2001
Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes
Everett A, Stoops T, Nairn A, Brautigan D. Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes. AJP Heart And Circulatory Physiology 2001, 281: h161-h167. PMID: 11406481, DOI: 10.1152/ajpheart.2001.281.1.h161.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin IIAnimalsCells, CulturedChromonesEnzyme InhibitorsMitogen-Activated Protein KinasesMorpholinesMyocardiumPeptide Elongation Factor 2Phosphoprotein PhosphatasesPhosphorylationProtein BiosynthesisProtein Phosphatase 2RatsRats, Sprague-DawleyReceptor, Angiotensin, Type 1Receptor, Angiotensin, Type 2Receptors, AngiotensinSignal TransductionSirolimusConceptsEukaryotic elongation factor 2Mitogen-activated protein kinaseElongation factor 2Protein phosphatase 2A inhibitor okadaic acidTranslation elongation factor 2Protein synthesisInhibitor okadaic acidFactor 2Rapamycin (mTOR) inhibitor rapamycinProtein translationDephosphorylated statePolypeptide elongationII-dependent increaseProtein kinaseEEF2 kinaseOkadaic acidDependent regulationInhibitor FK506MAPK activationPD 98059Cardiac myocytesDephosphorylationInhibitor rapamycinNeonatal cardiac myocytesRat neonatal cardiac myocytes
1997
Phosphorylation of Connexin43 and the Regulation of Neonatal Rat Cardiac Myocyte Gap Junctions
Sáez J, Nairn A, Czernik A, Fishman G, Spray D, Hertzberg E. Phosphorylation of Connexin43 and the Regulation of Neonatal Rat Cardiac Myocyte Gap Junctions. Journal Of Molecular And Cellular Cardiology 1997, 29: 2131-2145. PMID: 9281445, DOI: 10.1006/jmcc.1997.0447.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornCalcium-Calmodulin-Dependent Protein KinasesCDC2 Protein KinaseCells, CulturedConnexin 43DNA, ComplementaryElectrophoresis, Gel, Two-DimensionalEnzyme InhibitorsGap JunctionsMyocardiumPatch-Clamp TechniquesPhosphorylationProtein Processing, Post-TranslationalRatsRecombinant Fusion ProteinsStaurosporineTetradecanoylphorbol AcetateConceptsProtein kinase CTwo-dimensional tryptic phosphopeptide mapsTryptic phosphopeptide mapsState of phosphorylationMyocyte gap junctionsProtein kinase inhibitorsGap junctionsMajor gap junction proteinPhosphorylation of connexin43Gap junction proteinPhosphopeptide mapsTryptic phosphopeptidesPKC-dependent mechanismFunctional couplingPhosphorylated formKinase CPhosphorylationNeonatal rat cardiocytesCx43 phosphorylationStaurosporineCellular distributionImmunoblot analysisRat cardiocytesJunction proteinsCx43
1994
Role of elongation factor 2 in regulating peptide-chain elongation in the heart
Vary T, Nairn A, Lynch C. Role of elongation factor 2 in regulating peptide-chain elongation in the heart. American Journal Of Physiology 1994, 266: e628-e634. PMID: 7513958, DOI: 10.1152/ajpendo.1994.266.4.e628.Peer-Reviewed Original ResearchConceptsDiabetic ratsEF-2 contentFactor 2Protein synthesisInsulin therapyIncrease of RNADecreased translational efficiencyElongation factor 2RatsDiabetesCardiac muscleImpaired rateDecreased rateProgressive decreaseHeartInhibitionMolecular mechanismsRNA contentPeptide chain elongationH durationTherapyInsulinDecreaseCoupling of CFTR Cl− channel gating to an ATP hydrolysis cycle
Baukrowitz T, Hwang T, Nairn A, Gadsby D. Coupling of CFTR Cl− channel gating to an ATP hydrolysis cycle. Neuron 1994, 12: 473-482. PMID: 7512348, DOI: 10.1016/0896-6273(94)90206-2.Peer-Reviewed Original ResearchConceptsCystic fibrosis transmembrane conductance regulatorATP hydrolysis cycleHydrolysis cycleCFTR channelsFibrosis transmembrane conductance regulatorProtein kinase ATransmembrane conductance regulatorATP hydrolysisKinase AConductance regulatorNucleoside triphosphatesChannel openingInorganic phosphate analogueATPPhosphate analogueCardiac myocytesInorganic phosphateMean open timeRegulatorHydrolysis productsBeF3Open timeCycleTriphosphate
1993
Cardiac Chloride Channels: Incremental Regulation by Phosphorylation/Dephosphorylationa
GADSBY D, HWANG T, HORIE M, NAGEL G, NAIRN A. Cardiac Chloride Channels: Incremental Regulation by Phosphorylation/Dephosphorylationa. Annals Of The New York Academy Of Sciences 1993, 707: 259-274. PMID: 9137557, DOI: 10.1111/j.1749-6632.1993.tb38057.x.Peer-Reviewed Original Research
1992
The protein kinase A-regulated cardiac CI− channel resembles the cystic fibrosis transmembrane conductance regulator
Nagel G, Hwang T, Nastiuk K, Nairn A, Gadsbyt D. The protein kinase A-regulated cardiac CI− channel resembles the cystic fibrosis transmembrane conductance regulator. Nature 1992, 360: 81-84. PMID: 1279437, DOI: 10.1038/360081a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBiological Transport, ActiveBlotting, NorthernChloride ChannelsChlorineCystic Fibrosis Transmembrane Conductance RegulatorGuanosine TriphosphateGuinea PigsIn Vitro TechniquesIon Channel GatingMembrane PotentialsMembrane ProteinsMyocardiumPhosphorylationProtein KinasesReceptors, Adrenergic, betaRNAConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorConductance regulatorCyclic AMP-dependent protein kinaseAMP-dependent protein kinasePKA catalytic subunitResult of phosphorylationPhosphorylated channelsCatalytic subunitProtein kinaseSingle-channel conductanceNucleoside triphosphatesPhosphorylationMembrane potentialEpithelial cellsChannel activationRegulatorChannel conductanceCystic fibrosisKinaseCardiac ventricular myocytesSubunitsProteinUnitary current amplitudeRole 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
Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart.
Neumann J, Gupta R, Schmitz W, Scholz H, Nairn A, Watanabe A. Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart. Circulation Research 1991, 69: 1450-1457. PMID: 1659500, DOI: 10.1161/01.res.69.6.1450.Peer-Reviewed Original ResearchConceptsPhosphatase inhibitor-1Protein phosphatase inhibitor-1Type 1 phosphatase activityPhosphatase activityInhibitor-1Sodium dodecyl sulfate gelsDodecyl sulfate gelsIsoproterenol-induced phosphorylationSulfate gelsProteinRadioactive proteinsPhosphorylationPmol 32P/KdPhysiological bufferAntiserumActivityIndirect assayConcentrations of isoproterenolAgonist isoproterenolActivationAssaysVivoIntact heartCAMP
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 stimulation