2000
Basolateral K-Cl Cotransporter Regulates Colonic Potassium Absorption in Potassium Depletion*
Sangan P, Brill S, Sangan S, Forbush B, Binder H. Basolateral K-Cl Cotransporter Regulates Colonic Potassium Absorption in Potassium Depletion*. Journal Of Biological Chemistry 2000, 275: 30813-30816. PMID: 10878016, DOI: 10.1074/jbc.m003931200.Peer-Reviewed Original ResearchConceptsK-Cl cotransporterMembrane HK-Cl cotransportActive potassium absorptionProtein expressionBasolateral membranePotassium absorptionK-ATPaseNorthern blot analysisKCC1 mRNACoordinated regulationAlpha-subunit mRNABeta-subunit mRNAMRNA abundanceBlot analysisMRNAExpressionProteinMembraneCotransporterDepletionRat distal colonCDNAKCC1
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
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
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 state
1987
Rapid 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 Research
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 Research
1983
Assay 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 albuminNative Membranes from Dog Kidney Outer Medulla, Enriched in Na,K-ATPase and Vesicular in Nature
Forbush B. Native Membranes from Dog Kidney Outer Medulla, Enriched in Na,K-ATPase and Vesicular in Nature. Current Topics In Membranes 1983, 19: 113-118. DOI: 10.1016/s0070-2161(08)60556-0.Peer-Reviewed Original ResearchDog kidney outer medullaNa,K-ATPaseOuter medullaKidney outer medullaK-ATPaseNa,K-ATPase activityActivity of Na,K-ATPaseK-ATPase activityMembrane vesiclesSucrose gradient centrifugationMedullaNative membranesMammalian kidneyIncreased permeabilityCrude microsomal fractionGradient centrifugationCentrifugation mediumMicrosomal membranesCardiotonic Steroid Binding to Na,K-ATPase
Forbush B. Cardiotonic Steroid Binding to Na,K-ATPase. Current Topics In Membranes 1983, 19: 167-201. DOI: 10.1016/s0070-2161(08)60568-7.Peer-Reviewed Original Research
1979
Evidence that ouabain binds to the same large polypeptide chain of dimeric Na,K-ATPase that is phosphorylated from Pi.
Forbush B, Hoffman J. Evidence that ouabain binds to the same large polypeptide chain of dimeric Na,K-ATPase that is phosphorylated from Pi. Biochemistry 1979, 18: 2308-15. PMID: 221003, DOI: 10.1021/bi00578a027.Peer-Reviewed Original Research
1978
Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase.
Forbush B, Kaplan J, Hoffman J. Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the Na, K-ATPase. Biochemistry 1978, 17: 3667-76. PMID: 210802, DOI: 10.1021/bi00610a037.Peer-Reviewed Original Research