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, BiologicalN-MethylaspartateNeuronsOligomycinsPeptide 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
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 2
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