1999
Role of Phosphorylation of Alzheimer’s Amyloid Precursor Protein during Neuronal Differentiation
Ando K, Oishi M, Takeda S, Iijima K, Isohara T, Nairn A, Kirino Y, Greengard P, Suzuki T. Role of Phosphorylation of Alzheimer’s Amyloid Precursor Protein during Neuronal Differentiation. Journal Of Neuroscience 1999, 19: 4421-4427. PMID: 10341243, PMCID: PMC6782598, DOI: 10.1523/jneurosci.19-11-04421.1999.Peer-Reviewed Original Research
1997
Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA
Cheng X, Höög J, Nairn A, Greengard P, Aperia A. Regulation of rat Na+-K+-ATPase activity by PKC is modulated by state of phosphorylation of Ser-943 by PKA. American Journal Of Physiology 1997, 273: c1981-c1986. PMID: 9435504, DOI: 10.1152/ajpcell.1997.273.6.c1981.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionAnimalsColforsinCOS CellsCyclic AMPCyclic AMP-Dependent Protein KinasesCytosolDichlororibofuranosylbenzimidazoleEnzyme ActivationHomeostasisIsoenzymesKineticsMutagenesis, Site-DirectedPhorbol 12,13-DibutyratePhosphorylationProtein Kinase CRatsRecombinant ProteinsSerineSodium-Potassium-Exchanging ATPaseThionucleotidesTransfectionConceptsProtein kinase AProtein kinase CATPase alpha 1State of phosphorylationEffect of PKCWild-type enzymeSpecific PKA activatorActivity of PKCEnzyme activityAlpha 1Direct phosphorylationCOS cellsATPase alphaKinase ASer-23Kinase CPKA activatorPhosphorylationPKA systemPhorbol esterATPase activityMutantsEffect of PDBuCellsInhibitionCardiac Myocytes Gap Junctions: Phosphorylation of CX43 through a Protein Kinase C-Dependent Pathway
Sáez J, Nairn A, Czernik A, Fishman G, Spray D, Hertzberg E. Cardiac Myocytes Gap Junctions: Phosphorylation of CX43 through a Protein Kinase C-Dependent Pathway. Series Of The Centro De Estudios Científicos 1997, 381-394. DOI: 10.1007/978-1-4899-1795-9_22.Peer-Reviewed Original Research
1996
Amyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*
Desdouits F, Buxbaum J, Desdouits-Magnen J, Nairn A, Greengard P. Amyloid β Peptide Formation in Cell-free Preparations REGULATION BY PROTEIN KINASE C, CALMODULIN, AND CALCINEURIN*. Journal Of Biological Chemistry 1996, 271: 24670-24674. PMID: 8798734, DOI: 10.1074/jbc.271.40.24670.Peer-Reviewed Original ResearchConceptsProtein kinase CAction of PKCCell-free systemIntact cellsKinase CProtein phosphatase calcineurinCell-permeant inhibitorStimulation of PKCSpecific peptide inhibitorPhosphatase calcineurinMolecular mechanismsCalcineurinPeptide inhibitorRegulationShort peptidesCalmodulinCellsBeta peptideInhibitorsPeptide formationPeptidesMajor constituentsPronounced inhibitionCyclosporin ASingle substrateActivation of a Calcium-Calmodulin-dependent Protein Kinase I Cascade in PC12 Cells*
Aletta J, Selbert M, Nairn A, Edelman A. Activation of a Calcium-Calmodulin-dependent Protein Kinase I Cascade in PC12 Cells*. Journal Of Biological Chemistry 1996, 271: 20930-20934. PMID: 8702851, DOI: 10.1074/jbc.271.34.20930.Peer-Reviewed Original ResearchConceptsCaM kinase IDependent protein kinase IKinase IProtein kinase IPC12 cellsIntracellular Ca2L-type voltage-dependent Ca2PC12 pheochromocytoma cellsBlockade of Ca2Cellular regulationBiphasic phosphorylationVoltage-dependent Ca2Depolarization-induced activationPhosphorylationCalcium-calmodulinActivity of Ca2Extracellular Ca2I activityAcute formPheochromocytoma cellsPrior depolarizationIntracellular phosphorylationCellsActivationCa2
1994
Regulation of CFTR channel gating
Gadsby D, Nairn A. Regulation of CFTR channel gating. Trends In Biochemical Sciences 1994, 19: 513-518. PMID: 7531880, DOI: 10.1016/0968-0004(94)90141-4.Peer-Reviewed Original ResearchConceptsChannel gatingCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelAMP-dependent protein kinaseCFTR channel gatingReceptor-mediated activationRegulatory domainProtein kinaseATP hydrolysisCFTR channelsCl- channelsEpithelial cellsChannel openingComplex mechanismsCellsRecent advancesKinaseGenesPhosphorylationSerineGatingCFTRMutationsRegulationStemActivationCorrelation between protein kinase C binding proteins and substrates in REF52 cells.
