2023
Operant Training for Highly Palatable Food Alters Translating Messenger RNA in Nucleus Accumbens D2 Neurons and Reveals a Modulatory Role of Ncdn
Montalban E, Giralt A, Taing L, Nakamura Y, Pelosi A, Brown M, de Pins B, Valjent E, Martin M, Nairn A, Greengard P, Flajolet M, Hervé D, Gambardella N, Roussarie J, Girault J. Operant Training for Highly Palatable Food Alters Translating Messenger RNA in Nucleus Accumbens D2 Neurons and Reveals a Modulatory Role of Ncdn. Biological Psychiatry 2023, 95: 926-937. PMID: 37579933, PMCID: PMC11059129, DOI: 10.1016/j.biopsych.2023.08.006.Peer-Reviewed Original ResearchStriatal projection neuronsNucleus accumbensPalatable foodProjection neuronsNAc neuronsD2-striatal projection neuronsWild-type miceMessenger RNAConditioning-induced changesSpine densityDopamine neuronsDopamine receptorsDownregulated genesD2 neuronsModulatory roleNAc dopamineDopamine DFood altersCompensatory mechanismsRegular foodNeuronsFeeding behaviorBehavioral responsesMRNA alterationsMice
2016
Chapter 29 Regulation of Striatal Signaling by Protein Phosphatases
Girault J, Greengard P, Nairn A. Chapter 29 Regulation of Striatal Signaling by Protein Phosphatases. Techniques In The Behavioral And Neural Sciences 2016, 24: 583-607. DOI: 10.1016/b978-0-12-802206-1.00029-5.Peer-Reviewed Original ResearchSerine/threonine proteinProtein phosphatase regulationRegulation of proteinsPhosphatase regulationProtein phosphataseARPP-16Regulatory phosphoproteinsIntracellular signalingIntercellular communicationMedium spiny projection neuronsKey roleDARPP-32Major classesGenesRegulationSignalingProteinStriatal medium spiny projection neuronsSpecific setStriatal signalingPhosphoproteinRoleModulatory rolePhosphataseNeurons
2006
2‐Deoxyglucose and NMDA inhibit protein synthesis in neurons and regulate phosphorylation of elongation factor‐2 by distinct mechanisms
Maus M, Torrens Y, Gauchy C, Bretin S, Nairn A, Glowinski J, Premont J. 2‐Deoxyglucose and NMDA inhibit protein synthesis in neurons and regulate phosphorylation of elongation factor‐2 by distinct mechanisms. Journal Of Neurochemistry 2006, 96: 815-824. PMID: 16405506, DOI: 10.1111/j.1471-4159.2005.03601.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntimetabolitesBlotting, WesternCalciumCarbonyl Cyanide m-Chlorophenyl HydrazoneCells, CulturedCerebral CortexDeoxyglucoseDose-Response Relationship, DrugDrug InteractionsEmbryo, MammalianEnzyme InhibitorsExcitatory Amino Acid AgonistsIonophoresLeucineMiceModels, BiologicalNeuronsN-MethylaspartateOligomycinsPeptide Elongation Factor 2PhosphorylationProtein KinasesProtein Synthesis InhibitorsPyruvic AcidSodium AzideTime FactorsTOR Serine-Threonine KinasesTritiumConceptsCortical neuronsExcitatory amino acid releaseImine hydrogen maleateNMDA receptor antagonistAMP kinaseAmino acid releaseNeuronal protein synthesisCytosolic free Ca2Protein synthesisCerebral ischaemiaReceptor antagonistBrain damageNeuronal metabolismMetabolic impairmentNMDADistinct mechanismsCytosolic Ca2NeuronsMetabolic deprivationAcid releaseSecondary releaseProtein synthesis inhibitionSynthesis inhibitionElongation factor eEF-2ATP levels
2002
N-Methyl-D-aspartate receptor activation inhibits protein synthesis in cortical neurons independently of its ionic permeability properties
Gauchy C, Nairn A, Glowinski J, Prémont J. N-Methyl-D-aspartate receptor activation inhibits protein synthesis in cortical neurons independently of its ionic permeability properties. Neuroscience 2002, 114: 859-867. PMID: 12379242, DOI: 10.1016/s0306-4522(02)00322-6.Peer-Reviewed Original ResearchConceptsCortical neuronsAbsence of externalNMDA treatmentTransient cerebral ischemiaAspartate receptor activationGlutamate-induced increaseThapsigargin-sensitive poolMobilization of intracellularProtein synthesisCerebral ischemiaNMDA receptorsNMDAReceptor activationTransient risePresence of externalNeuronsCGP-37157D-serineFree mediumIntracellularIonic permeability propertiesTreatmentSustained releaseIschemiaBlockade
