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 cells
1994
Kinetic heterogeneity of phosphoenzyme of Na,K-ATPase modeled by unmixed lipid phases. Competence of the phosphointermediate.
Klodos I, Post R, Forbush B. Kinetic heterogeneity of phosphoenzyme of Na,K-ATPase modeled by unmixed lipid phases. Competence of the phosphointermediate. Journal Of Biological Chemistry 1994, 269: 1734-1743. PMID: 8294422, DOI: 10.1016/s0021-9258(17)42089-8.Peer-Reviewed Original Research
1990
Biosynthesis of the Na,K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery.
Caplan MJ, Forbush B, Palade GE, Jamieson JD. Biosynthesis of the Na,K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery. Journal Of Biological Chemistry 1990, 265: 3528-3534. PMID: 2154482, DOI: 10.1016/s0021-9258(19)39801-1.Peer-Reviewed Original Research
1988
Rapid 86Rb release from an occluded state of the Na,K-pump reflects the rate of dephosphorylation or dearsenylation.
Forbush B. Rapid 86Rb release from an occluded state of the Na,K-pump reflects the rate of dephosphorylation or dearsenylation. Journal Of Biological Chemistry 1988, 263: 7961-7969. PMID: 2836403, DOI: 10.1016/s0021-9258(18)68428-5.Peer-Reviewed Original ResearchRapid release of 45Ca from an occluded state of the Na,K-pump.
Forbush B. Rapid release of 45Ca from an occluded state of the Na,K-pump. Journal Of Biological Chemistry 1988, 263: 7970-7978. PMID: 2836404, DOI: 10.1016/s0021-9258(18)68429-7.Peer-Reviewed Original ResearchConceptsNa,K-pumpNa,K-ATPaseK-pumpK-ATPasePhosphorylation of Na,K-ATPaseRelease of 45CaExposure to K+Release of 86RbApparent affinityCa2+Transport sitesK+ congenerMg2+ + ATPIntracellular faceRelease of K+Simultaneous occlusionExtracellular sitesPrevent phosphorylationCa2Exposure to Mg2Extracellular faceReleaseAbsence of PiN-methylglucamineIntracellular mediumThe interaction of amines with the occluded state of the Na,K-pump.
Forbush B. The interaction of amines with the occluded state of the Na,K-pump. Journal Of Biological Chemistry 1988, 263: 7979-7988. PMID: 2836405, DOI: 10.1016/s0021-9258(18)68430-3.Peer-Reviewed Original ResearchConceptsRelease of 86RbInteraction of aminesPresence of aminesNa,K-pumpIntracellular faceDog kidney NaK-pumpK-ATPaseEffect of aminesBenzyl amineBifunctional aminesBlock releaseKidney NaOcclusionOrganic cationsPre-incubationAminesAmine blocksTransport sitesPresence of ATPK+ siteCompetitive mannerLow affinityOccluded statePhotoaffinity labelling of a 150 kDa (Na + K + Cl)-cotransport protein from duck red cells with an analog of bumetanide
Haas M, Forbush B. Photoaffinity labelling of a 150 kDa (Na + K + Cl)-cotransport protein from duck red cells with an analog of bumetanide. Biochimica Et Biophysica Acta 1988, 939: 131-144. PMID: 3349075, DOI: 10.1016/0005-2736(88)90054-5.Peer-Reviewed Original ResearchConceptsDuck red cellsRed cellsSimultaneous presence of Na+Binding to intact cellsIncubation mediumDog kidney membraneConsistent with labelingDuck red blood cellsRed blood cellsBumetanideCotransporterRed cell membraneBlood cellsKidney membranesPresence of Na+DucksCellsCell membranePlasma membraneSDS-polyacrylamide gelsIntact cellsSDS-polyacrylamideProteinNorepinephrine
1987
Na,K,Cl-cotransport system: characterization by bumetanide binding and photolabelling.
Haas M, Forbush B. Na,K,Cl-cotransport system: characterization by bumetanide binding and photolabelling. Kidney International Supplement 1987, 23: s134-43. PMID: 3481640.Peer-Reviewed Original ResearchPhotolabeling of a 150-kDa (Na + K + Cl) cotransport protein from dog kidney with a bumetanide analogue
Haas M, Forbush B. Photolabeling of a 150-kDa (Na + K + Cl) cotransport protein from dog kidney with a bumetanide analogue. American Journal Of Physiology 1987, 253: c243-c252. PMID: 3618761, DOI: 10.1152/ajpcell.1987.253.2.c243.Peer-Reviewed Original ResearchConceptsKidney cortexBinding to kidney membranesDog kidney cortexSite of actionCotransporter proteinApical membraneAscending limbBumetanideCotransport systemHenle's loopEpithelial cellsPhotolysis mediumKidney membranesK 1/2Mammalian kidneyCrude membranesBenzophenone analoguesKidneyDog kidneyPresence of NaCortexPhotolysisSucrose density gradientsMolecular mass proteinsDogsRapid release of 42K and 86Rb from an occluded state of the Na,K-pump in the presence of ATP or ADP.
Forbush B. Rapid release of 42K and 86Rb from an occluded state of the Na,K-pump in the presence of ATP or ADP. Journal Of Biological Chemistry 1987, 262: 11104-11115. PMID: 2440883, DOI: 10.1016/s0021-9258(18)60932-9.Peer-Reviewed Original ResearchRapid release of 42K or 86Rb from two distinct transport sites on the Na,K-pump in the presence of Pi or vanadate.