Hyatt S, Liao L, Aderem A, Nairn A, Jaken S. Correlation between protein kinase C binding proteins and substrates in REF52 cells. Molecular Cancer Research 1994, 5: 495-502. PMID: 8049156.Peer-Reviewed Original ResearchMeSH KeywordsBlotting, WesternCalmodulin-Binding ProteinsCell LineCell Line, TransformedCell Transformation, NeoplasticDown-RegulationIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane ProteinsMolecular WeightMyristoylated Alanine-Rich C Kinase SubstratePhosphatidylserinesPhosphorylationProtein BindingProtein DenaturationProtein Kinase CProtein Kinase C-alphaProteinsSolubilityConceptsProtein kinase CREF52 cellsPKC substrateKinase CBinding proteinProperties of PKCCalmodulin-Sepharose chromatographyBlot overlay assaysProteins/substratesMajor PKC substrateMajor binding proteinPhosphorylation assaysBlot overlayOverlay assaysTarget proteinsBasal phosphorylationProteinCellsSufficient affinityMARCKSAssaysPhosphorylationSubstratePhenotypeSV40Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K(+)-ATPase and effects of site-directed mutagenesis.
Fisone G, Cheng S, Nairn A, Czernik A, Hemmings H, Höög J, Bertorello A, Kaiser R, Bergman T, Jörnvall H. Identification of the phosphorylation site for cAMP-dependent protein kinase on Na+,K(+)-ATPase and effects of site-directed mutagenesis. Journal Of Biological Chemistry 1994, 269: 9368-9373. PMID: 7510709, DOI: 10.1016/s0021-9258(17)37117-x.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineAmino Acid SequenceAnimalsBase SequenceColforsinCyclic AMP-Dependent Protein KinasesDNA PrimersKineticsMolecular Sequence DataMutagenesis, Site-DirectedPeptide MappingPeptidesPhosphoserineRatsRecombinant ProteinsSodium-Potassium-Exchanging ATPaseStructure-Activity RelationshipConceptsCAMP-dependent protein kinasePhosphorylation sitesProtein kinaseSignal transduction pathwaysWild-type enzymeSite-directed mutagenesisATPase alpha subunitAlpha 1 isoformCatalytic subunitTransduction pathwaysDependent phosphorylationSeryl residuesCOS cellsAlpha subunitIntact cellsATPaseKinasePhosphorylationEnzymeSubunitsCellsExperimental approachMutagenesisCDNAIsoforms
1993
Phosphorylation of elongation factor 2 in normal and malignant rat glial cells.
Bagaglio DM, Cheng EH, Gorelick FS, Mitsui K, Nairn AC, Hait WN. Phosphorylation of elongation factor 2 in normal and malignant rat glial cells. Cancer Research 1993, 53: 2260-4. PMID: 8485712.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCalmodulinCell DivisionCells, CulturedElongation Factor 2 KinaseGliomaMaleNeurogliaPeptide Elongation Factor 2Peptide Elongation FactorsPhosphorylationPrecipitin TestsProtein KinasesRatsRats, Sprague-DawleyTrifluoperazineTumor Cells, CulturedConceptsRat brain white matterNormal glial tissueGlial tissueGlioma cellsC6 cellsC6 rat glioma cellsCaM kinase IIIRat glial cellsFactor 2Rat glioma cellsBrain white matterNormal gliaElongation factor 2Glial cellsRat brainWhite matterTumor tissueBasal levelsIII activityCellular proliferationTissueDependent proteinsCellsEndogenous substratesHomogenates
1992
cGMP-dependent protein kinase regulation of a chloride channel in T84 cells
Lin M, Nairn A, Guggino S. cGMP-dependent protein kinase regulation of a chloride channel in T84 cells. American Journal Of Physiology 1992, 262: c1304-c1312. PMID: 1317106, DOI: 10.1152/ajpcell.1992.262.5.c1304.Peer-Reviewed Original ResearchConceptsProtein kinaseChloride channelsIntestinal epithelial cellsCGMP-dependent protein kinaseProtein kinase regulationApical membraneDependent protein kinaseT84 cellsEpithelial cellsInhibitor of PKGKinase regulationCatalytic subunitCombination of ATPNonhydrolyzable formExcessive fluid secretionIntracellular faceEscherichia coliElevated guanosineSingle-channel recordingsATPKinasePKGLinear current-voltage relationshipCellsChloride secretionPhosphorylation of elongation factor 2 during Ca2+-mediated secretion from rat parotid acini
Hincke M, Nairn A. Phosphorylation of elongation factor 2 during Ca2+-mediated secretion from rat parotid acini. Biochemical Journal 1992, 282: 877-882. PMID: 1372803, PMCID: PMC1130869, DOI: 10.1042/bj2820877.Peer-Reviewed Original ResearchConceptsElongation factor 2Protein synthesisFactor 2Two-dimensional PAGECalmodulin-dependent phosphorylationRapid phosphorylationParotid acinar cellsMolecular mechanismsRat parotid cellsPhosphorylationPhorbol esterStimulation of secretionProteinParotid cellsAcinar cellsRat parotid aciniParotid aciniSpecific antiseraCellsCa2ImmunoprecipitationExtracellular Ca2SecretionStimulationInhibition
1990
Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells.