2001
Inhibition of protein synthesis in cortical neurons during exposure to hydrogen peroxide
Alirezaei M, Marin P, Nairn A, Glowinski J, Prémont J. Inhibition of protein synthesis in cortical neurons during exposure to hydrogen peroxide. Journal Of Neurochemistry 2001, 76: 1080-1088. PMID: 11181828, DOI: 10.1046/j.1471-4159.2001.00105.x.Peer-Reviewed Original ResearchMeSH KeywordsAniline CompoundsAnimalsCalciumCells, CulturedCerebral CortexDose-Response Relationship, DrugEukaryotic Initiation Factor-2Fluorescent DyesHydrogen PeroxideIntracellular FluidMiceNeuronsPeptide Chain Elongation, TranslationalPeptide Elongation Factor 2PhosphorylationProtein BiosynthesisProtein Synthesis InhibitorsProteinsThapsigarginXanthenesConceptsCortical neuronsGlutamate-induced increaseTransient cerebral ischemiaDose-dependent mannerEffects of thapsigarginProtein synthesisCerebral ischemiaReperfusion periodCommon intracellularEEF-2BlockadeTreatmentNeuronsInhibitionThapsigarginIntracellularPhosphorylationSustained releaseIschemiaEIF-2alphaSlow increaseProtein translation
2000
Severe deficiencies in dopamine signaling in presymptomatic Huntington's disease mice
Bibb J, Yan Z, Svenningsson P, Snyder G, Pieribone V, Horiuchi A, Nairn A, Messer A, Greengard P. Severe deficiencies in dopamine signaling in presymptomatic Huntington's disease mice. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 6809-6814. PMID: 10829080, PMCID: PMC18747, DOI: 10.1073/pnas.120166397.Peer-Reviewed Original ResearchConceptsMedium spiny neuronsDisease miceSpiny neuronsStriatal medium spiny neuronsHuntington's diseaseSevere deficiencyHuntington's disease miceHD model miceModel miceDopaminergic neurotransmissionHD miceSelective neurodegenerationHD pathologyMiceDARPP-32DopamineHuman huntingtinBehavioral phenotypesDiseaseNeuronsIon channelsTotal levelsDisease-causing formHuntingtinDeficiency
1999
Zinc Inhibits Protein Synthesis in Neurons POTENTIAL ROLE OF PHOSPHORYLATION OF TRANSLATION INITIATION FACTOR-2α*
Alirezaei M, Nairn A, Glowinski J, Prémont J, Marin P. Zinc Inhibits Protein Synthesis in Neurons POTENTIAL ROLE OF PHOSPHORYLATION OF TRANSLATION INITIATION FACTOR-2α*. Journal Of Biological Chemistry 1999, 274: 32433-32438. PMID: 10542287, DOI: 10.1074/jbc.274.45.32433.Peer-Reviewed Original ResearchConceptsCultured cortical neuronsEukaryotic elongation factor 2Central nervous systemFactor 2Translation initiation factor 2αProtein synthesisCerebral cortexCortical neuronsNervous systemProfound inhibitionSustained increaseBasal levelsTransient increaseBasal ratePotential roleProgressive decreaseInhibits protein synthesisNeuronsAmount of polyribosomesElongation factor 2EIF-2alpha phosphorylationAlpha subunitInhibitionPhosphorylationEukaryotic initiation factor 2Role 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
Glutamate-Dependent Phosphorylation of Elongation Factor-2 and Inhibition of Protein Synthesis in Neurons
Marin P, Nastiuk K, Daniel N, Girault J, Czernik A, Glowinski J, Nairn A, Prémont J. Glutamate-Dependent Phosphorylation of Elongation Factor-2 and Inhibition of Protein Synthesis in Neurons. Journal Of Neuroscience 1997, 17: 3445-3454. PMID: 9133370, PMCID: PMC6573691, DOI: 10.1523/jneurosci.17-10-03445.1997.Peer-Reviewed Original ResearchMeSH Keywords6-Cyano-7-nitroquinoxaline-2,3-dioneAnimalsAntibody SpecificityCalciumCell SurvivalCells, CulturedCerebral CortexDizocilpine MaleateExcitatory Amino Acid AntagonistsGlutamic AcidMiceNerve Tissue ProteinsNeuronsNeurotoxinsPeptide Elongation Factor 2Peptide Elongation FactorsPhosphorylationProtein BiosynthesisProtein Synthesis InhibitorsReceptors, AMPAReceptors, N-Methyl-D-AspartateConceptsNeuronal deathEukaryotic elongation factor 2Factor 2Cortical neuronsElongation factor 2Glutamate receptorsProtective effectLong-term effectsProtein synthesisPersistent inhibitionPharmacological analysisPharmacological inhibitionCytosolic Ca2Phosphorylation state-specific antibodiesNeuronsNMDAGlutamateInhibitionProtein translationDeathPhosphorylationClose correlationTransient phosphorylationCa2Excitotoxicity
