2021
β3 adrenergic receptor as potential therapeutic target in ADPKD
Schena G, Carmosino M, Chiurlia S, Onuchic L, Mastropasqua M, Maiorano E, Schena FP, Caplan MJ. β3 adrenergic receptor as potential therapeutic target in ADPKD. Physiological Reports 2021, 9: e15058. PMID: 34676684, PMCID: PMC8531837, DOI: 10.14814/phy2.15058.Peer-Reviewed Original ResearchConceptsAutosomal dominant polycystic kidney diseaseΒ3-ARΒ3-adrenergic receptorTherapeutic targetKidney/body weight ratioΒ3-AR levelSympathetic nerve activityBody weight ratioType 2 receptorCyst-lining epithelial cellsDominant polycystic kidney diseaseRenal tubular cellsNovel therapeutic targetCyclic AMP accumulationPotential therapeutic targetVasopressin type 2 receptorHuman renal tissuePolycystic kidney diseaseFluid-filled cystsADPKD mouse modelNerve activityKidney functionKidney diseaseRenal parenchymaHealthy controls
2015
Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin
Farr GA, Hull M, Stoops EH, Bateson R, Caplan MJ. Dual pulse-chase microscopy reveals early divergence in the biosynthetic trafficking of the Na,K-ATPase and E-cadherin. Molecular Biology Of The Cell 2015, 26: 4401-4411. PMID: 26424804, PMCID: PMC4666135, DOI: 10.1091/mbc.e14-09-1385.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkPlasma membraneE-cadherinK-ATPasePolarized MDCK epithelial cellsPost-Golgi traffickingCell surfacePolarized epithelial cellsEpithelial cellsMDCK epithelial cellsDistinct trafficking routesBiosynthetic traffickingCarrier vesiclesSecretory pathwayMembrane proteinsSurface deliveryBasolateral domainMost proteinsTrafficking routesGolgi complexTemperature blockTraffickingProteinMembraneCellsPolycystin-1 Is a Cardiomyocyte Mechanosensor That Governs L-Type Ca2+ Channel Protein Stability
Pedrozo Z, Criollo A, Battiprolu PK, Morales CR, Contreras-Ferrat A, Fernández C, Jiang N, Luo X, Caplan MJ, Somlo S, Rothermel BA, Gillette TG, Lavandero S, Hill JA. Polycystin-1 Is a Cardiomyocyte Mechanosensor That Governs L-Type Ca2+ Channel Protein Stability. Circulation 2015, 131: 2131-2142. PMID: 25888683, PMCID: PMC4470854, DOI: 10.1161/circulationaha.114.013537.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornBiomarkersCalcium Channels, L-TypeCardiomegalyCells, CulturedFibrosisHypertrophyHypotonic SolutionsMaleMechanotransduction, CellularMiceMice, KnockoutMyocytes, CardiacProtein Interaction MappingProtein StabilityProtein Structure, TertiaryRatsRats, Sprague-DawleyRecombinant Fusion ProteinsRNA InterferenceStress, MechanicalTRPP Cation ChannelsConceptsL-type calcium channel activityCalcium channel activityNeonatal rat ventricular myocytesRat ventricular myocytesKnockout miceVentricular myocytesChannel activityMechanical stretchNeonatal rat ventricular myocyte hypertrophyProtein levelsVentricular myocyte hypertrophyL-type Ca2G protein-coupled receptor-like proteinPolycystin-1Channel protein levelsCyclic mechanical stretchControl miceInterstitial fibrosisStress-induced activationCardiac massMechanical stress-induced activationCardiac functionRNAi-dependent knockdownCardiac hypertrophyLittermate controls
2011
The γ-Secretase Cleavage Product of Polycystin-1 Regulates TCF and CHOP-Mediated Transcriptional Activation through a p300-Dependent Mechanism
