2013
Activation of the Ca2+-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane
Jouret F, Wu J, Hull M, Rajendran V, Mayr B, Schöfl C, Geibel J, Caplan MJ. Activation of the Ca2+-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane. Journal Of Cell Science 2013, 126: 5132-5142. PMID: 24013548, PMCID: PMC3828589, DOI: 10.1242/jcs.127555.Peer-Reviewed Original ResearchConceptsTJ assemblyMDCK cellsStable transfectionFunction mutant formZO-1Tight junction components ZO-1G protein-coupled receptorsHuman CaSRCell-cell contactEpithelial cell plasma membranesMadin-Darby canine kidney cellsCell plasma membraneStimulation of CaSRDivalent ion homeostasisCanine kidney cellsTight junctionsJunction-associated proteinsTight junction componentsEndogenous CaSRProtein kinasePlasma membraneIon homeostasisMutant formsChelator BAPTA-AMCell differentiation
2011
Interactions between β-Catenin and the HSlo Potassium Channel Regulates HSlo Surface Expression
Bian S, Bai JP, Chapin H, Le Moellic C, Dong H, Caplan M, Sigworth FJ, Navaratnam DS. Interactions between β-Catenin and the HSlo Potassium Channel Regulates HSlo Surface Expression. PLOS ONE 2011, 6: e28264. PMID: 22194818, PMCID: PMC3237428, DOI: 10.1371/journal.pone.0028264.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBeta CateninBinding SitesBiological AssayCell MembraneChickensGene Knockdown TechniquesHair Cells, AuditoryHEK293 CellsHumansImmunoprecipitationIntercellular JunctionsKineticsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsModels, MolecularMolecular Sequence DataMutant ProteinsMutationPhosphorylationProtein BindingProtein TransportRNA, Small InterferingSequence DeletionTransfectionWnt Signaling PathwayConceptsΒ-cateninS10 regionHEK cellsSurface expressionCell biology toolsPotassium channel alpha subunitΒ-catenin interactionDownregulation of WntCytoskeleton frameworkChannel alpha subunitChicken hair cellsPhosphorylation sitesDeletion mutantsBiology toolsΒ-catenin-dependent canonical WntAlpha subunitCanonical WntMultiple binding sitesNumber of diseasesStable bindingWntPhysiological significanceBinding sitesReduced expressionHair cells
2010
Exosome release of β-catenin: a novel mechanism that antagonizes Wnt signaling
Chairoungdua A, Smith DL, Pochard P, Hull M, Caplan MJ. Exosome release of β-catenin: a novel mechanism that antagonizes Wnt signaling. Journal Of Cell Biology 2010, 190: 1079-1091. PMID: 20837771, PMCID: PMC3101591, DOI: 10.1083/jcb.201002049.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDBeta CateninCadherinsCell LineExosomesGene Knockdown TechniquesGenes, ReporterGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHumansKangai-1 ProteinLysosomesMembrane GlycoproteinsMiceModels, BiologicalProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalProtein StabilityProtein TransportSignal TransductionTetraspanin 29TransfectionWnt ProteinsConceptsΒ-cateninΒ-catenin-mediated WntProtein degradation pathwaysCellular signaling pathwaysTetraspanin membrane proteinΒ-catenin protein levelsGlycogen synthase kinase-3βWnt/β-catenin signalingSynthase kinase-3βΒ-catenin signalingMembrane proteinsCytosolic proteinsSignaling pathwaysKinase-3βExosomal packagingExosome releaseSphingomyelinase inhibitorNovel mechanismE-cadherinDegradation pathwayProtein levelsCD82Tumor metastasisCD9Wnt
2009
Ligand-modified gene carriers increased uptake in target cells but reduced DNA release and transfection efficiency