1991
Immunocytochemical localization of phosphatase inhibitor‐1 in rat brain
Gustafson E, Girault J, Hemmings H, Nairn A, Greengard P. Immunocytochemical localization of phosphatase inhibitor‐1 in rat brain. The Journal Of Comparative Neurology 1991, 310: 170-188. PMID: 1955581, DOI: 10.1002/cne.903100204.Peer-Reviewed Original ResearchConceptsPhosphatase inhibitor-1Inhibitor-1Intracellular signal transductionPhosphatase 1Protein phosphorylationSignal transductionWidespread roleNumerous immunoreactive cell bodiesSuprachiasmatic nucleusCyclic AMPImmunocytochemical localizationUse of immunocytochemistrySubstantial populationNeurotransmitter regulationDephosphorylationLocalizationNucleusTransductionImmunocytochemical studyCell bodiesPhosphorylationProteinNeuronsRegulationHigh levels
1988
DARPP‐32 and Phosphatase Inhibitor‐1, Two Structurally Related Inhibitors of Protein Phosphatase‐1, Are Both Present in Striatonigral Neurons
Nairn A, Hemmings H, Walaas S, Greengard P. DARPP‐32 and Phosphatase Inhibitor‐1, Two Structurally Related Inhibitors of Protein Phosphatase‐1, Are Both Present in Striatonigral Neurons. Journal Of Neurochemistry 1988, 50: 257-262. PMID: 3335843, DOI: 10.1111/j.1471-4159.1988.tb13258.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBasal GangliaCarrier ProteinsCorpus StriatumDopamine and cAMP-Regulated Phosphoprotein 32Electrophoresis, Polyacrylamide GelIntracellular Signaling Peptides and ProteinsKainic AcidMaleMusclesNerve Tissue ProteinsNeuronsPhosphoproteinsPhosphorylationProteinsRatsRats, Inbred StrainsSubstantia NigraConceptsPhosphatase inhibitor-1Protein phosphatase 1Phosphatase 1DARPP-32Inhibitor-1Striatonigral neuronsSubstantia nigraKainic acidStriatonigral fibersBiochemical propertiesRelated inhibitorsSpecific neuronal subpopulationsIpsilateral substantia nigraBovine caudate nucleusSpecific activityStriatal neuronsNeuronal localizationRat neostriatumNeuronal subpopulationsRat brainCaudate nucleusLesioned neostriatumNeostriatumNeuronsInhibitors
1987
Cholecystokinin induces a decrease in Ca2+ current in snail neurons that appears to be mediated by protein kinase C
Hammond C, Paupardin-Tritsch D, Nairn A, Greengard P, Gerschenfeld H. Cholecystokinin induces a decrease in Ca2+ current in snail neurons that appears to be mediated by protein kinase C. Nature 1987, 325: 809-811. PMID: 2434859, DOI: 10.1038/325809a0.Peer-Reviewed Original ResearchConceptsProtein kinase CAction of noradrenalineDependent action potentialsKinase CIntracellular injectionSnail neuronsAction potentialsProtein kinaseCardiac muscleCholecystokininSnail Helix aspersaExcitable tissuesProtein kinase C.Low concentrationsCa2Cyclic GMP-dependent protein kinaseHelix aspersaInjectionGMP-dependent protein kinaseKinase C.KinaseNoradrenalineCCK8Neurons
1986
Intracellular injection of cGMP-dependent protein kinase results in increased input resistance in neurons of the mammalian motor cortex
Woody C, Bartfai T, Gruen E, Nairn A. Intracellular injection of cGMP-dependent protein kinase results in increased input resistance in neurons of the mammalian motor cortex. Brain Research 1986, 386: 379-385. PMID: 3779415, DOI: 10.1016/0006-8993(86)90175-7.Peer-Reviewed Original ResearchConceptsMammalian motor cortexMotor cortexInput resistanceSame cortical areaCyclic GMP-dependent protein kinasePrecruciate cortexIntracellular injectionAwake catsCortical areasMicroM cGMPNeuronsCortexInjectionCGMPGMP-dependent protein kinaseProtein kinase resultsAcetylcholineProtein kinasePresent results