocytes after amino acid feeding","volume":"304","author":"Rojek","year":"2013","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1111\/j.1477-2574.2008.00014.x","article-title":"Altered aquaporin 9 expression and localization in human hepatocellular carcinoma","volume":"11","author":"Padma","year":"2009","journal-title":"HPB (Oxf.)"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1369\/0022155416641028","article-title":"A systematic characterization of aquaporin-9 expression in human normal and pathological tissues","volume":"64","author":"Lindskog","year":"2016","journal-title":"J. Histochem. Cytochem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.canlet.2016.05.021","article-title":"Aquaporin 9 has is down-regulated in hepatocellular carcinoma and its over-expression suppresses hepatoma cell invasion through inhibiting epithelial-to-mesenchymal transition","volume":"378","author":"Zhang","year":"2016","journal-title":"Cancer Lett."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.pharmthera.2015.08.002","article-title":"Challenges and achievements in the therapeutic modulation of aquaporin functionality","volume":"155","author":"Beitz","year":"2015","journal-title":"Pharmacol. Ther."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"246","DOI":"10.3109\/09687688.2013.773095","article-title":"The identification of novel, high affinity AQP9 inhibitors in an intracellular binding site","volume":"30","author":"Wacker","year":"2013","journal-title":"Mol. Membr. Biol."},{"key":"ref_88","unstructured":"Owen, M. (2015). Sertoli Cell Metabolism and Spermatogenesis, Springer."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1210\/er.2003-0022","article-title":"Sertoli-Sertoli and Sertoli-germ cell interactions and their significance in germ cell movement in the seminiferous epithelium during spermatogenesis","volume":"25","author":"Mruk","year":"2004","journal-title":"Endocr. Rev."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1095\/biolreprod.114.118331","article-title":"Physiology of Na+\/H+ exchangers in the male reproductive tract: Relevance for male fertility","volume":"91","author":"Martins","year":"2014","journal-title":"Biol. Reprod."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"4037","DOI":"10.2174\/15672050113109990200","article-title":"Molecular basis of bicarbonate membrane transport in the male reproductive tract","volume":"20","author":"Bernardino","year":"2013","journal-title":"Curr. Med. Chem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1038\/nrurol.2012.77","article-title":"Metabolic regulation is important for spermatogenesis","volume":"9","author":"Rato","year":"2012","journal-title":"Nat. Rev. Urol."},{"key":"ref_93","first-page":"499","article-title":"New insights on hormones and factors that modulate Sertoli cell metabolism","volume":"31","author":"Rato","year":"2016","journal-title":"Histol. Histopathol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1007\/s00018-012-1079-1","article-title":"Hormonal control of Sertoli cell metabolism regulates spermatogenesis","volume":"70","author":"Alves","year":"2013","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/s00232-008-9139-z","article-title":"Membrane transporters and cytoplasmatic pH regulation on bovine Sertoli cells","volume":"227","author":"Oliveira","year":"2009","journal-title":"J. Membr. Biol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1530\/REP-08-0363","article-title":"Intracellular pH regulation in human Sertoli cells: Role of membrane transporters","volume":"137","author":"Oliveira","year":"2009","journal-title":"Reproduction"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1007\/s00232-010-9294-x","article-title":"Tubular fluid secretion in the seminiferous epithelium: Ion transporters and aquaporins in Sertoli cells","volume":"236","author":"Rato","year":"2010","journal-title":"J. Membr. Biol."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Bernardino, R.L., Costa, A.R., Martins, A.D., Silva, J., Barros, A., Sousa, M., S\u00e1, R., Alves, M.G., and Oliveira, P.F. (2016). Estradiol modulates Na+-dependent HCO3\u2212 transporters altering intracellular pH and ion transport in human Sertoli cells: A role on male fertility?. Biol. Cell.","DOI":"10.1111\/boc.201500094"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1002\/j.1939-4640.1980.tb00003.x","article-title":"The functional significance of the blood-testis barrier","volume":"1","author":"Setchell","year":"1980","journal-title":"J. Androl."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1095\/biolreprod24.5.1032","article-title":"Metabolism of glucose by Sertoli cells in culture","volume":"24","author":"Robinson","year":"1981","journal-title":"Biol. Reprod."