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 populationsBcl-XL–Caspase-9 Interactions in the Developing Nervous System: Evidence for Multiple Death Pathways
Zaidi A, D'Sa-Eipper C, Brenner J, Kuida K, Zheng T, Flavell R, Rakic P, Roth K. Bcl-XL–Caspase-9 Interactions in the Developing Nervous System: Evidence for Multiple Death Pathways. Journal Of Neuroscience 2001, 21: 169-175. PMID: 11150333, PMCID: PMC6762421, DOI: 10.1523/jneurosci.21-01-00169.2001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisBcl-2-Associated X ProteinBcl-X ProteinCaspase 3Caspase 9CaspasesCells, CulturedCytarabineGanglia, SpinalGenes, LethalHeterozygoteHomozygoteImmunohistochemistryIn Situ Nick-End LabelingLiverMiceMice, KnockoutNervous SystemNeuronsProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2TelencephalonTumor Suppressor Protein p53ConceptsGene family membersCaspase-9 deficiencyCaspase-9Telencephalic neural precursor cellsCell deathDouble homozygous mutantsCaspase family membersMultiple death pathwaysNormal nervous system developmentBcl-2Nervous system developmentBax-deficient neuronsNeuronal apoptosisTelencephalic neuronsDeficient embryosNeural precursor cellsDeath pathwaysFamily membersHomozygous mutantsApoptotic pathwayObligate pathwayBcl-xLApoptosis inducersDeficient neuronsTargeted disruption
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
1998
Reduced Apoptosis and Cytochrome c–Mediated Caspase Activation in Mice Lacking Caspase 9
Kuida K, Haydar T, Kuan C, Gu Y, Taya C, Karasuyama H, Su M, Rakic P, Flavell R. Reduced Apoptosis and Cytochrome c–Mediated Caspase Activation in Mice Lacking Caspase 9. Cell 1998, 94: 325-337. PMID: 9708735, DOI: 10.1016/s0092-8674(00)81476-2.Peer-Reviewed Original ResearchConceptsCritical upstream activatorUpstream activatorCaspase-9Cell death machineryCytochrome cDeath machineryApoptotic stimuliCaspase activationCaspase cascadeDNA fragmentationPrevents activationCytosolic extractsEmbryonic brainCaspasesReduced apoptosisCASP9ApoptosisActivatorCASP3Brain developmentKnockout miceEssential componentCleavageActivationVivo
1996
Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
Kuida K, Zheng T, Na S, Kuan C, Yang D, Karasuyama H, Rakic P, Flavell R. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 1996, 384: 368-372. PMID: 8934524, DOI: 10.1038/384368a0.Peer-Reviewed Original ResearchConceptsCED-3Protease familyMajor morphogenetic changesProgrammed Cell DeathICE protease familyMutant embryosCaenorhabditis elegansDeath genesMorphogenetic cellApoptotic stimuliHomologous recombinationMorphogenetic changesMendelian geneticsSequence homologyHigh similarityCell deathPremature lethalitySupernumerary cellsEmbryonic day 12Mammalian brainCPP32Critical rolePostnatal stagesApoptosisBrain development