2024
Enzymatic and non-enzymatic transnitrosylation: “SCAN”ning the SNO-proteome
Nakamura T, Lipton S. Enzymatic and non-enzymatic transnitrosylation: “SCAN”ning the SNO-proteome. Molecular Cell 2024, 84: 191-193. PMID: 38242098, DOI: 10.1016/j.molcel.2023.12.018.Peer-Reviewed Original Research
2022
Unfolded protein response IRE1/XBP1 signaling is required for healthy mammalian brain aging
Cabral‐Miranda F, Tamburini G, Martinez G, Ardiles A, Medinas D, Gerakis Y, Hung M, Vidal R, Fuentealba M, Miedema T, Duran‐Aniotz C, Diaz J, Ibaceta‐Gonzalez C, Sabusap C, Bermedo‐Garcia F, Mujica P, Adamson S, Vitangcol K, Huerta H, Zhang X, Nakamura T, Sardi S, Lipton S, Kennedy B, Henriquez J, Cárdenas J, Plate L, Palacios A, Hetz C. Unfolded protein response IRE1/XBP1 signaling is required for healthy mammalian brain aging. The EMBO Journal 2022, 41: embj2022111952. PMID: 36314651, PMCID: PMC9670206, DOI: 10.15252/embj.2022111952.Peer-Reviewed Original ResearchConceptsUnfolded protein responseER stress sensor IRE1Stress sensor IRE1IRE1/XBP1 signalingTranscription factor XBP1Mammalian brain agingNeurodegenerative diseasesProteostasis networkEndoplasmic reticulum stressProteomic profilingProtein responseCell senescenceGenetic disruptionBrain agingXBP1 expressionReticulum stressMammalian brainMajor risk factorActive formHealthy brain agingSynaptic functionXBP1Age-related cognitive declinePathwayHippocampal tissue
2021
Protein Transnitrosylation Signaling Networks Contribute to Inflammaging and Neurodegenerative Disorders
Nakamura T, Oh C, Zhang X, Tannenbaum S, Lipton S. Protein Transnitrosylation Signaling Networks Contribute to Inflammaging and Neurodegenerative Disorders. Antioxidants & Redox Signaling 2021, 35: 531-550. PMID: 33957758, PMCID: PMC8388249, DOI: 10.1089/ars.2021.0081.Peer-Reviewed Original ResearchMeSH KeywordsHumansNeurodegenerative DiseasesNitric OxideOxidation-ReductionProtein Processing, Post-TranslationalReactive Nitrogen SpeciesSignal TransductionConceptsRelated reactive nitrogen speciesS-nitrosylationRedox-based posttranslational modificationProtein S-nitrosylationGlyceraldehyde-3-phosphate dehydrogenaseInhibitor of apoptosisThiol-containing proteinsNeurodegenerative diseasesSignaling networksPosttranslational modificationsReactive nitrogen speciesTransnitrosylation reactionsNuclear proteinsUnderstanding of agingCysteine thiolsTransnitrosylationBiochemical pathwaysChemical biologyMechanisms of diseaseProteinCaspase-3Nitrogen speciesUCH-L1Neurodegenerative disordersPhysiological concentrations
2014
Essential versus accessory aspects of cell death: recommendations of the NCCD 2015
Galluzzi L, Bravo-San Pedro JM, Vitale I, Aaronson SA, Abrams JM, Adam D, Alnemri ES, Altucci L, Andrews D, Annicchiarico-Petruzzelli M, Baehrecke EH, Bazan NG, Bertrand MJ, Bianchi K, Blagosklonny MV, Blomgren K, Borner C, Bredesen DE, Brenner C, Campanella M, Candi E, Cecconi F, Chan FK, Chandel NS, Cheng EH, Chipuk JE, Cidlowski JA, Ciechanover A, Dawson TM, Dawson VL, De Laurenzi V, De Maria R, Debatin KM, Di Daniele N, Dixit VM, Dynlacht BD, El-Deiry WS, Fimia GM, Flavell RA, Fulda S, Garrido C, Gougeon ML, Green DR, Gronemeyer H, Hajnoczky G, Hardwick JM, Hengartner MO, Ichijo H, Joseph B, Jost PJ, Kaufmann T, Kepp O, Klionsky DJ, Knight RA, Kumar S, Lemasters JJ, Levine B, Linkermann A, Lipton SA, Lockshin RA, López-Otín C, Lugli E, Madeo F, Malorni W, Marine JC, Martin SJ, Martinou JC, Medema JP, Meier P, Melino S, Mizushima N, Moll U, Muñoz-Pinedo C, Nuñez