1999
Arginine vasopressin stimulates phosphorylation of aquaporin-2 in rat renal tissue
Nishimoto G, Zelenina M, Li D, Yasui M, Aperia A, Nielsen S, Nairn A. Arginine vasopressin stimulates phosphorylation of aquaporin-2 in rat renal tissue. American Journal Of Physiology 1999, 276: f254-f259. PMID: 9950956, DOI: 10.1152/ajprenal.1999.276.2.f254.Peer-Reviewed Original ResearchConceptsPhosphorylation of AQP2Protein kinase AAquaporin-2Two-dimensional phosphopeptide mappingCAMP-dependent protein kinase AConsensus phosphorylation sitesActivation of PKAPhosphopeptide mappingPhosphorylation sitesMaximal phosphorylationAQP2 phosphorylationKinase APhosphorylationSer256Immunoblot analysis
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 PDBuCellsInhibition
1995
Modulation of calcium currents by a D1 dopaminergic protein kinase/phosphatase cascade in rat neostriatal neurons
Surmeier D, Bargas J, Hemmings H, Nairn A, Greengard P. Modulation of calcium currents by a D1 dopaminergic protein kinase/phosphatase cascade in rat neostriatal neurons. Neuron 1995, 14: 385-397. PMID: 7531987, DOI: 10.1016/0896-6273(95)90294-5.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthine2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl esterAnimalsBrainCalcium Channel BlockersCalcium ChannelsCells, CulturedColforsinCyclic AMPCyclic AMP-Dependent Protein KinasesElectrophysiologyKineticsMembrane PotentialsNeostriatumNeuronsNifedipinePhosphoprotein PhosphatasesProtein Phosphatase 1RatsRats, WistarReceptors, Dopamine D1TetraethylammoniumTetraethylammonium CompoundsTime FactorsConceptsProtein phosphatase 1Protein kinaseInhibition of PP1Cyclic AMP-dependent protein kinaseAMP-dependent protein kinaseInhibition of PKARat neostriatal neuronsPhosphatase cascadePP1 activityReceptor-mediated activationPhosphatase 1Neostriatal neuronsCalcium currentPKA enhancementDifferential regulationHigh voltage-activated calcium currentsVoltage-activated calcium currentsWhole-cell voltage-clamp techniqueD1 pathwayMedium spiny neuronsCyclic AMP analogueD1 dopamine receptorsL-type currentDiversity of effectsSubset of neurons
1994
Identification 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
1992
Role of GTP-binding proteins in the regulation of mammalian cardiac chloride conductance.
Hwang T, Horie M, Nairn A, Gadsby D. Role of GTP-binding proteins in the regulation of mammalian cardiac chloride conductance. The Journal Of General Physiology 1992, 99: 465-489. PMID: 1375958, PMCID: PMC2219206, DOI: 10.1085/jgp.99.4.465.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAdenylate Cyclase ToxinAdrenergic beta-AgonistsAnimalsCarbacholCells, CulturedChloride ChannelsChloridesColforsinCyclic AMPGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guinea PigsHeartHistamineIon ChannelsIsoproterenolMembrane ProteinsMyocardiumPertussis ToxinPhosphorylationPropranololReceptors, Adrenergic, betaReceptors, MuscarinicTime FactorsVirulence Factors, BordetellaConceptsProtein kinaseNonhydrolyzable GTP analogG proteinsCAMP-dependent protein kinaseG protein turnoverGTP-binding proteinsCl- conductanceAdenylyl cyclase activityCl- current activationGTP analogueMammalian cardiac myocytesGDP beta SSynthetic peptide inhibitorProtein turnoverStimulatory G proteinMammalian modelsPertussis toxinBeta SInhibitory G proteinBasal activationGTPPeptide inhibitorAdenylyl cyclaseCyclase activityProtein
1991
Enhancement of the Glutamate Response by cAMP-Dependent Protein Kinase in Hippocampal Neurons
Greengard P, Jen J, Nairn A, Stevens C. Enhancement of the Glutamate Response by cAMP-Dependent Protein Kinase in Hippocampal Neurons. Science 1991, 253: 1135-1138. PMID: 1716001, DOI: 10.1126/science.1716001.Peer-Reviewed Original ResearchConceptsProtein kinaseCAMP-dependent protein kinaseGlutamate receptor channelsMonophosphate-dependent protein kinaseReceptor channelsType glutamate receptor channelsAdenylate cyclase cascadeCultured hippocampal pyramidal neuronsSpontaneous excitatory postsynaptic currentsWhole-cell current responsesSingle-channel analysisNeuromodulatory regulationMammalian brainExcitatory postsynaptic currentsHippocampal pyramidal neuronsKinaseLong-term potentiationPyramidal neuronsPostsynaptic currentsGlutamate responseExcitatory neurotransmitterMean open timeHippocampal neuronsAdenylate cyclaseSynaptic events
1989
Protein kinase inhibitors selectively block phorbol ester- or forskolin- induced changes in excitability of Aplysia neurons
Conn P, Strong J, Azhderian E, Nairn A, Greengard P, Kaczmarek L. Protein kinase inhibitors selectively block phorbol ester- or forskolin- induced changes in excitability of Aplysia neurons. Journal Of Neuroscience 1989, 9: 473-479. PMID: 2537389, PMCID: PMC6569795, DOI: 10.1523/jneurosci.09-02-00473.1989.Peer-Reviewed Original ResearchConceptsProtein kinase CBag cell neuronsVoltage-dependent calcium currentsCAMP-PKPhorbol esterKinase CCell neuronsAction potentialsCalcium currentInhibitor of PKCProtein kinase inhibitorsPhorbol ester-induced enhancementKinase inhibitor 1Protein kinase inhibitor 1Adenylate cyclase activator forskolinCyclase activator forskolinProtein inhibitorGranule movementVoltage-dependent currentsCell action potentialsCAMP analogEffect of forskolinActivator forskolinPhorbol ester-induced changesNeuronal excitability
1987
Nerve growth factor treatment or cAMP elevation reduces Ca2+/calmodulin-dependent protein kinase III activity in PC12 cells.
Nairn A, Nichols R, Brady M, Palfrey H. Nerve growth factor treatment or cAMP elevation reduces Ca2+/calmodulin-dependent protein kinase III activity in PC12 cells. Journal Of Biological Chemistry 1987, 262: 14265-14272. PMID: 2443502, DOI: 10.1016/s0021-9258(18)47933-1.Peer-Reviewed Original ResearchConceptsNerve growth factorEffect of forskolinIII activityPC12 cellsGrowth factorLong-term treatmentShort-term treatmentEffect of treatmentNerve growth factor treatmentGrowth factor treatmentAbility of forskolinAbility of NGFPhorbol esterEpidermal growth factorMaximal effectCytosolic extractsFactor treatmentForskolinCAMP elevationTreatmentCell linesProtein kinase CRemoval of forskolinImmunological techniquesDependent protein phosphorylation