2016
CFTR-associated ligand is a negative regulator of Mrp2 expression
Li M, Soroka CJ, Harry K, Boyer JL. CFTR-associated ligand is a negative regulator of Mrp2 expression. American Journal Of Physiology - Cell Physiology 2016, 312: c40-c46. PMID: 27834195, PMCID: PMC5283898, DOI: 10.1152/ajpcell.00100.2016.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCells, CulturedChlorocebus aethiopsCOS CellsDown-RegulationGene Expression RegulationGolgi Matrix ProteinsHepatocytesHumansMaleMembrane ProteinsMembrane Transport ProteinsMiceMultidrug Resistance-Associated Protein 2Multidrug Resistance-Associated ProteinsRatsRats, Sprague-DawleySignal TransductionConceptsPull-down assaysGST pull-down assaysCOOH-terminal PDZNegative regulatorCotransfected COS-7 cellsGlutathione S-transferase fusion proteinS-transferase fusion proteinATP-binding cassette (ABC) transportersTrans-Golgi networkCystic fibrosis transmembrane conductance regulatorProtein-protein interactionsExchanger regulatory factor 1Fibrosis transmembrane conductance regulatorStreptavidin pull-down assaysTransmembrane conductance regulatorCOS-7 cellsRegulatory factor 1PDZ domainCell surface expressionPosttranscriptional regulationTransmembrane proteinPlasma membraneLLC-PK1 cellsCassette transportersCOS-7
2010
The maximal cytoprotective function of the heat shock protein 27 is dependent on heat shock protein 70
Sreedharan R, Riordan M, Thullin G, Van Why S, Siegel NJ, Kashgarian M. The maximal cytoprotective function of the heat shock protein 27 is dependent on heat shock protein 70. Biochimica Et Biophysica Acta 2010, 1813: 129-135. PMID: 20934464, PMCID: PMC3014454, DOI: 10.1016/j.bbamcr.2010.08.012.Peer-Reviewed Original ResearchConceptsHeat shock protein 70Shock protein 70Cell injuryProtein 70Heat shock protein 27Renal cell injuryExpression of HSP27Maximal cytoprotective effectShock protein 27Endogenous hspNuclear binding sitesCytoprotective effectsInjuryRenal cellsLLC-PK1 cellsProtein 27Specific siRNAHSP-70HSP70 inductionRespective controlsHSP27Particular HSP70Cytoprotective functionEnergy depletionATP depletion
2005
HSP70 binding modulates detachment of Na-K-ATPase following energy deprivation in renal epithelial cells
Riordan M, Sreedharan R, Wang S, Thulin G, Mann A, Stankewich M, Van Why S, Kashgarian M, Siegel NJ. HSP70 binding modulates detachment of Na-K-ATPase following energy deprivation in renal epithelial cells. American Journal Of Physiology. Renal Physiology 2005, 288: f1236-f1242. PMID: 15701813, DOI: 10.1152/ajprenal.00438.2004.Peer-Reviewed Original ResearchConceptsRenal epithelial cellsATP depletionMolecular chaperone Hsp70Binding of Hsp70Na-K-ATPaseFundamental cellular mechanismsRenal epithelial polarityCultured renal epithelial cellsEpithelial cellsHeat shock protein 70Protein clathrinEpithelial polarityMolecular chaperonesOverexpression of HSP70Chaperone Hsp70Shock protein 70Energy deprivationLLC-PK1 cellsStress proteinsMolecular mechanismsHSP bindingHSP70Cell lysatesCellular mechanismsATP turnover
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 membrane
2003
Hsp27 associates with actin and limits injury in energy depleted renal epithelia.