Merrick D, Chapin H, Baggs JE, Yu Z, Somlo S, Sun Z, Hogenesch JB, Caplan MJ. The γ-Secretase Cleavage Product of Polycystin-1 Regulates TCF and CHOP-Mediated Transcriptional Activation through a p300-Dependent Mechanism. Developmental Cell 2011, 22: 197-210. PMID: 22178500, PMCID: PMC3264829, DOI: 10.1016/j.devcel.2011.10.028.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid Precursor Protein SecretasesAnimalsApoptosisCell ProliferationCells, CulturedCystsEmbryo, NonmammalianHumansImmunoblottingImmunoprecipitationKidneyP300-CBP Transcription FactorsPhenotypePolycystic Kidney, Autosomal DominantTCF Transcription FactorsTranscription Factor CHOPTranscriptional ActivationTRPP Cation ChannelsWnt Signaling PathwayZebrafishConceptsCarboxy-terminal tailPolycystin-1P300-dependent mechanismTranscription factor TCFTranscriptional coactivator p300Cultured renal epithelial cellsΓ-secretase-mediated cleavageAutosomal dominant polycystic kidney diseaseRenal epithelial cellsTranscriptional activationZebrafish embryosCoactivator p300Γ-secretase activityNormal growth ratePKD1 expressionNull cellsProtein fragmentsCyst formationΓ-secretase inhibitionCHOP pathwayApoptosisEpithelial cellsCleavage productsPolycystic kidney diseaseExpression
2010
TLR9-Targeted Biodegradable Nanoparticles as Immunization Vectors Protect against West Nile Encephalitis
Demento SL, Bonafé N, Cui W, Kaech SM, Caplan MJ, Fikrig E, Ledizet M, Fahmy TM. TLR9-Targeted Biodegradable Nanoparticles as Immunization Vectors Protect against West Nile Encephalitis. The Journal Of Immunology 2010, 185: 2989-2997. PMID: 20660705, PMCID: PMC3753007, DOI: 10.4049/jimmunol.1000768.Peer-Reviewed Original ResearchConceptsBiodegradable nanoparticlesUnmodified nanoparticlesImmune responseNanoparticlesCell-mediated immune responsesRobust humoral responseTh1 immune responseEffector T cellsAg-specific lymphocytesTh2-biased responsesAdjuvant aluminum hydroxideWest Nile encephalitisVirus encephalitisWest Nile virusAgHumoral responseCpG oligodeoxynucleotideT cellsMouse modelLive virusInfectious agentsProtein AgVaccine developmentWN virusNile virus
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
2003
Polycystin-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
2002
Calcium-pump inhibitors induce functional surface expression of ΔF508-CFTR protein in cystic fibrosis epithelial cells
Egan ME, Glöckner-Pagel J, Ambrose C, Cahill PA, Pappoe L, Balamuth N, Cho E, Canny S, Wagner CA, Geibel J, Caplan MJ. Calcium-pump inhibitors induce functional surface expression of ΔF508-CFTR protein in cystic fibrosis epithelial cells. Nature Medicine 2002, 8: 485-492. PMID: 11984593, DOI: 10.1038/nm0502-485.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumCalcium pump inhibitorΔF508-CFTR proteinCystic fibrosis epithelial cellsCystic fibrosis transmembrane conductance regulator (CFTR) proteinCystic fibrosis cell lineFunctional surface expressionSurface expressionChaperone activityChaperone proteinsRegulator proteinPlasma membraneCystic fibrosis defectCell surfaceProteinCell linesPotential targetOptimal activityInhibitor thapsigarginEpithelial cellsExpressionCommon mutationsInhibitorsMouse modelReticulum
1999
Nongastric H+,K+-ATPase: cell biologic and functional properties.
