2001
Programmed Cell Death of Developing Mammalian Neurons after Genetic Deletion of Caspases
Oppenheim R, Flavell R, Vinsant S, Prevette D, Kuan C, Rakic P. Programmed Cell Death of Developing Mammalian Neurons after Genetic Deletion of Caspases. Journal Of Neuroscience 2001, 21: 4752-4760. PMID: 11425902, PMCID: PMC6762357, DOI: 10.1523/jneurosci.21-13-04752.2001.Peer-Reviewed Original ResearchConceptsCell deathGenetic deletionExtensive cytoplasmic vacuolizationPro-apoptotic proteasesCaspase familySpecific caspasesChromatin condensationNonapoptotic pathwaysPostmitotic neuronsCaspase-9Mammalian neuronsCell typesDeath processSpecific perturbationsCaspase-3Altered morphologyCaspasesNuclear changesKey membersDeletionUTP nickCytoplasmic vacuolizationElectron microscopic levelTerminal deoxynucleotidyl transferase-mediated biotinylated UTP nickNeuronal populationsCaspases and Their Regulation in Apoptosis during Brain Development
Kuan C, Flavell R, Rakic P. Caspases and Their Regulation in Apoptosis during Brain Development. Research And Perspectives In Neurosciences 2001, 75-88. DOI: 10.1007/978-3-662-04333-2_7.Peer-Reviewed Original ResearchJun N-terminal kinasePost-mitotic neuronsMammalian brain developmentCaspase-3 activationCell deathC. elegansCaspase familyDeath gene ced-3Caspase-3Caspase-9Mammalian caspase familyGene ced-3Ectopic cell deathGene ced-9Complex regulation mechanismsNematode C. elegansCell death pathwaysNormal mouse brain developmentN-terminal kinaseBrain developmentCell death cascadeMouse brain developmentCaspase-3 deficiencyCED-3CED-9
2000
Amyloid Beta-Induced Neuronal Death is Bax-Dependent but Caspase-Independent
Selznick L, Zheng T, Flavell R, Rakic P, Roth K. Amyloid Beta-Induced Neuronal Death is Bax-Dependent but Caspase-Independent. Journal Of Neuropathology & Experimental Neurology 2000, 59: 271-279. PMID: 10759182, DOI: 10.1093/jnen/59.4.271.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid Chloromethyl KetonesAmyloid beta-PeptidesAnimalsApoptosisBcl-2-Associated X ProteinCaspase 3Caspase InhibitorsCaspasesCell DeathCells, CulturedCysteine Proteinase InhibitorsDose-Response Relationship, DrugFemaleGlycoproteinsIn Situ Nick-End LabelingMaleMiceMice, KnockoutMicrotubule-Associated ProteinsMicrotubulesNeuronsPaclitaxelProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2TelencephalonConceptsNeuronal deathNeuronal apoptosisCaspase-3 activationTelencephalic neuronsFibrillar amyloid-beta (Abeta) peptidesAbeta-induced neuronal apoptosisAD treatment strategiesAbeta-induced neuronal deathPathogenesis of ADAlzheimer's disease brainEffects of AbetaAmyloid-beta peptideApoptotic nuclear featuresUnderlying pathophysiologyTreatment strategiesDisease brainSenile plaquesNeurotoxic effectsAmyloid betaCalpain inhibitionPharmacological inhibitionBeta peptideNuclear featuresAbetaCaspase-3Caspase‐3 is required for apoptosis‐associated DNA fragmentation but not for cell death in neurons deprived of potassium
D'Mello S, Kuan C, Flavell R, Rakic P. Caspase‐3 is required for apoptosis‐associated DNA fragmentation but not for cell death in neurons deprived of potassium. Journal Of Neuroscience Research 2000, 59: 24-31. PMID: 10658182, DOI: 10.1002/(sici)1097-4547(20000101)59:1<24::aid-jnr4>3.0.co;2-8.Peer-Reviewed Original ResearchConceptsCell deathCaspase-3Apoptosis-associated DNA fragmentationDNA fragmentationCell death pathwaysRegulated cell deathPan-caspase inhibitorApoptosis-inducing stimuliDeath pathwaysChromatin condensationCaspase inhibitorsCaspase inhibitionApoptotic featuresCerebellar granule neuronsPotassium deprivationFmkCultured cerebellar granule neuronsCaspasesCrucial effectorNonneuronal cellsApoptosisSame extentGranule neuronsPivotal roleNeuronal death