2008
ATP8B1 Deficiency Disrupts the Bile Canalicular Membrane Bilayer Structure in Hepatocytes, But FXR Expression and Activity Are Maintained
Cai S, Gautam S, Nguyen T, Soroka CJ, Rahner C, Boyer JL. ATP8B1 Deficiency Disrupts the Bile Canalicular Membrane Bilayer Structure in Hepatocytes, But FXR Expression and Activity Are Maintained. Gastroenterology 2008, 136: 1060-1069.e4. PMID: 19027009, PMCID: PMC3439851, DOI: 10.1053/j.gastro.2008.10.025.Peer-Reviewed Original ResearchMeSH Keywords4-Chloro-7-nitrobenzofurazanAdenosine TriphosphatasesAnimalsATP Binding Cassette Transporter, Subfamily B, Member 11ATP-Binding Cassette TransportersBile CanaliculiCaco-2 CellsChenodeoxycholic AcidDNA-Binding ProteinsGastrointestinal AgentsGene ExpressionHepatocytesHumansMultidrug Resistance-Associated Protein 2PhosphatidylserinesPhospholipid Transfer ProteinsRatsReceptors, Cytoplasmic and NuclearRNA, Small InterferingTranscription FactorsTransfectionConceptsAminophospholipid flippaseMessenger RNAMembrane bilayer structureCanalicular membraneFarnesoid X receptorRat hepatocytesSmall heterodimer partnerMembrane transportersNBD-phosphatidylserineHeterodimer partnerDeficiency disruptsLuminal accumulationMembrane disruptionRNAConflicting hypothesesRat cellsFlippaseProtein levelsProtein expressionX receptorExpressionBSEP functionATP8B1CellsMembrane
2003
1102 Susceptibility to estrogen induced cholestasis in the female is associated with loss of radixin, an MRP2 tethering protein, from the canalicular membrane
Soroka C, Mennone A, Boyer J. 1102 Susceptibility to estrogen induced cholestasis in the female is associated with loss of radixin, an MRP2 tethering protein, from the canalicular membrane. Hepatology 2003, 38: 687. DOI: 10.1016/s0270-9139(03)81140-0.Peer-Reviewed Original ResearchTethering proteinsCanalicular membrane
2000
Bile salt excretion in skate liver is mediated by a functional analog of Bsep/Spgp, the bile salt export pump
Ballatori N, Rebbeor J, Connolly G, Seward D, Lenth B, Henson J, Sundaram P, Boyer J. Bile salt excretion in skate liver is mediated by a functional analog of Bsep/Spgp, the bile salt export pump. AJP Gastrointestinal And Liver Physiology 2000, 278: g57-g63. PMID: 10644562, DOI: 10.1152/ajpgi.2000.278.1.g57.Peer-Reviewed Original ResearchConceptsTransport activityPlasma membrane vesiclesApparent molecular massVertebrate evolutionATP-dependent componentMultidrug resistance protein 1Similar transport activityFunctional characterizationPlasma membraneApical localizationCanalicular membraneResistance protein 1Liver plasma membrane vesiclesATP-dependent uptakeSkate liverMembrane vesiclesWestern blot analysisDominant protein bandsMammalian liverMolecular massLittle skateFunctional analogueProtein 1Raja erinaceaCanalicular multidrug resistance
1998
Cyclic AMP stimulates sorting of the canalicular organic anion transporter (Mrp2/cMoat) to the apical domain in hepatocyte couplets
Roelofsen H, Soroka C, Keppler D, Boyer J. Cyclic AMP stimulates sorting of the canalicular organic anion transporter (Mrp2/cMoat) to the apical domain in hepatocyte couplets. Journal Of Cell Science 1998, 111: 1137-1145. PMID: 9512509, DOI: 10.1242/jcs.111.8.1137.Peer-Reviewed Original ResearchConceptsTransport proteinsApical membraneApical domainTransporter-containing vesiclesMultidrug resistance protein 2Protein 2Cell-cell contactMicrotubule-dependent fashionBasolateral plasma membraneApical proteinsEffect of cAMPVesicle trafficAnion transportersSecretory polarityOrganic anion transportersPlasma membraneCanalicular membraneAnion transport capacityTransport activityApical excretionApical poleCanalicular organic anion transportMultispecific organic anion transporterAmphiphilic organic anionsTransport function
1995
Vesicle targeting to the apical domain regulates bile excretory function in isolated rat hepatocyte couplets
Boyer J, Soroka C. Vesicle targeting to the apical domain regulates bile excretory function in isolated rat hepatocyte couplets. Gastroenterology 1995, 109: 1600-1611. PMID: 7557144, DOI: 10.1016/0016-5085(95)90649-5.Peer-Reviewed Original ResearchConceptsInsertion of vesiclesTranslocation of vesiclesMembrane transport activityVesicle trafficApical domainIsolated rat hepatocyte coupletsAcid transportersTransport activityNocodazoleRat hepatocyte coupletsVesiclesIndependent mechanismsEpithelial cellsBile acid transporterSite of residenceHepatocyte coupletsTransportersCanalicular membraneRat hepatocytesImmunocytochemical localizationCyclic monophosphateAdenosine triphosphataseBile excretory function
1975
Scanning Electron Microscopy of the Rat Liver Studies of the effect of taurolithocholate and other models of cholestasis
Layden T, Schwarz J, Boyer J. Scanning Electron Microscopy of the Rat Liver Studies of the effect of taurolithocholate and other models of cholestasis. Gastroenterology 1975, 69: 724-738. PMID: 1158090, DOI: 10.1016/s0016-5085(19)32475-8.Peer-Reviewed Original ResearchConceptsModel of cholestasisBile duct ligationEstradiol treatmentDuct ligationEffect of cholestasisEffect of taurolithocholateTLC-induced cholestasisDirect toxic effectBile canaliculiLithocholate sulfateRat liver studiesCanalicular membraneLoss of microvilliNormal findingsFinger fracturesPortal veinDistinctive abnormalitiesSimultaneous infusionCholestasisSodium taurolithocholateSevere abnormalitiesSodium taurocholateInfusionTaurolithocholateLiver studies