Grishin AV, Reinhard J, Dunbar LA, Courtois-Coutry N, Wang T, Giebisch G, Caplan MJ. Nongastric H+,K+-ATPase: cell biologic and functional properties. Seminars In Nephrology 1999, 19: 421-30. PMID: 10511382.Peer-Reviewed Original ResearchConceptsATPase isoformsP-type ATPasesEndocytic regulationEndocytosis signalATPase familyCell machineryCytoplasmic tailK resorptionATPasesIon pumpsATPase isoform expressionApical surfaceIsoformsCell biologicIsoform expressionPhysiological studiesTubule epithelial cellsATPaseEpithelial cellsTransgenic miceCation transportK transportFunctional propertiesRenal K transportEndocytosisCation 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
Identification of Sorting Determinants in the C-terminal Cytoplasmic Tails of the γ-Aminobutyric Acid Transporters GAT-2 and GAT-3*
Muth T, Ahn J, Caplan M. Identification of Sorting Determinants in the C-terminal Cytoplasmic Tails of the γ-Aminobutyric Acid Transporters GAT-2 and GAT-3*. Journal Of Biological Chemistry 1998, 273: 25616-25627. PMID: 9748227, DOI: 10.1074/jbc.273.40.25616.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsCells, CulturedCloning, MolecularDogsFluorescent Antibody TechniqueGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidGenes, mycIon ChannelsKidneyMembrane ProteinsMembrane Transport ProteinsMicroscopy, ConfocalMolecular Sequence DataRecombinant Fusion ProteinsSequence DeletionConceptsC-terminal cytoplasmic tailIon transport proteinsMadin-Darby canine kidney cellsCytoplasmic tailMembrane proteinsC-terminusCanine kidney cellsTransporter familyAmino acidsBasolateral distributionTransport proteinsGAT-2Polytopic membrane proteinsProtein-based signalsProtein-protein interactionsTerminal cytoplasmic tailC-terminal sequencesKidney cellsClass of polypeptidesEpithelial cellsApical sortingPDZ domainChimeric transportersPolarized sortingSorting determinant[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
1996
Immunolocalization of ion transport proteins in human autosomal dominant polycystic kidney epithelial cells.
Brill SR, Ross KE, Davidow CJ, Ye M, Grantham JJ, Caplan MJ. Immunolocalization of ion transport proteins in human autosomal dominant polycystic kidney epithelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 10206-10211. PMID: 8816777, PMCID: PMC38362, DOI: 10.1073/pnas.93.19.10206.Peer-Reviewed Original ResearchConceptsCyst epithelial cellsEpithelial cellsCystic fibrosis transmembrane conductance regulatorIon transport proteinsFibrosis transmembrane conductance regulatorK-ATPaseApical cystic fibrosis transmembrane conductance regulatorTransmembrane conductance regulatorKidney epithelial cellsK-ATPase proteinRenal epithelial cellsCFTR proteinTransport proteinsConductance regulatorIntracellular structuresFluid-filled cystsApical membraneForskolin treatmentBasolateral surfacePermeable filter supportsApical surfaceProteinCl- channelsApical labelingAutosomal dominant polycystic kidney diseaseCell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*
Gu H, Ahn J, Caplan M, Blakely R, Levey A, Rudnick G. Cell-specific Sorting of Biogenic Amine Transporters Expressed in Epithelial Cells*. Journal Of Biological Chemistry 1996, 271: 18100-18106. PMID: 8663573, DOI: 10.1074/jbc.271.30.18100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiogenic AminesBiological TransportCarrier ProteinsCell CompartmentationCell MembraneCell PolarityCells, CulturedDogsDopamineDopamine Plasma Membrane Transport ProteinsEpithelial CellsHumansImmunohistochemistryMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsRatsRecombinant ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsSymportersConceptsMadin-Darby canine kidneyMDCK cellsLLC-PK1 cellsNeurotransmitter transportersCell surface biotinylationConfocal immunofluorescence microscopyBasolateral membraneCell-specific mechanismsEpithelial cellsBiogenic amine transportersMembrane proteinsSurface biotinylationCDNA encodingHuman DA transporterAmine transportersImmunofluorescence microscopyBiotinylating reagentTransportersPermeable filter supportsApical surfaceImmunocytochemistry resultsBasolateral mediumSurface expressionApical sideDA transporter
1994
The axonal gamma-aminobutyric acid transporter GAT-1 is sorted to the apical membranes of polarized epithelial cells.