Demolle D, Lecomte M, Boutherin-Falson O, Cragoe E, Nairn A, Boeynaems J. Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells. Molecular Pharmacology 1990, 37: 827-32. PMID: 2359404.Peer-Reviewed Original ResearchConceptsElongation factor 2Protein synthesisFactor 2Rabbit reticulocyte lysateCell-free systemBovine aortic endothelial cellsDependent phosphorylationReticulocyte lysateEndothelial cellsAmiloride analoguesPhosphorylationSimilar MrCytosolic pHVascular endothelial cellsProteinAnalogues of amilorideAortic endothelial cellsPotent inhibitorInhibitory effectAntiportCellsEIPAAmilorideATPLysates
1989
Chloride conductance regulated by cyclic AMP-dependent protein kinase in cardiac myocytes
Bahinski A, Nairn A, Greengard P, Gadsby D. Chloride conductance regulated by cyclic AMP-dependent protein kinase in cardiac myocytes. Nature 1989, 340: 718-721. PMID: 2475783, DOI: 10.1038/340718a0.Peer-Reviewed Original ResearchConceptsCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseProtein kinaseChloride ion currentCatalytic subunitRegulatory proteinsKinase activationIon channelsKinaseChloride conductanceCalcium entrySingle-channel currentsCardiac myocytesCellsHeart cellsPhosphorylationAction potential repolarizationConductanceSubunitsProteinIntracellular dialysisMyocytesRegulationChannel currentsAdrenergic stimulationRegulation of Chloride Channels by Protein Kinase C in Normal and Cystic Fibrosis Airway Epithelia
Li M, McCann J, Anderson M, Clancy J, Liedtke C, Nairn A, Greengard P, Welsch M. Regulation of Chloride Channels by Protein Kinase C in Normal and Cystic Fibrosis Airway Epithelia. Science 1989, 244: 1353-1356. PMID: 2472006, DOI: 10.1126/science.2472006.Peer-Reviewed Original ResearchConceptsProtein kinase CChloride channelsKinase CApical membrane chloride channelMembrane chloride channelCystic fibrosis cellsMembrane proteinsCell-free membraneCystic fibrosis airway epitheliaChloride secretionIntact cellsPhorbol esterPhysiological statusDefective regulationAirway epithelial cellsEpithelial cellsCellsRegulationChannel inactivationCystic fibrosisActivationCalcium concentrationLow calcium concentrationsProteinAirway epithelium
1988
Cyclic AMP-dependent protein kinase opens chloride channels in normal but not cystic fibrosis airway epithelium
Li M, McCann J, Liedtket C, Nairn A, Greengard P, Welsh M. Cyclic AMP-dependent protein kinase opens chloride channels in normal but not cystic fibrosis airway epithelium. Nature 1988, 331: 358-360. PMID: 2448645, DOI: 10.1038/331358a0.Peer-Reviewed Original ResearchConceptsCAMP-dependent protein kinaseProtein kinaseRegulatory proteinsCl- channelsCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseCommon lethal genetic diseaseNormal cellsLethal genetic diseaseApical Cl- channelsCatalytic subunitCell-free patchesCystic fibrosis airway epitheliaGenetic diseasesVariety of hormonesCF airway epitheliaCF cellsChloride channelsKinaseIntracellular levelsProteinAirway epitheliumCyclic AMPChloride secretionCells
1986
Protein phosphorylation in cultured endothelial cells
Mackie K, Lai Y, Nairn A, Greengard P, Pitt B, Lazo J. Protein phosphorylation in cultured endothelial cells. Journal Of Cellular Physiology 1986, 128: 367-374. PMID: 3745280, DOI: 10.1002/jcp.1041280304.Peer-Reviewed Original ResearchConceptsCalcium/calmodulin-dependent protein kinaseCalmodulin-dependent protein kinaseCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseProtein kinase activityProtein kinaseKinase activityCyclic GMP-dependent protein kinase activityRespective substrate proteinsProtein phosphorylation systemsProtein kinase CSubstrate proteinsProtein phosphorylationPhosphorylation systemEndothelial cellsNumerous substratesTyrosine kinaseKinase CPulmonary artery endothelial cellsKinaseCultured endothelial cellsArtery endothelial cellsSimilar culture conditionsCulture conditionsCells
1983
Cyclic Nucleotide‐Dependent Protein Kinases and Some Major Substrates in the Rat Cerebellum After Neonatal X‐Irradiation
Dolphin A, Detre J, Schlichter D, Nairn A, Yeh H, Woodward D, Greengard P. Cyclic Nucleotide‐Dependent Protein Kinases and Some Major Substrates in the Rat Cerebellum After Neonatal X‐Irradiation. Journal Of Neurochemistry 1983, 40: 577-581. PMID: 6296321, DOI: 10.1111/j.1471-4159.1983.tb11321.x.Peer-Reviewed Original Research