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
Opposing Changes in Phosphorylation of Specific Sites in Synapsin I During Ca2+-Dependent Glutamate Release in Isolated Nerve Terminals
Jovanovic J, Sihra T, Nairn A, Hemmings H, Greengard P, Czernik A. Opposing Changes in Phosphorylation of Specific Sites in Synapsin I During Ca2+-Dependent Glutamate Release in Isolated Nerve Terminals. Journal Of Neuroscience 2001, 21: 7944-7953. PMID: 11588168, PMCID: PMC6763853, DOI: 10.1523/jneurosci.21-20-07944.2001.Peer-Reviewed Original ResearchConceptsDependent dephosphorylationProtein phosphatase 2AMultiple protein kinasesPhosphorylation site 1Protein phosphatase 2BSynapsin IPhosphatase 2APhosphorylation sitesPhosphatase 2BSynapsin functionProtein kinaseDependent phosphorylationSynapsin I phosphorylationDephosphorylation processNeuronal phosphoproteinSynapsin I.Synaptic vesiclesCalcineurin activityPhosphorylationI phosphorylationDephosphorylationNeurotransmitter releaseSpecific sitesExcellent substrateSite 1Phosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5*
Bibb J, Nishi A, O'Callaghan J, Ule J, Lan M, Snyder G, Horiuchi A, Saito T, Hisanaga S, Czernik A, Nairn A, Greengard P. Phosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5*. Journal Of Biological Chemistry 2001, 276: 14490-14497. PMID: 11278334, DOI: 10.1074/jbc.m007197200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBrainCalcineurinCarrier ProteinsCDC2 Protein KinaseCyclic AMPCyclic AMP-Dependent Protein KinasesCyclin-Dependent Kinase 5Cyclin-Dependent KinasesGlutamic AcidIntracellular Signaling Peptides and ProteinsKineticsMiceMice, Inbred C57BLMutagenesis, Site-DirectedN-MethylaspartatePhosphoprotein PhosphatasesPhosphorylationProlineProtein Phosphatase 1RabbitsRatsRecombinant ProteinsRNA-Binding ProteinsSerineTime FactorsConceptsProtein phosphatase inhibitor-1Protein phosphatase 1Phosphatase inhibitor-1Ser-67Protein kinasePhosphatase 1CAMP-dependent protein kinase resultsSelective protein kinase inhibitorsCAMP-dependent protein kinaseProtein phosphatase 2AProline-directed kinasesMitogen-activated protein kinaseInhibitor-1Protein kinase resultsSignal transduction eventsPhosphorylation state-specific antibodiesCAMP-dependent protein kinase activationState of phosphorylationProtein kinase inhibitorsProtein kinase activationPhosphatase 2AThr-35Protein phosphatasePhosphorylation sitesGlutamate-dependent regulation
2000
NMDA receptor-mediated control of protein synthesis at developing synapses
Scheetz A, Nairn A, Constantine-Paton M. NMDA receptor-mediated control of protein synthesis at developing synapses. Nature Neuroscience 2000, 3: 211-216. PMID: 10700251, DOI: 10.1038/72915.Peer-Reviewed Original ResearchMeSH Keywords2-Amino-5-phosphonovalerateAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCycloheximideElectrophoresis, Gel, Two-DimensionalGlutamic AcidIsoelectric PointMolecular WeightN-MethylaspartatePeptide Elongation Factor 2PhosphorylationPrecipitin TestsProtein BiosynthesisProteinsRatsReceptors, N-Methyl-D-AspartateRetinal Ganglion CellsSuperior ColliculiSynapsesSynaptosomesTime FactorsConceptsNMDAR activationReceptor activationN-methyl-D-aspartate (NMDA) receptor activationActivity-dependent synaptic changesEukaryotic elongation factor 2Receptor-mediated controlSynaptic protein synthesisEEF2 phosphorylationProtein synthesisSuperior colliculiYoung ratsDependent kinase IISynaptic changesLow dosesTotal protein synthesisII synthesisFactor 2Overall protein synthesisActivationElongation factor 2Kinase IIPhosphorylation
1998
Ca2+/calmodulin-dependent kinase II mediates simultaneous enhancement of gap-junctional conductance and glutamatergic transmission
Pereda A, Bell T, Chang B, Czernik A, Nairn A, Soderling T, Faber D. Ca2+/calmodulin-dependent kinase II mediates simultaneous enhancement of gap-junctional conductance and glutamatergic transmission. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 13272-13277. PMID: 9789078, PMCID: PMC23780, DOI: 10.1073/pnas.95.22.13272.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzylaminesCalciumCalcium ChlorideCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCell CommunicationDendritesEgtazic AcidElectric ConductivityElectric StimulationEnzyme ActivationEnzyme InhibitorsEvoked PotentialsExcitatory Postsynaptic PotentialsGap JunctionsGlutamic AcidGoldfishMembrane PotentialsNeuronsSpinal CordSulfonamidesSynapsesSynaptic TransmissionVestibulocochlear NerveConceptsGlutamatergic synapsesGap junctional conductanceCaM-KIIGap junctionsLong-term potentiationGoldfish Mauthner cellIntradendritic Ca2Intradendritic injectionPostsynaptic increaseExcitatory transmissionGlutamatergic transmissionAuditory afferentsSynaptic responsesSynaptic activityDependent kinase inhibitorDependent kinase IIIntracellular Ca2Interneuronal communicationSpecific peptide inhibitorChemical synapsesKinase inhibitorsMauthner cellKN-93Mammalian glutamatergic synapsesSynapses
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
1995
A Role for Calcineurin (Protein Phosphatase-2B) in the Regulation of Glutamate Release
Sihra T, Nairn A, Kloppenburg P, Lin Z, Pouzat C. A Role for Calcineurin (Protein Phosphatase-2B) in the Regulation of Glutamate Release. Biochemical And Biophysical Research Communications 1995, 212: 609-616. PMID: 7542882, DOI: 10.1006/bbrc.1995.2013.Peer-Reviewed Original ResearchConceptsRelease of glutamateGlutamate releaseVoltage-dependent Ca channel activityVoltage-dependent Ca influxRat cerebral cortexCa-dependent componentCa channel activityCerebral cortexNerve terminalsCa influxInflux of CaCa entryActivation of calcineurinCa channelsCalcineurin activityGlutamateFK506CalcineurinRelease