2009
Sites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity
Rinehart J, Maksimova YD, Tanis JE, Stone KL, Hodson CA, Zhang J, Risinger M, Pan W, Wu D, Colangelo CM, Forbush B, Joiner CH, Gulcicek EE, Gallagher PG, Lifton RP. Sites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity. Cell 2009, 138: 525-536. PMID: 19665974, PMCID: PMC2811214, DOI: 10.1016/j.cell.2009.05.031.Peer-Reviewed Original ResearchConceptsIntrinsic transport activityK-Cl cotransporterTransport activityCell volume regulationRegulated phosphorylationRNA interferenceAlanine substitutionsCultured cellsHomologous sitesKCC activityCl exitWNK1 expressionNeonatal mouse brainVolume regulationNeuronal functionHypotonic conditionsActive cotransportPhosphorylationIntracellular chloride concentrationCotransporter activityKCC3Human red blood cellsKCC2 activationFundamental roleMouse brain
2006
The Residues Determining Differences in Ion Affinities among the Alternative Splice Variants F, A, and B of the Mammalian Renal Na-K-Cl Cotransporter (NKCC2)*
Giménez I, Forbush B. The Residues Determining Differences in Ion Affinities among the Alternative Splice Variants F, A, and B of the Mammalian Renal Na-K-Cl Cotransporter (NKCC2)*. Journal Of Biological Chemistry 2006, 282: 6540-6547. PMID: 17186942, DOI: 10.1074/jbc.m610780200.Peer-Reviewed Original ResearchExpression of the basolateral Na–K–Cl cotransporter during mouse nephrogenesis and embryonic development
Heuvel G, Payne J, Igarashi P, Forbush B. Expression of the basolateral Na–K–Cl cotransporter during mouse nephrogenesis and embryonic development. Gene Expression Patterns 2006, 6: 1000-1006. PMID: 16814616, DOI: 10.1016/j.modgep.2006.04.004.Peer-Reviewed Original ResearchConceptsIn situ hybridizationNa-K-Cl cotransporterDorsal root ganglionBranching ureteric budEndocapillary cellsPeripheral nervous systemRoot ganglionTooth budsNasal epitheliumMouse nephrogenesisChoroid plexusSubmandibular glandMature nephronsUreteric budNorthern blot analysisSLC12A2Nervous systemMesenchymal cellsNKCC1Blot analysisMetanephroiNephric structuresGlomeruliMiceEmbryonic development
2004
WNK4 regulates apical and basolateral Cl– flux in extrarenal epithelia
Kahle KT, Gimenez I, Hassan H, Wilson FH, Wong RD, Forbush B, Aronson PS, Lifton RP. WNK4 regulates apical and basolateral Cl– flux in extrarenal epithelia. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 2064-2069. PMID: 14769928, PMCID: PMC357052, DOI: 10.1073/pnas.0308434100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCarrier ProteinsCell PolarityChloridesEpitheliumHumansImmunohistochemistryIon TransportKidneyMembrane ProteinsMembrane Transport ProteinsMiceOocytesProtein Serine-Threonine KinasesRNA, MessengerSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 2Sulfate TransportersXenopus laevisConceptsCl fluxBlood-brain barrierUnrelated ion channelsActivity of mediatorsWNK4 mRNABile ductPancreatic ductExtrarenal expressionExtrarenal tissuesCl(-) handlingPseudohypoaldosteronism type IIChannel ROMKNaCl reabsorptionSerine-threonine kinase WNK4Specialized endotheliumExchanger SLC26A6NaCl cotransporterWNK4 effectsColonic cryptsEpitheliumVariable inhibitionSweat ductsTight junctionsKidneyElectrolyte flux
2003
Short-term Stimulation of the Renal Na-K-Cl Cotransporter (NKCC2) by Vasopressin Involves Phosphorylation and Membrane Translocation of the Protein*
Giménez I, Forbush B. Short-term Stimulation of the Renal Na-K-Cl Cotransporter (NKCC2) by Vasopressin Involves Phosphorylation and Membrane Translocation of the Protein*. Journal Of Biological Chemistry 2003, 278: 26946-26951. PMID: 12732642, DOI: 10.1074/jbc.m303435200.Peer-Reviewed Original ResearchConceptsNa-K-Cl cotransporterRenal Na-K-Cl cotransporterCell membrane compartmentsRegulatory threonineMembrane compartmentsAntidiuretic hormone vasopressinPhosphospecific antibodiesMembrane translocationAmino terminusCytoplasmic vesiclesNKCC2 phosphorylationShort-term activationApical membranePhosphorylationTerm activationHormone vasopressinShort-term stimulationThick ascending limbProteinTranslocationCotransporterNKCC2ActivationAscending limbMorphometric analysis
1995
Cloning, embryonic expression, and alternative splicing of a murine kidney-specific Na-K-Cl cotransporter
Igarashi P, Heuvel G, Payne J, Forbush B. Cloning, embryonic expression, and alternative splicing of a murine kidney-specific Na-K-Cl cotransporter. American Journal Of Physiology 1995, 269: f405-f418. PMID: 7573490, DOI: 10.1152/ajprenal.1995.269.3.f405.Peer-Reviewed Original ResearchConceptsNa-K-Cl cotransporterExpression of NKCC2In situ hybridizationCassette exonsRenal Na-K-Cl cotransporterOuter medullaAscending limbAlternative splicingInner stripe of outer medullaPotential sites of phosphorylationAdenosine 3',5'-cyclic monophosphate-dependent protein kinaseDays post coitusFull-length cDNAAnchored polymerase chain reactionSites of phosphorylationConsensus splice donorLoop of HenleS-shaped bodiesProtein kinase CNorthern blot analysisPattern of expressionGenomic clonesNKCC2Outer stripeProtein sequencesLocalization of the renal Na−K−Cl cotransporter gene (Slc 12a1) on mouse Chromosome 2
Quaggin S, Payne J, Forbush B, Igarashi P. Localization of the renal Na−K−Cl cotransporter gene (Slc 12a1) on mouse Chromosome 2. Mammalian Genome 1995, 6: 557-558. PMID: 8589530, DOI: 10.1007/bf00356178.Peer-Reviewed Original Research
1993
Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase.
