2017
Linaclotide activates guanylate cyclase‐C/cGMP/protein kinase‐II‐dependent trafficking of CFTR in the intestine
Ahsan K, Tchernychev B, Kessler MM, Solinga RM, Arthur D, Linde CI, Silos‐Santiago I, Hannig G, Ameen NA. Linaclotide activates guanylate cyclase‐C/cGMP/protein kinase‐II‐dependent trafficking of CFTR in the intestine. Physiological Reports 2017, 5: e13299. PMID: 28592587, PMCID: PMC5471438, DOI: 10.14814/phy2.13299.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineCell Line, TumorCell MembraneCyclic AMP-Dependent Protein KinasesCyclic GMPCyclic GMP-Dependent Protein Kinase Type IICystic Fibrosis Transmembrane Conductance RegulatorGuanylyl Cyclase C AgonistsHumansIntestinal MucosaMalePeptidesProtein TransportRatsRats, Sprague-DawleyReceptors, Guanylate Cyclase-CoupledSignal TransductionConceptsRat intestinal loopsLinaclotide treatmentFluid secretionIntestinal loopsCystic fibrosis transmembrane conductance regulatorCell surfaceFibrosis transmembrane conductance regulatorCell surface traffickingChronic idiopathic constipationIrritable bowel syndromeTransmembrane conductance regulatorIntestinal fluid secretionCell surface translocationReceptor guanylyl cyclaseHuman intestinal tissueCaco-2BBe cellsCFTR traffickingCFTR pathwaySubapical compartmentCellular signalingCGMP/PKGProtein kinaseSurface biotinylationIdiopathic constipationPathway componentsAP2 α modulates cystic fibrosis transmembrane conductance regulator function in the human intestine
Kumari V, Desai S, Ameen NA. AP2 α modulates cystic fibrosis transmembrane conductance regulator function in the human intestine. Journal Of Cystic Fibrosis 2017, 16: 327-334. PMID: 28438500, PMCID: PMC5502754, DOI: 10.1016/j.jcf.2017.03.012.Peer-Reviewed Original Research
2016
Identification of intestinal ion transport defects in microvillus inclusion disease
Kravtsov DV, Ahsan MK, Kumari V, van Ijzendoorn SC, Reyes-Mugica M, Kumar A, Gujral T, Dudeja PK, Ameen NA. Identification of intestinal ion transport defects in microvillus inclusion disease. AJP Gastrointestinal And Liver Physiology 2016, 311: g142-g155. PMID: 27229121, PMCID: PMC4967175, DOI: 10.1152/ajpgi.00041.2016.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingCaco-2 CellsChloride-Bicarbonate AntiportersCystic Fibrosis Transmembrane Conductance RegulatorEnterocytesGene Expression RegulationHumansIon TransportJejunumMalabsorption SyndromesMembrane Transport ProteinsMicrovilliMucolipidosesMyosin Heavy ChainsMyosin Type VPhenotypePhosphoproteinsRNA InterferenceSignal TransductionSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersSulfate TransportersTranscription FactorsTransfectionYAP-Signaling ProteinsConceptsMicrovillus inclusion diseaseStool lossVillus atrophyInclusion diseaseEnterocyte maturationMicrovillus inclusionsIntestinal fluid transportIntestinal cell modelIon transport defectImmunohistochemical stainingSecretory diarrheaBrush border defectsImmature enterocytesC2BBe cellsT84 cellsElectrophysiological approachesCFTR ion transportBB membraneLoss of MYO5BEnterocytesFunctional CFTRDiarrheaAtrophyFunction mutationsCFTR localization
2013
Functional vacuolar ATPase (V-ATPase) proton pumps traffic to the enterocyte brush border membrane and require CFTR
Collaco AM, Geibel P, Lee BS, Geibel JP, Ameen NA. Functional vacuolar ATPase (V-ATPase) proton pumps traffic to the enterocyte brush border membrane and require CFTR. American Journal Of Physiology - Cell Physiology 2013, 305: c981-c996. PMID: 23986201, PMCID: PMC4109618, DOI: 10.1152/ajpcell.00067.2013.Peer-Reviewed Original ResearchConceptsV-ATPaseCystic fibrosis transmembrane conductance regulator (CFTR) channelV-ATPase complexV-ATPase functionBrush border membraneProton effluxRat Brunner's glandsIntestinal cellsCAMP/PKACaco-2BBe cellsBorder membraneApical domainCoimmunoprecipitation studiesCFTR distributionVacuolar ATPasesSubapical cytoplasmSpecific subunitsCAMP stimulationProton pumpCAMP treatmentEnterocyte brush border membraneSodium-hydrogen exchangerHydrogen exchangerApical membraneCFTRRegulated traffic of anion transporters in mammalian Brunner's glands: a role for water and fluid transport