Cu Y, LeMoëllic C, Caplan MJ, Saltzman WM. Ligand-modified gene carriers increased uptake in target cells but reduced DNA release and transfection efficiency. Nanomedicine Nanotechnology Biology And Medicine 2009, 6: 334-343. PMID: 19800989, PMCID: PMC2847641, DOI: 10.1016/j.nano.2009.09.001.Peer-Reviewed Original ResearchConceptsTransfection efficiencyDNA deliveryDNA release rateParticle carriersUnmodified particlesCLINICAL EDITORDrug carriersGene carriersPayload releaseBovine serum albuminCell uptakeParticle surfaceDNA releasePolymer drug carriersPLGASpecific cellsBiodegradable polymersCarriersSerum albuminRelease rateBSAParticlesHigh densityHigh uptakeDelivery
2008
Exon Loss Accounts for Differential Sorting of Na-K-Cl Cotransporters in Polarized Epithelial Cells
Carmosino M, Giménez I, Caplan M, Forbush B. Exon Loss Accounts for Differential Sorting of Na-K-Cl Cotransporters in Polarized Epithelial Cells. Molecular Biology Of The Cell 2008, 19: 4341-4351. PMID: 18667527, PMCID: PMC2555935, DOI: 10.1091/mbc.e08-05-0478.Peer-Reviewed Original ResearchConceptsDileucine motifNa-K-Cl cotransporterRenal Na-K-Cl cotransporterPolarized epithelial cellsAmino acid stretchApical proteinsApical sortingEvolutionary lossRenal epithelial cell lineGene structurePhylogenetic analysisDifferential sortingDirect traffickingEpithelial cell lineAdditional exonC-terminusMammalian kidneyApical membraneExonsNovel mechanismNKCC2 geneCell linesBasolateral membraneMotifEpithelial cellsPolycystin-1 C-terminal tail associates with β-catenin and inhibits canonical Wnt signaling
Lal M, Song X, Pluznick JL, Di Giovanni V, Merrick DM, Rosenblum ND, Chauvet V, Gottardi CJ, Pei Y, Caplan MJ. Polycystin-1 C-terminal tail associates with β-catenin and inhibits canonical Wnt signaling. Human Molecular Genetics 2008, 17: 3105-3117. PMID: 18632682, PMCID: PMC2722884, DOI: 10.1093/hmg/ddn208.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta CateninBinding SitesCell LineCell NucleusCHO CellsCricetinaeCricetulusGene Expression ProfilingGene Expression RegulationHumansLigandsOligonucleotide Array Sequence AnalysisPeptide FragmentsPolycystic Kidney, Autosomal DominantRecombinant ProteinsSignal TransductionSystems BiologyTCF Transcription FactorsTransfectionTRPP Cation ChannelsWnt ProteinsConceptsC-terminal tailCanonical WntPolycystin-1Wnt-dependent signalingDNA microarray analysisDependent gene transcriptionN-terminal portionInhibits canonical WntTCF proteinsT-cell factorAutosomal dominant polycystic kidney disease (ADPKD) casesMotif presentGene transcriptionDevelopmental processesMicroarray analysisWntPKD1 geneΒ-cateninNovel mechanismExpression of Tetraspan Protein CD63 Activates Protein-tyrosine Kinase (PTK) and Enhances the PTK-induced Inhibition of ROMK Channels*
Lin D, Kamsteeg EJ, Zhang Y, Jin Y, Sterling H, Yue P, Roos M, Duffield A, Spencer J, Caplan M, Wang WH. Expression of Tetraspan Protein CD63 Activates Protein-tyrosine Kinase (PTK) and Enhances the PTK-induced Inhibition of ROMK Channels*. Journal Of Biological Chemistry 2008, 283: 7674-7681. PMID: 18211905, DOI: 10.1074/jbc.m705574200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDBenzoquinonesCSK Tyrosine-Protein KinaseEnzyme InhibitorsFemaleGene Expression RegulationHumansKidney CortexKidney MedullaLactams, MacrocyclicMaleOocytesOrgan SpecificityPatch-Clamp TechniquesPhosphorylationPlatelet Membrane GlycoproteinsPotassium Channels, Inwardly RectifyingProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsRats, Sprague-DawleyReceptor-Like Protein Tyrosine Phosphatases, Class 4RifabutinSrc-Family KinasesTetraspanin 30TransfectionXenopus laevisConceptsExpression of CD63T cellsOuter medullaRenal cortexROMK channelsProtein tyrosine kinasesC-SrcRole of CD63Potassium restrictionROMK activityPotassium currentTwo-electrode voltage clampRat kidneyDecreased expressionImmunocytochemical stainingROMK1 channelsInhibitory effectMedullaNative rat kidneyCD63Voltage clampCortexRPTPalphaTyrosine phosphorylationHerbimycin A
2005
The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase α-Subunit
Zatti A, Chauvet V, Rajendran V, Kimura T, Pagel P, Caplan MJ. The C-Terminal Tail of the Polycystin-1 Protein Interacts with the Na,K-ATPase α-Subunit. Molecular Biology Of The Cell 2005, 16: 5087-5093. PMID: 16107561, PMCID: PMC1266409, DOI: 10.1091/mbc.e05-03-0200.Peer-Reviewed Original ResearchConceptsC-terminal tailPolycystin-1Cytoplasmic C-terminal tailK-ATPase α-subunitPolycystin-1 proteinK-ATPase activityRegulation of NaChinese hamster ovary cellsProtein interactsHamster ovary cellsProtein exhibitΑ-subunitFunctional studiesAmino acidsPKD1 geneOvary cellsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseasePolycystic kidney diseaseInteractsKinetic propertiesRegulationGenesTailProtein
2004
Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression
Duffield A, Fölsch H, Mellman I, Caplan MJ. Sorting of H,K‐ATPase β‐Subunit in MDCK and LLC‐PK1 Cells is Independent of μ1B Adaptin Expression. Traffic 2004, 5: 449-461. PMID: 15117319, DOI: 10.1111/j.1398-9219.2004.00192.x.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAmino Acid MotifsAnimalsCell LineCytoplasmDogsEpithelial CellsGlutathione TransferaseH(+)-K(+)-Exchanging ATPaseLLC-PK1 CellsMembrane ProteinsProtein SubunitsProtein TransportReceptors, LDLReceptors, TransferrinRecombinant Fusion ProteinsSwineTransfectionTyrosineConceptsLow-density lipoproteinTransferrin receptorBasolateral localizationTyrosine-based motifMDCK cellsB expressionLLC-PK1 cellsEpithelial cellsLipoproteinMadin-Darby canine kidney cellsCertain epithelial cellsReceptorsKidney cellsCanine kidney cellsK-ATPase beta subunitCellsDifferential expressionK-ATPaseBasolateral expressionExpressionApical membraneCurcumin, a Major Constituent of Turmeric, Corrects Cystic Fibrosis Defects
Egan ME, Pearson M, Weiner SA, Rajendran V, Rubin D, Glöckner-Pagel J, Canny S, Du K, Lukacs GL, Caplan MJ. Curcumin, a Major Constituent of Turmeric, Corrects Cystic Fibrosis Defects. Science 2004, 304: 600-602. PMID: 15105504, DOI: 10.1126/science.1093941.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalnexinCell LineCell MembraneCricetinaeCurcuminCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorElectrolytesEndoplasmic ReticulumGene TargetingGlycosylationHumansIntestinal MucosaIntestinal ObstructionIsoproterenolMembrane PotentialsMiceMice, KnockoutMutationNasal MucosaPolyethylene GlycolsProtein FoldingRectumTransfectionConceptsCystic fibrosis transmembrane conductance regulatorCFTR proteinDeltaF508 cystic fibrosis transmembrane conductance regulatorDeltaF508 CFTR proteinFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorBaby hamster kidney cellsPlasma membraneComplete knockoutConductance regulatorHamster kidney cellsEndoplasmic reticulumCystic fibrosis defectCFTR geneKidney cellsCFTR miceGenesProteinMutationsCommon mutationsHomozygous expressionCurcumin treatmentFunctional appearanceWeight basisRegulator