Mercer R, Biemesderfer D, Bliss D, Collins J, Forbush B. Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase. Journal Of Cell Biology 1993, 121: 579-586. PMID: 8387529, PMCID: PMC2119561, DOI: 10.1083/jcb.121.3.579.Peer-Reviewed Original ResearchConceptsNa,K-ATPaseGamma subunitK-ATPaseSmall membrane proteinsN-linked glycosylationTissue-specific fashionCardiac glycoside bindingGamma subunit mRNAGamma-specific antibodiesNorthern blot analysisHydropathy analysisSequenced proteinsNAB-ouabainMembrane proteinsGamma polypeptidesMolecular cloningGlycoside bindingSmall proteinsNephron segmentsBeta subunitSubunit mRNAAlpha subunitSubunitAmino acidsHydrophobic domains
1992
The Na-K-Cl cotransport protein of shark rectal gland. I. Development of monoclonal antibodies, immunoaffinity purification, and partial biochemical characterization.
Lytle C, Xu J, Biemesderfer D, Haas M, Forbush B. The Na-K-Cl cotransport protein of shark rectal gland. I. Development of monoclonal antibodies, immunoaffinity purification, and partial biochemical characterization. Journal Of Biological Chemistry 1992, 267: 25428-25437. PMID: 1460038, DOI: 10.1016/s0021-9258(19)74059-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodies, MonoclonalBenzophenonesBlotting, WesternCarrier ProteinsCell MembraneChloridesCholic AcidsChromatography, AffinityChromatography, High Pressure LiquidChromatography, Ion ExchangeDogfishElectrophoresis, Polyacrylamide GelFluorescent Antibody TechniqueMembrane ProteinsMiceMice, Inbred BALB CMolecular Sequence DataMolecular WeightPeptide FragmentsPotassiumRectumSebaceous GlandsSodiumSodium-Potassium-Chloride SymportersSulfanilamidesConceptsNa-K-Cl cotransport proteinNa-K-ClCotransporter proteinNa-K-Cl cotransporterMonoclonal antibodiesShark rectal glandLoop diureticsBasolateral membraneApical membraneTransport of NaRepresentative antibodiesCotransporterCoupled transport of NaAntibodiesPattern of recognitionTreated with N-glycanaseGland secretory cellsImmunoelectron microscopyCell membranePlasma membraneEpitopesPhysiological evidenceSecretory cellsProteolytic fragments
1991
[3H]bumetanide binding to mouse kidney membranes: identification of corresponding membrane proteins
Haas M, Dunham P, Forbush B. [3H]bumetanide binding to mouse kidney membranes: identification of corresponding membrane proteins. American Journal Of Physiology 1991, 260: c791-c804. PMID: 2018111, DOI: 10.1152/ajpcell.1991.260.4.c791.Peer-Reviewed Original ResearchMeSH KeywordsAffinity LabelsAnimalsBenzophenonesBumetanideCarcinoma, Ehrlich TumorCarrier ProteinsCell FractionationCell MembraneCentrifugation, Density GradientFemaleKidneyKidney CortexKidney MedullaKineticsMembrane ProteinsMiceProtein BindingSodium-Potassium-Chloride SymportersSulfanilamidesTritiumConceptsMouse kidney membranesKidney membranesNa-K-Cl cotransport systemNa-K-ClLow-affinity peakDog kidney membraneMouse Ehrlich ascites tumor cellsMouse kidney proteinsDog kidneyCrude plasma membranesTumor cellsWestern blot analysisEhrlich ascites tumor cellsCotransport systemAscites tumor cellsMouse kidneyMiceStaining profileLow-affinity sitesWestern blottingBinding sitesAntiserum cross-reactedKidneyBlot analysisKidney proteins
1987
Monoclonal 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