Collaco AM, Jakab RL, Hoekstra NE, Mitchell KA, Brooks A, Ameen NA. Regulated traffic of anion transporters in mammalian Brunner's glands: a role for water and fluid transport. AJP Gastrointestinal And Liver Physiology 2013, 305: g258-g275. PMID: 23744739, PMCID: PMC3742856, DOI: 10.1152/ajpgi.00485.2012.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnion Transport ProteinsAquaporin 5BicarbonatesBiological TransportBrunner GlandsCarbacholCeliac DiseaseChloridesCyclic AMPCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDuodenumHumansMaleProtonsRatsRats, Sprague-DawleySecond Messenger SystemsVacuolar Proton-Translocating ATPasesWaterConceptsCystic fibrosis transmembrane conductance regulatorV-ATPaseProton-pumping vacuolar ATPaseApical membraneDistinct membrane domainsFibrosis transmembrane conductance regulatorRat Brunner's glandsTransmembrane conductance regulatorSodium bicarbonate cotransporterAnion transportersApical traffickingMembrane domainsChloride cotransporter 1Secretion of glycoproteinsVacuolar ATPaseSecond messenger activationTransporter localizationConductance regulatorSubcellular distributionAquaporin 5 water channelFunctional transportPKA inhibitorAntimicrobial peptidesTransportersBasolateral membrane
2000
Cellular localization of the cystic fibrosis transmembrane conductance regulator in mouse intestinal tract
Ameen N, Alexis J, Salas P. Cellular localization of the cystic fibrosis transmembrane conductance regulator in mouse intestinal tract. Histochemistry And Cell Biology 2000, 114: 69-75. PMID: 10959824, DOI: 10.1007/s004180000164.Peer-Reviewed Original ResearchConceptsMouse intestinal tractCystic fibrosisIntestinal tractCystic fibrosis transmembrane conductance regulatorSmall intestinal obstructionSevere gastrointestinal diseasePathophysiology of CFMouse model systemFibrosis transmembrane conductance regulatorVillus distributionTransmembrane conductance regulatorIntestinal obstructionDifferent phenotypic expressionsCF intestineGastrointestinal diseasesBicarbonate secretionTransgenic miceHuman CF diseaseSmall intestineDisease expressionImmunoblot techniqueLethal obstructionMouse intestineMiceConductance regulatorMicrovillus Inclusion Disease: A Genetic Defect Affecting Apical Membrane Protein Traffic in Intestinal Epithelium
Ameen N, Salas P. Microvillus Inclusion Disease: A Genetic Defect Affecting Apical Membrane Protein Traffic in Intestinal Epithelium. Traffic 2000, 1: 76-83. PMID: 11208062, DOI: 10.1034/j.1600-0854.2000.010111.x.Peer-Reviewed Original ResearchConceptsMicrovillus inclusion diseaseApical membrane trafficMembrane protein trafficVacuolar apical compartmentApical membrane markersMicrovillus inclusionsF-actin layerBasolateral proteinsFirst genetic defectMembrane trafficTissue culture epithelial cellsProtein trafficApical exocytosisLater stepsApical membraneMembrane markersTerminal webImmunofluorescence analysisApical cytoplasmGenetic defectsEpithelial cellsProteinApical compartmentIntestinal epitheliumNormal microtubules
1995
A unique subset of rat and human intestinal villus cells express the cystic fibrosis transmembrane conductance regulator
Ameen N, Ardito T, Kashgarian M, Marino C. A unique subset of rat and human intestinal villus cells express the cystic fibrosis transmembrane conductance regulator. Gastroenterology 1995, 108: 1016-1023. PMID: 7535272, DOI: 10.1016/0016-5085(95)90198-1.Peer-Reviewed Original ResearchConceptsProximal small intestineCrypt epithelial cellsVillus cellsSmall intestineHuman proximal small intestineCystic fibrosis transmembrane conductance regulatorEpithelial cellsSurface marker expressionFibrosis transmembrane conductance regulatorBrush border sucraseTransmembrane conductance regulatorIntestinal villus cellsBACKGROUND/Marker antibodiesMarker expressionUnique subsetVillus enterocytesConductance regulatorIntestineLactase expressionBrush border