Van Why SK, Mann AS, Ardito T, Thulin G, Ferris S, Macleod MA, Kashgarian M, Siegel NJ. Hsp27 associates with actin and limits injury in energy depleted renal epithelia. Journal Of The American Society Of Nephrology 2003, 14: 98-106. PMID: 12506142, DOI: 10.1097/01.asn.0000038687.24289.83.Peer-Reviewed Original ResearchConceptsGreen fluorescence proteinFluorescence energy transferATP depletionF-actinRenal epitheliumSpecific intracellular domainsCellular ATP levelsHsp27 interactionHsp27 associatesIntracellular domainLLC-PK1 cellsFluorescence proteinLateral cell boundariesHuman HSP27Phalloidin fluorescenceActinHSP27K-ATPaseCytoskeletonControl cellsATP levelsEnergy depletionCell bodiesG cellsCells
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
Tyrosine-based Membrane Protein Sorting Signals Are Differentially Interpreted by Polarized Madin-Darby Canine Kidney and LLC-PK1 Epithelial Cells*
Roush D, Gottardi C, Naim H, Roth M, Caplan M. Tyrosine-based Membrane Protein Sorting Signals Are Differentially Interpreted by Polarized Madin-Darby Canine Kidney and LLC-PK1 Epithelial Cells*. Journal Of Biological Chemistry 1998, 273: 26862-26869. PMID: 9756932, DOI: 10.1074/jbc.273.41.26862.Peer-Reviewed Original ResearchConceptsProtein sorting signalsTyrosine-based motifLLC-PK1 cellsCytoplasmic tailSorting signalsMDCK cellsApical membraneBeta-subunit polypeptidesBasolateral membraneK-ATPase beta subunitDi-leucine motifBeta subunit proteinLLC-PK1 epithelial cellsMadin-Darby canine kidney cellsMadin-Darby canine kidneyEpithelial cell typesCanine kidney cellsK-ATPase betaHA-Y543Cytoplasmic sequencesSequence motifsSubunit polypeptidesMembrane proteinsBasolateral domainPolarized epitheliumA 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
1997
Cloned 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
1996
Cell-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 transporterIon Coupling Stoichiometry for the Norepinephrine Transporter in Membrane Vesicles from Stably Transfected Cells (∗)
Gu H, Wall S, Rudnick G. Ion Coupling Stoichiometry for the Norepinephrine Transporter in Membrane Vesicles from Stably Transfected Cells (∗). Journal Of Biological Chemistry 1996, 271: 6911-6916. PMID: 8636118, DOI: 10.1074/jbc.271.12.6911.Peer-Reviewed Original ResearchConceptsMembrane vesiclesTransmembrane ion gradientsLLC-PK1 cellsMajor substrateTransport substratesTransfected CellsStably Transfected CellsIon gradientsCoupling stoichiometryNet positive chargeDA accumulationVesiclesSubstrate moleculesTransportersNorepinephrine transporterAccumulationCellsGamma-aminobutyric acidCotransportDAGradientStoichiometrySubstrateAbsenceTransport processes
1995
Biogenic amine flux mediated by cloned transporters stably expressed in cultured cell lines: amphetamine specificity for inhibition and efflux.
Wall S, Gu H, Rudnick G. Biogenic amine flux mediated by cloned transporters stably expressed in cultured cell lines: amphetamine specificity for inhibition and efflux. Molecular Pharmacology 1995, 47: 544-550. PMID: 7700252, DOI: 10.1016/s0026-895x(25)08574-8.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-4-phenylpyridiniumAmphetaminesBiogenic MonoaminesBiological TransportCarrier ProteinsCell MembraneCells, CulturedCloning, MolecularCocaineDNA, ComplementaryDopamineDopamine Plasma Membrane Transport ProteinsHumansMazindolMembrane GlycoproteinsMembrane Transport ProteinsNerve Tissue ProteinsNeurotransmitter Uptake InhibitorsNorepinephrineNorepinephrine Plasma Membrane Transport ProteinsSerotoninSerotonin Plasma Membrane Transport ProteinsStimulation, ChemicalSubstrate SpecificitySymportersTransfectionConceptsBiogenic amine transportersCell linesAmine transportersRat serotonin transporterCultured cell linesInhibitor of transportRat dopamine transporterHuman norepinephrine transporterPlasma membraneLLC-PK1 cellsSubstrate effluxSubstrate influxDopamine transporterNorepinephrine transporterAmphetamine derivativesTransportersSerotonin transporterEffluxDistinct patternsP-chloroamphetamineAmine substratesCellsInhibited transportCDNAInhibitors
1994
Porcine myosin-VI: characterization of a new mammalian unconventional myosin.
