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
Renal Cystic Proteins in the Olfactory Epithelium (OE)
Pluznick J, Rodriguez‐Gil D, Hull M, Mistry K, Gattone V, Johnson C, Weatherbee S, Greer C, Caplan M. Renal Cystic Proteins in the Olfactory Epithelium (OE). The FASEB Journal 2010, 24: 1002.17-1002.17. DOI: 10.1096/fasebj.24.1_supplement.1002.17.Peer-Reviewed Original ResearchMutant animalsPolycystin-2Olfactory epitheliumIndividual olfactory receptorsDisease-causing mutationsCilia formationΑ-tubulin stainingMurine olfactory epitheliumMature olfactory neuronsMKS3Olfactory receptorsOlfactory neuronsProteinDendritic knobsCiliaPhysiological activityMutant miceAC3 expressionVitro dataMutant ratsRT-PCRSyndrome 1Similar reductionExpressionRats
2009
Localization of proteins associated with renal cystic diseases to the olfactory epithelium
Pluznick J, Rodriguez‐Gil D, Mistry K, Hull M, Johnson C, Greer C, Caplan M. Localization of proteins associated with renal cystic diseases to the olfactory epithelium. The FASEB Journal 2009, 23: 796.11-796.11. DOI: 10.1096/fasebj.23.1_supplement.796.11.Peer-Reviewed Original ResearchFunctional expression of the olfactory signaling system in the kidney
Pluznick JL, Zou DJ, Zhang X, Yan Q, Rodriguez-Gil DJ, Eisner C, Wells E, Greer CA, Wang T, Firestein S, Schnermann J, Caplan MJ. Functional expression of the olfactory signaling system in the kidney. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 2059-2064. PMID: 19174512, PMCID: PMC2644163, DOI: 10.1073/pnas.0812859106.Peer-Reviewed Original ResearchConceptsGlomerular filtration ratePlasma renin levelsMacula densa cellsCOX-2 expressionRenal distal nephronOlfactory G-proteinMDS cell linesOlfactory receptorsRenin levelsRenin secretionFiltration rateNNOS activityTubuloglomerular feedbackDistal nephronOlfactory epitheliumRenal tubulesGFR regulationAdenylate cyclaseG proteinsCell linesSensory roleKidneyFunctional expressionOlfactionExpression
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
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
2000
The Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*
Asano S, Kawada K, Kimura T, Grishin A, Caplan M, Takeguchi N. The Roles of Carbohydrate Chains of the β-Subunit on the Functional Expression of Gastric H+,K+-ATPase*. Journal Of Biological Chemistry 2000, 275: 8324-8330. PMID: 10722662, DOI: 10.1074/jbc.275.12.8324.Peer-Reviewed Original ResearchConceptsAlpha/beta assemblyN-glycosylation sitesATPase activityBeta assemblyPutative N-glycosylation sitesCarbohydrate chainsAlpha/beta complexSingle carbohydrate chainCatalytic subunitSurface deliveryFunctional enzymeAsparagine residuesAlpha subunitΒ-subunitBeta complexDelivery mechanismFunctional expressionComplete lossATPaseAssemblyExpressionSubunits
1998
[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
Functional expression of the cDNA encoded by the human ATP1AL1 gene
Grishin AV, Bevensee MO, Modyanov NN, Rajendran V, Boron WF, Caplan MJ. Functional expression of the cDNA encoded by the human ATP1AL1 gene. American Journal Of Physiology 1996, 271: f539-f551. PMID: 8853415, DOI: 10.1152/ajprenal.1996.271.3.f539.Peer-Reviewed Original ResearchConceptsHuman ATP1AL1 geneAcute loweringNH4Cl pulseUptake activityHEK-293 cellsSpontaneous intracellularMM ouabainProtein expressionCOS cellsATP1AL1Polyclonal antibodiesPH-sensitive dyeOuabainBeta-subunit cDNAExtrusion activityCellsK-ATPaseTransfection studiesSame cellsFunctional expressionBeta complexExpressionDependent ATPaseEndplasmic reticulumProtein
1989
Polarized distribution of Na+,K+-ATPase in giant cells elicited in vivo and in vitro.
Vignery A, Niven-Fairchild T, Ingbar DH, Caplan M. Polarized distribution of Na+,K+-ATPase in giant cells elicited in vivo and in vitro. Journal Of Histochemistry & Cytochemistry 1989, 37: 1265-1271. PMID: 2546991, DOI: 10.1177/37.8.2546991.Peer-Reviewed Original ResearchConceptsPlasma membranePolarized distributionAdherent plasma membraneGiant cell differentiationLysosomal membrane antigenAlpha subunit synthesisSuitable model systemSpecialized functionsCell differentiationBiochemical studiesCell surfaceLysosomal componentsCell formationATPase expressionGiant cell formationModel systemATPaseExpressionCells