Pietrini G, Suh YJ, Edelmann L, Rudnick G, Caplan MJ. The axonal gamma-aminobutyric acid transporter GAT-1 is sorted to the apical membranes of polarized epithelial cells. Journal Of Biological Chemistry 1994, 269: 4668-4674. PMID: 8308038, DOI: 10.1016/s0021-9258(17)41828-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBetaineCarrier ProteinsCell CompartmentationCell LineCell MembraneCell PolarityCells, CulturedDogsEpitheliumFluorescent Antibody TechniqueGABA Plasma Membrane Transport ProteinsGamma-Aminobutyric AcidIn Vitro TechniquesMembrane ProteinsMembrane Transport ProteinsNerve Tissue ProteinsOrganic Anion TransportersConceptsGamma-aminobutyric acid (GABA) transporter GAT-1MDCK cellsDistinct cell surface domainsEpithelial Madin-Darby canine kidney (MDCK) cell lineTransporter GAT-1Cell surfaceCell surface domainsCell surface biotinylationApical cell surfaceBasolateral cell surfaceEpithelial cellsBGT-1Axonal plasma membraneCell surface membraneSorting signalsCanine kidney cell lineMadin-Darby canine kidney (MDCK) cell lineGAT-1GABA transporterDistinct subdomainsKidney cell lineBetaine transporterHyperosmotic stressSurface biotinylationApical localization
1993
Functional properties of an H,K-ATPase/Na,K-ATPase chimera
Blostein R, Zhang R, Gottardi C, Caplan M. Functional properties of an H,K-ATPase/Na,K-ATPase chimera. Journal Of Biological Chemistry 1993, 268: 10654-10658. PMID: 8387526, DOI: 10.1016/s0021-9258(18)82247-5.Peer-Reviewed Original ResearchAn ion-transporting ATPase encodes multiple apical localization signals.
Gottardi CJ, Caplan MJ. An ion-transporting ATPase encodes multiple apical localization signals. Journal Of Cell Biology 1993, 121: 283-293. PMID: 8385670, PMCID: PMC2200096, DOI: 10.1083/jcb.121.2.283.Peer-Reviewed Original ResearchConceptsK-ATPaseIon-transporting ATPaseDifferential subcellular distributionEpithelial cell typesEpithelial sortingEpithelial cellsEndocytosis signalLocalization signalEndocytic pathwayMembrane proteinsPlasmalemmal domainsApical localizationMolecular signalsSubcellular distributionBeta subunitRenal proximal tubular epithelial cellsCell typesIon pumpsApical surfaceDistinct populationsFull lengthBasolateral membraneProximal tubular epithelial cellsIndependent signalsTubular epithelial cells
1992
Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture.
Pietrini G, Matteoli M, Banker G, Caplan MJ. Isoforms of the Na,K-ATPase are present in both axons and dendrites of hippocampal neurons in culture. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 8414-8418. PMID: 1326755, PMCID: PMC49930, DOI: 10.1073/pnas.89.18.8414.Peer-Reviewed Original ResearchConceptsHippocampal neuronsAlpha 1Epithelial cellsMature cultured hippocampal neuronsCultured hippocampal neuronsK-ATPase alpha subunitPolarized epithelial cell lineAlpha 3 proteinAlpha 3 isoformDistribution of isoformsEpithelial cell lineRenal epithelial cellsInfluenza glycoproteinsVesicular stomatitis virusNeuronal cellsNeuronsAlpha subunitCell linesStable transfectionStomatitis virusAxonsK-ATPaseIsoformsCellsDendrites