Hasson T, Mooseker M. Porcine myosin-VI: characterization of a new mammalian unconventional myosin. Journal Of Cell Biology 1994, 127: 425-440. PMID: 7929586, PMCID: PMC2120210, DOI: 10.1083/jcb.127.2.425.Peer-Reviewed Original Research
1992
Immunocytochemical characterization of Na(+)-H+ exchanger isoform NHE-1 in rabbit kidney
Biemesderfer D, Reilly RF, Exner M, Igarashi P, Aronson PS. Immunocytochemical characterization of Na(+)-H+ exchanger isoform NHE-1 in rabbit kidney. American Journal Of Physiology 1992, 263: f833-f840. PMID: 1279986, DOI: 10.1152/ajprenal.1992.263.5.f833.Peer-Reviewed Original ResearchConceptsNHE-1 proteinNHE-1Rabbit kidneyDistal convoluted tubuleMultiple nephron segmentsThick ascending limbWestern blot analysisRenal cortexRabbit renal cortexConvoluted tubulesProximal tubulesAscending limbRabbit nephronTubule cellsGuinea pigsLLC-PK1 cellsNephron segmentsIndirect immunofluorescenceKidneyImmunocytochemical characterizationPrincipal cellsExchanger isoformsBlot analysisFusion proteinAntibodiesIsolation of putative voltage-gated epithelial K-channel isoforms from rabbit kidney and LLC-PK1 cells
Desir GV, Hamlin HA, Puente E, Reilly RF, Hildebrandt F, Igarashi P. Isolation of putative voltage-gated epithelial K-channel isoforms from rabbit kidney and LLC-PK1 cells. American Journal Of Physiology 1992, 262: f151-f157. PMID: 1733291, DOI: 10.1152/ajprenal.1992.262.1.f151.Peer-Reviewed Original ResearchConceptsDeduced amino acid sequenceAmino acid sequenceAcid sequenceVoltage-gated K channelsRabbit genomic DNAPutative transmembrane segmentsShaker-like genesPutative voltage sensorShaker gene familyVoltage-gated potassium channelsGene familyShaker proteinRenal epithelial cellsTransmembrane segmentsSequence similarityRabbit cDNAEpithelial cell lineSouthern analysisProtein sequencesLLC-PK1 cellsDifferent genesGenomic DNAKidney cDNACDNAS4 segment
1991
cDNA cloning and immunolocalization of a Na(+)-H+ exchanger in LLC-PK1 renal epithelial cells
Reilly RF, Hildebrandt F, Biemesderfer D, Sardet C, Pouyssegur J, Aronson PS, Slayman CW, Igarashi P. cDNA cloning and immunolocalization of a Na(+)-H+ exchanger in LLC-PK1 renal epithelial cells. American Journal Of Physiology 1991, 261: f1088-f1094. PMID: 1661081, DOI: 10.1152/ajprenal.1991.261.6.f1088.Peer-Reviewed Original ResearchConceptsLLC-PK1 cellsFusion proteinAmino-terminal hydrophobic regionLLC-PK1 renal epithelial cellsHydrophobic regionAmino acid sequenceConfluent LLC-PK1 cellsRelative molecular massRenal epithelial cellsSignificant homologyHuman proteinsCDNA cloningAcid sequenceNucleotide identityHuman sequenceLibrary screeningCDNAMolecular massPolymerase chain reactionAmino acidsApical membraneProteinConfocal microscopyHydrophilic domainsLLC-PK1Molecular biology of renal Na(+)-H+ exchangers.
Igarashi P, Reilly RF, Hildebrandt F, Biemesderfer D, Rebouças NA, Slayman CW, Aronson PS. Molecular biology of renal Na(+)-H+ exchangers. Kidney International Supplement 1991, 33: s84-9. PMID: 1653876.Commentaries, Editorials and LettersConceptsKb cDNALLC-PK1 cellsSteady-state transcript levelsPlasma membrane proteinsMembrane-associated domainSequence of cDNACDNA library screeningAmino acid sequenceExchanger gene expressionNorthern blot analysisEvolutionary conservationRenal epithelial cellsCytoplasmic domainMembrane proteinsRegulation of intracellularAcid sequenceTranscript levelsUntranslated regionGene expressionSimilar transcriptsCDNALibrary screeningMolecular biologyPolymerase chain reactionBlot analysis
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