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/j.tem.2004.07.003","article-title":"Lactate and energy metabolism in male germ cells","volume":"15","author":"Boussouar","year":"2004","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1093\/molehr\/8.2.109","article-title":"Lactate inhibits germ cell apoptosis in the human testis","volume":"8","author":"Aito","year":"2002","journal-title":"Mol. Hum. Reprod."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1002\/med.21325","article-title":"The warburg effect revisited\u2014Lesson from the Sertoli cell","volume":"35","author":"Oliveira","year":"2015","journal-title":"Med. Res. Rev."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1530\/jrf.0.0770109","article-title":"Metabolism of radiolabelled energy-yielding substrates by rat Sertoli cells","volume":"77","author":"Grootegoed","year":"1986","journal-title":"J. Reprod. Fertil."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1111\/j.1365-2605.2005.00516.x","article-title":"Ontogenetic profile and thyroid hormone regulation of type-1 and type-8 glucose transporters in rat Sertoli cells","volume":"28","author":"Carosa","year":"2005","journal-title":"Int. J. Androl."},{"key":"ref_106","first-page":"156","article-title":"Immunohistochemical detection of glucose transporters class i subfamily in the mouse, rat and human testis","volume":"40","author":"Kokk","year":"2003","journal-title":"Medicina"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.bbagen.2011.11.006","article-title":"Effect of insulin deprivation on metabolism and metabolism-associated gene transcript levels of in vitro cultured human Sertoli cells","volume":"1820","author":"Oliveira","year":"2012","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"e612","DOI":"10.1111\/j.1365-2605.2011.01205.x","article-title":"Influence of 5\u03b1-dihydrotestosterone and 17\u03b2-estradiol on human Sertoli cells metabolism","volume":"34","author":"Oliveira","year":"2011","journal-title":"Int. J. Androl."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1016\/j.bbamcr.2012.06.002","article-title":"In vitro cultured human Sertoli cells secrete high amounts of acetate that is stimulated by 17\u03b2-estradiol and suppressed by insulin deprivation","volume":"1823","author":"Alves","year":"2012","journal-title":"Biochim. Biophys. Acta Mol. Cell Res."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0969-8051(00)00195-5","article-title":"Characterization of acetate metabolism in tumor cells in relation to cell proliferation: Acetate metabolism in tumor cells","volume":"28","author":"Yoshimoto","year":"2001","journal-title":"Nucl. Med. Biol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1016\/j.bbadis.2013.01.011","article-title":"Molecular mechanisms beyond glucose transport in diabetes-related male infertility","volume":"1832","author":"Alves","year":"2013","journal-title":"Biochim. Biophys. Acta Mol. Basis Dis."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1530\/eje.0.1380322","article-title":"Changes in carbohydrate metabolism of testicular germ cells during meiosis in the rat","volume":"138","author":"Bajpai","year":"1998","journal-title":"Eur. J. Endocrinol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1530\/jrf.0.0620399","article-title":"Exogenous lactate is essential for metabolic activities in isolated rat spermatocytes and spermatids","volume":"62","author":"Jutte","year":"1981","journal-title":"J. Reprod. Fertil."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.semcdb.2005.03.008","article-title":"The hypoxic testis and post-meiotic expression of pas domain proteins","volume":"16","author":"Wenger","year":"2005","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1002\/aja.1001840302","article-title":"Postnatal development of the Sertoli cell barrier, tubular lumen, and cytoskeleton of Sertoli and myoid cells in the rat, and their relationship to tubular fluid secretion and flow","volume":"184","author":"Russell","year":"1989","journal-title":"Am. J. Anat."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1093\/humupd\/dml035","article-title":"Function of aquaporins in female and male reproductive systems","volume":"12","author":"Huang","year":"2006","journal-title":"Hum. Reprod. Update"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/978-3-540-79885-9_11","article-title":"Function of aquaporin-7 in the kidney and the male reproductive system","volume":"Volume 190","author":"Beitz","year":"2009","journal-title":"Aquaporins"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1002\/j.1939-4640.2002.tb02243.x","article-title":"Expression and regulation of aquaporins 1, 8, and 9 in the testis, efferent ducts, and epididymis of adult rats and during postnatal development","volume":"23","author":"Badran","year":"2002","journal-title":"J. Androl."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1002\/j.1939-4640.2004.tb02820.x","article-title":"Cell specificity of aquaporins 0, 3, and 10 expressed in the testis, efferent ducts, and epididymis of adult rats","volume":"25","author":"Hermo","year":"2004","journal-title":"J. Androl."