2003
The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit
Duffield A, Kamsteeg EJ, Brown AN, Pagel P, Caplan MJ. The tetraspanin CD63 enhances the internalization of the H,K-ATPase β-subunit. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 15560-15565. PMID: 14660791, PMCID: PMC307607, DOI: 10.1073/pnas.2536699100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDChlorocebus aethiopsCloning, MolecularCOS CellsGene LibraryH(+)-K(+)-Exchanging ATPaseHumansKidneyMembrane ProteinsModels, BiologicalPlatelet Membrane GlycoproteinsProtein SubunitsProtein TransportRabbitsRatsRats, Sprague-DawleyRecombinant ProteinsTetraspanin 30TransfectionConceptsAdaptor protein complex 2Intracellular compartmentsK-ATPaseTetraspanin CD63K-ATPase β-subunitCOS-7 cellsEndocytic machineryAdaptor proteinLate endosomesSecretory vesiclesPlasma membraneGastric parietal cellsBiochemical experimentsInteraction partnersΒ-subunitParietal cellsCell surfaceEnhanced endocytosisTubulovesicular elementsCD63CompartmentsCellsInternalizationComplexes 2EndosomesPolycystin-1 Distribution Is Modulated by Polycystin-2 Expression in Mammalian Cells*
Grimm DH, Cai Y, Chauvet V, Rajendran V, Zeltner R, Geng L, Avner ED, Sweeney W, Somlo S, Caplan MJ. Polycystin-1 Distribution Is Modulated by Polycystin-2 Expression in Mammalian Cells*. Journal Of Biological Chemistry 2003, 278: 36786-36793. PMID: 12840011, DOI: 10.1074/jbc.m306536200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCell LineCell MembraneCells, CulturedCOS CellsDNA, ComplementaryEndoplasmic ReticulumGene Expression RegulationMembrane ProteinsMiceMice, TransgenicMicroscopy, FluorescenceModels, BiologicalMutationPrecipitin TestsProtein BindingProtein BiosynthesisProteinsRecombinant Fusion ProteinsRNA, MessengerTransfectionTRPP Cation ChannelsConceptsPolycystin-1Polycystin-2Mammalian cellsLevel of expressionPolycystin-2 expressionEndoplasmic reticulumCell surfaceCOS-7 cellsNull cell lineRelative expression levelsSubcellular localizationFusion proteinGradient of expressionExpression levelsProteinCell linesPolycystinsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseaseDivergent patternsExpressionPolycystic kidney diseaseReticulumCellsLocalization
2000
Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells
Reinhardt J, Grishin A, Oberleithner H, Caplan M. Differential localization of human nongastric H+-K+-ATPase ATP1AL1 in polarized renal epithelial cells. American Journal Of Physiology. Renal Physiology 2000, 279: f417-f425. PMID: 10966921, DOI: 10.1152/ajprenal.2000.279.3.f417.Peer-Reviewed Original ResearchConceptsApical plasma membranePlasma membraneRenal epithelial cellsIon pumpsPlasma membrane localizationConfocal immunofluorescence microscopyEpithelial cellsATPase beta subunitRenal epithelial cell lineMembrane localizationLow expression levelsEpithelial cell lineSurface biotinylationPump subunitsBeta subunitFunctional expressionStable transfectionLateral membranesMDCK cellsATP1AL1Immunofluorescence microscopyDifferential localizationSorting mechanismStable interactionExpression levelsA Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase
Dunbar L, Aronson P, Caplan M. A Transmembrane Segment Determines the Steady-State Localization of an Ion-Transporting Adenosine Triphosphatase. Journal Of Cell Biology 2000, 148: 769-778. PMID: 10684257, PMCID: PMC2169368, DOI: 10.1083/jcb.148.4.769.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCationsCell LineCell MembraneCell PolarityGlycosphingolipidsGlycosylphosphatidylinositolsH(+)-K(+)-Exchanging ATPaseHydrogen-Ion ConcentrationMembrane ProteinsMolecular Sequence DataOuabainParietal Cells, GastricProtein Sorting SignalsRecombinant Fusion ProteinsSequence AlignmentSequence DeletionSodium-Potassium-Exchanging ATPaseSolubilityTransfectionConceptsK-ATPase alpha subunitAlpha subunitTransmembrane domainPolytopic membrane transport proteinK-ATPaseApical distributionGlycosphingolipid-rich membrane domainsDetergent-insoluble complexesMembrane transport proteinsApical membrane proteinsApical plasma membraneK-ATPase alphaFourth transmembrane domainLocalization signalChimeric pumpsFourth transmembraneTransmembrane segmentsK-ATPase sequencesMembrane compartmentsMembrane domainsMembrane proteinsSequence domainsPlasma membraneGastric parietal cellsTransport proteins
1999
Cation Selectivity of Gastric H,K-ATPase and Na,K-ATPase Chimeras*
Blostein R, Dunbar L, Mense M, Scanzano R, Wilczynska A, Caplan M. Cation Selectivity of Gastric H,K-ATPase and Na,K-ATPase Chimeras*. Journal Of Biological Chemistry 1999, 274: 18374-18381. PMID: 10373442, DOI: 10.1074/jbc.274.26.18374.Peer-Reviewed Original Research
1998
A basolateral sorting signal is encoded in the α-subunit of Na-K-ATPase
Muth TR, Gottardi CJ, Roush DL, Caplan MJ. A basolateral sorting signal is encoded in the α-subunit of Na-K-ATPase. American Journal Of Physiology 1998, 274: c688-c696. PMID: 9530100, DOI: 10.1152/ajpcell.1998.274.3.c688.Peer-Reviewed Original ResearchConceptsLLC-PK1 cellsK-ATPaseAmino acidsPlasma membrane distributionIntracellular vesicular compartmentsBasolateral surfaceAmino acid residuesNa-K-ATPaseBasolateral signalSurface expressionK-ATPase sequencesProtein domainsPlasma membraneVesicular compartmentsGastric parietal cellsTranscriptional upregulationΑ-subunitLLC-PK1 cell lineMembrane distributionAcid residuesSecretagogue stimulationIon pumpsApical surfaceChimerasCell lines[25] Expression of neurotransmitter transport systems in polarized cells
Ahn J, Pietrini G, Muth TR, Caplan MJ. [25] Expression of neurotransmitter transport systems in polarized cells. Methods In Enzymology 1998, 296: 370-388. PMID: 9779461, DOI: 10.1016/s0076-6879(98)96027-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsCell Culture TechniquesCell DivisionCell LineCell MembraneCell PolarityCells, CulturedClone CellsDogsEpithelial CellsGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidHippocampusKidneyMembrane ProteinsMembrane Transport ProteinsNeuronsOrganic Anion TransportersRecombinant ProteinsTransfectionConceptsNeurotransmitter transport systemsComplementary DNASpecific subcellular distributionTransport protein familySpecific subcellular structuresExogenous protein expressionCultured epithelial cell linesProtein familyEpithelial cell linePlasma membraneTransport assaysTransport proteinsTransporter proteinsSubcellular distributionSubcellular structuresTransport systemFluorescence microscopySpecific subdomainsProtein expressionCell linesProteinExpressionCellsTransportersDNA
1997
A Tyrosine-Based Signal Targets H/K-ATPase to a Regulated Compartment and Is Required for the Cessation of Gastric Acid Secretion