Forbush B. Rapid release of 42K or 86Rb from two distinct transport sites on the Na,K-pump in the presence of Pi or vanadate. Journal Of Biological Chemistry 1987, 262: 11116-11127. PMID: 2440884, DOI: 10.1016/s0021-9258(18)60933-0.Peer-Reviewed Original ResearchMonoclonal antibody localization of Na+-K+-ATPase in the exocrine pancreas and parotid of the dog
Smith ZD, Caplan MJ, Forbush B, Jamieson JD. Monoclonal antibody localization of Na+-K+-ATPase in the exocrine pancreas and parotid of the dog. American Journal Of Physiology 1987, 253: g99-g109. PMID: 2441610, DOI: 10.1152/ajpgi.1987.253.2.g99.Peer-Reviewed Original ResearchConceptsDuct cellsAcinar cellsRenal tubular cellsInterlobular duct cellsSodium pumpMonoclonal antibody localizationDuct-derived cellsIntralobular duct cellsTubular cellsElectrolyte secretionFrozen sectionsPancreasExocrine pancreasMonoclonal antibodiesOligosaccharide determinantsParotidAntibody localizationParotid cellsAntibodiesDog pancreasThin frozen sections
1985
Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments
Kashgarian M, Biemesderfer D, Caplan M, Forbush B. Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments. Kidney International 1985, 28: 899-913. PMID: 3003443, DOI: 10.1038/ki.1985.216.Peer-Reviewed Original ResearchConceptsMonoclonal antibodiesNephron segmentsEvidence of labellingRenal tubular epithelial cellsTubular epithelial cellsK-ATPaseThick ascending limbOnly principal cellsDifferent nephron segmentsDog antigensBasal-lateral membranesSignificant antibodiesAscending limbMesangial regionHenle's loopOccasional cellsRenal medullaOuter renal medullaAbundant antibodyAntibodiesApical labelingTubule segmentsPrincipal cellsEpithelial cellsImmunocytochemical localization
1984
Na+ movement in a single turnover of the Na pump.
Forbush B. Na+ movement in a single turnover of the Na pump. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 5310-5314. PMID: 6089192, PMCID: PMC391693, DOI: 10.1073/pnas.81.17.5310.Peer-Reviewed Original ResearchAn apparatus for rapid kinetic analysis of isotopic efflux from membrane vesicles and of ligand dissociation from membrane proteins
Forbush B. An apparatus for rapid kinetic analysis of isotopic efflux from membrane vesicles and of ligand dissociation from membrane proteins. Analytical Biochemistry 1984, 140: 495-505. PMID: 6091496, DOI: 10.1016/0003-2697(84)90200-8.Peer-Reviewed Original Research
1983
[3H]bumetanide binding to membranes isolated from dog kidney outer medulla. Relationship to the Na,K,Cl co-transport system.
Forbush B, Palfrey H. [3H]bumetanide binding to membranes isolated from dog kidney outer medulla. Relationship to the Na,K,Cl co-transport system. Journal Of Biological Chemistry 1983, 258: 11787-11792. PMID: 6619143, DOI: 10.1016/s0021-9258(17)44299-2.Peer-Reviewed Original ResearchConceptsOuter medullaCl- co-transport systemDog kidney outer medullaCl- cotransport systemLoop of HenleCo-transport systemLoop diureticsBasolateral membraneKidney outer medullaProximal tubulesAscending limbLuminal membraneCotransport systemKidney cortexMedullaKidney membranesBrush borderCo-transportCrude membranesKidneyDog kidneyBinding to membranesBinding activityGradient centrifugationAssay of Na,K-ATPase in plasma membrane preparations: Increasing the permeability of membrane vesicles using sodium dodecyl sulfate buffered with bovine serum albumin
Forbush B. Assay of Na,K-ATPase in plasma membrane preparations: Increasing the permeability of membrane vesicles using sodium dodecyl sulfate buffered with bovine serum albumin. Analytical Biochemistry 1983, 128: 159-163. PMID: 6303151, DOI: 10.1016/0003-2697(83)90356-1.Peer-Reviewed Original ResearchConceptsMaximal Na,K-ATPase activityAmount of membrane proteinNa,K-ATPase activityElectric organ of eelIsolated plasma membranesNa,K-ATPaseSodium dodecyl sulfate bufferK-ATPase activityPlasma membrane preparationsTransmembrane proteinsMembrane proteinsDetergent bufferPlasma membraneOptimal activityActivity of membranesBovine serum albuminMembrane vesiclesK-ATPasePermeability of membrane vesiclesDetergentDetergent activitySulfate bufferProteinVesicular natureSerum albumin
1982
Characterization of right-side-out membrane vesicles rich in (Na,K)-ATPase and isolated from dog kidney outer medulla.
Forbush B. Characterization of right-side-out membrane vesicles rich in (Na,K)-ATPase and isolated from dog kidney outer medulla. Journal Of Biological Chemistry 1982, 257: 12678-12684. PMID: 6290476, DOI: 10.1016/s0021-9258(18)33564-6.Peer-Reviewed Original ResearchConceptsDog kidney outer medullaK)-ATPase activityK)-ATPaseKidney outer medullaOuter medullaRight-side-out membrane vesiclesMembrane vesiclesBasolateral membranePorcine trypsinMg2+ + ATPRight-side-out orientationDensity gradient centrifugationCaged ATPIntravesicular volumePresence of Na+H1 populationMedullaMembrane proteinsSucrose gradientsGradient centrifugationTrypsin-sensitiveDetergent treatmentVesicle volumeVesiclesATP