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1111\/j.1365-2605.2009.00998.x","article-title":"Aquaporins in the human testis and spermatozoa\u2014Identification, involvement in sperm volume regulation and clinical relevance","volume":"33","author":"Yeung","year":"2010","journal-title":"Int. J. Androl."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1002\/aja.1001780109","article-title":"Comparative study of cytoplasmic elimination in spermatids of selected mammalian species","volume":"178","author":"Sprando","year":"1987","journal-title":"Am. J. Anat."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"565","DOI":"10.2164\/jandrol.110.012831","article-title":"Thirsty business: Cell, region, and membrane specificity of aquaporins in the testis, efferent ducts, and epididymis and factors regulating their expression","volume":"32","author":"Hermo","year":"2011","journal-title":"J. Androl."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"993","DOI":"10.2174\/1573399811666150615144108","article-title":"CFTR regulation of Aquaporin-mediated water transport: A target in male fertility","volume":"16","author":"Alves","year":"2015","journal-title":"Curr. Drug Targets"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1016\/j.bbrc.2014.03.046","article-title":"Aquaporin-4 as a molecular partner of cystic fibrosis transmembrane conductance regulator in rat Sertoli cells","volume":"446","author":"Jesus","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1002\/ar.22709","article-title":"Region-specific expression of aquaporin subtypes in equine testis, epididymis, and ductus deferens","volume":"296","author":"Klein","year":"2013","journal-title":"Anat. Rec."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1111\/j.1939-165X.2011.00390.x","article-title":"The role of aquaporin 4 in the brain","volume":"41","author":"Iacovetta","year":"2012","journal-title":"Vet. Clin. Pathol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"401","DOI":"10.2174\/157339912803529896","article-title":"Impact of diabetes in blood-testis and blood-brain barriers: Resemblances and differences","volume":"8","author":"Alves","year":"2012","journal-title":"Curr. Diabetes Rev."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1679\/aohc.64.159","article-title":"Immunolocalization of aquaporin-8 in rat digestive organs and testis","volume":"64","author":"Tani","year":"2001","journal-title":"Arch. Histol. Cytol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1006\/geno.1998.5552","article-title":"Cloning and functional expression of human aquaporin8 cDNA and analysis of its gene","volume":"54","author":"Koyama","year":"1998","journal-title":"Genomics"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1002\/aja.1001470403","article-title":"Light and electron microscopic localization of ATPase in normal and degenerating testes of syrian hamsters","volume":"147","author":"Gravis","year":"1976","journal-title":"Am. J. Anat."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"C1161","DOI":"10.1152\/ajpcell.00564.2004","article-title":"Phenotype analysis of aquaporin-8 null mice","volume":"288","author":"Yang","year":"2005","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1002\/iub.1312","article-title":"Aquaporin-9 is expressed in rat Sertoli cells and interacts with the cystic fibrosis transmembrane conductance regulator","volume":"66","author":"Jesus","year":"2014","journal-title":"IUBMB Life"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1679\/aohc.64.81","article-title":"Immunolocalization of aquaporin-9 in rat hepatocytes and leydig cells","volume":"64","author":"Nihei","year":"2001","journal-title":"Arch. Histol. Cytol."},{"key":"ref_134","first-page":"515","article-title":"Possible functional implications of aquaporin water channels in reproductive physiology and medically assisted procreation","volume":"49","author":"Cho","year":"2003","journal-title":"Cell. Mol. Biol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.neuroscience.2004.06.035","article-title":"Distribution and possible roles of aquaporin 9 in the brain","volume":"129","author":"Badaut","year":"2004","journal-title":"Neuroscience"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1002\/j.1939-4640.2000.tb02129.x","article-title":"Glycerol disrupts tight junction-associated actin microfilaments, occludin, and microtubules in Sertoli cells","volume":"21","author":"Wiebe","year":"2000","journal-title":"J. Androl."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/17\/7\/1096\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T19:25:47Z","timestamp":1760210747000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/17\/7\/1096"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,7,9]]},"references-count":136,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2016,7]]}},"alternative-id":["ijms17071096"],"URL":"https:\/\/doi.org\/10.3390\/ijms17071096","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,7,9]]}}}