Courtois-Coutry N, Roush D, Rajendran V, McCarthy J, Geibel J, Kashgarian M, Caplan M. A Tyrosine-Based Signal Targets H/K-ATPase to a Regulated Compartment and Is Required for the Cessation of Gastric Acid Secretion. Cell 1997, 90: 501-510. PMID: 9267030, DOI: 10.1016/s0092-8674(00)80510-3.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCOS CellsCytomegalovirusDNA PrimersEndocytosisGastric AcidGastric MucosaH(+)-K(+)-Exchanging ATPaseMacromolecular SubstancesMiceMice, TransgenicMicroscopy, ImmunoelectronMutagenesis, Site-DirectedParietal Cells, GastricPolymerase Chain ReactionPromoter Regions, GeneticRecombinant ProteinsSignal TransductionTransfectionTyrosineConceptsK-ATPase beta subunitTyrosine-based signalsK-ATPaseTyrosine-based endocytosis signalTyrosine residuesBeta subunitIntracellular storage compartmentEndocytosis signalCytoplasmic tailMutant betaRegulated compartmentsSecrete acidResidue sequenceStorage compartmentCell surfaceCell plasmalemmaSubunitsTransgenic miceParietal cellsGastric glandsCompartmentsSecretionAcid secretionReinternalizationPlasmalemmaSorting of Two Polytopic Proteins, the γ-Aminobutyric Acid and Betaine Transporters, in Polarized Epithelial Cells*
Perego C, Bulbarelli A, Longhi R, Caimi M, Villa A, Caplan M, Pietrini G. Sorting of Two Polytopic Proteins, the γ-Aminobutyric Acid and Betaine Transporters, in Polarized Epithelial Cells*. Journal Of Biological Chemistry 1997, 272: 6584-6592. PMID: 9045687, DOI: 10.1074/jbc.272.10.6584.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsCell CompartmentationCell LineCell MembraneCell PolarityCytosolDogsEndoplasmic ReticulumFluorescent Antibody Technique, IndirectGABA Plasma Membrane Transport ProteinsHumansMembrane ProteinsMembrane Transport ProteinsMolecular Sequence DataOrganic Anion TransportersReceptors, Nerve Growth FactorRecombinant Fusion ProteinsRecombinant ProteinsStructure-Activity RelationshipTransfectionConceptsCytosolic tailMadin-Darby canine kidney cellsCanine kidney cellsBetaine transporterEndoplasmic reticulumPolarized epithelial cellsTerminal cytosolic domainHuman nerve growth factor receptorKidney cellsPolytopic proteinsApical proteinsCytosolic domainChimeric transportersGrowth factor receptorApical localizationBasolateral distributionBasic residuesBasolateral localizationTransporter isoformsGAT-1Nerve growth factor receptorBgtBasolateral surfaceFactor receptorProteinCloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry
Gu H, Caplan MJ, Rudnick G. Cloned Catecholamine Transporters Expressed in Polarized Epithelial Cells: Sorting, Drug Sensitivity, and Ion-Coupling Stoichiometry. Advances In Pharmacology 1997, 42: 175-179. PMID: 9327872, DOI: 10.1016/s1054-3589(08)60721-8.Peer-Reviewed Original ResearchMeSH KeywordsAmphetamineAnimalsBiological TransportCarrier ProteinsCell LineCell PolarityCloning, MolecularDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidHumansKineticsMembrane GlycoproteinsMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsOrganic Anion TransportersRatsRecombinant Fusion ProteinsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSubstrate SpecificitySwineSymportersTransfectionConceptsCell linesPolarized epithelial cellsHeterologous expression systemBiogenic amine transportersCanine kidney cellsSame cellular backgroundKidney cell lineLLC-PK1 cellsExpression systemBiogenic amine releaseCellular backgroundIntact cellsPig kidney cell lineSame cDNAInhibitor sensitivityAmine transportersCatecholamine transportersCoupling stoichiometryTransportersKidney cellsDrug sensitivityPharmacological propertiesEpithelial cellsMolecule of substrateAmine release