G, Oberst A, Panaretakis T, Penninger JM, Peter ME, Piacentini M, Pinton P, Prehn JH, Puthalakath H, Rabinovich GA, Ravichandran KS, Rizzuto R, Rodrigues CM, Rubinsztein DC, Rudel T, Shi Y, Simon HU, Stockwell BR, Szabadkai G, Tait SW, Tang HL, Tavernarakis N, Tsujimoto Y, Vanden Berghe T, Vandenabeele P, Villunger A, Wagner EF, Walczak H, White E, Wood WG, Yuan J, Zakeri Z, Zhivotovsky B, Melino G, Kroemer G. Essential versus accessory aspects of cell death: recommendations of the NCCD 2015. Cell Death & Differentiation 2014, 22: 58-73. PMID: 25236395, PMCID: PMC4262782, DOI: 10.1038/cdd.2014.137.Peer-Reviewed Original ResearchConceptsRegulated cell deathAccidental cell deathCell deathCellular demiseCourse of apoptosisAdaptive responseExecutioner caspasesMammalian systemsLethal signalPhysiologic programGenetic interventionsNomenclature CommitteeBiochemical phenomenaCytoprotective effectsMechanical stimuliCaspasesTransductionBiochemical correlatesApoptosisCytoprotectionDeathCellsActivationResponseVariants
2006
Activation of the Keap1/Nrf2 pathway for neuroprotection by electrophillic phase II inducers
Satoh T, Okamoto S, Cui J, Watanabe Y, Furuta K, Suzuki M, Tohyama K, Lipton S. Activation of the Keap1/Nrf2 pathway for neuroprotection by electrophillic phase II inducers. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 768-773. PMID: 16407140, PMCID: PMC1334635, DOI: 10.1073/pnas.0505723102.Peer-Reviewed Original ResearchConceptsNeurite outgrowth-promoting prostaglandinsHemeoxygenase-1Cerebral ischemia/reperfusion injuryKeap1/Nrf2/HOIschemia/reperfusion injuryGlutamate-related excitotoxicityKeap1/Nrf2 pathwayNrf2/HOHO-1 expressionCultured neuronal cellsInactivation of Nrf2Phase II enzymesThiol-dependent mannerTranscription factor Nrf2HO-1 promoterNeuroprotective actionReperfusion injuryNeuroprotective compoundsNrf2 pathwayTherapeutic approachesNrf2 translocationAntioxidant responsive elementNeurodegenerative disordersNeuronal cellsFactor Nrf2
2005
HIV-1 infection and AIDS: consequences for the central nervous system
Kaul M, Zheng J, Okamoto S, Gendelman H, Lipton S. HIV-1 infection and AIDS: consequences for the central nervous system. Cell Death & Differentiation 2005, 12: 878-892. PMID: 15832177, DOI: 10.1038/sj.cdd.4401623.Peer-Reviewed Original ResearchMeSH KeywordsAcquired Immunodeficiency SyndromeAIDS Dementia ComplexAnimalsAntiretroviral Therapy, Highly ActiveApoptosisApoptosis Regulatory ProteinsBrainChemokinesForecastingHIV Envelope Protein gp120HIV-1HumansMembrane GlycoproteinsMicrogliaNerve DegenerationNeuronsReceptors, ChemokineSignal TransductionStem CellsTNF-Related Apoptosis-Inducing LigandTumor Necrosis Factor-alphaConceptsHuman immunodeficiency virus-1Glutamate receptor-mediated excitotoxicityReceptor-mediated excitotoxicityHIV-1 infectionImmune competent cellsExtracellular matrix-degrading enzymesImmunodeficiency virus-1Central nervous systemFuture therapeutic interventionsMatrix-degrading enzymesFrank dementiaInflammatory mediatorsNeuronal damageMotor dysfunctionChemokine receptorsGlial functionDegenerative mechanismsNeurological problemsParticular macrophagesBehavioral abnormalitiesNervous systemTherapeutic interventionsNeuropathological responsesVirus 1Infection
2004
Signaling pathways to neuronal damage and apoptosis in human immunodeficiency virus type 1-associated dementia: Chemokine receptors, excitotoxicity, and beyond
Kaul M, Lipton S. Signaling pathways to neuronal damage and apoptosis in human immunodeficiency virus type 1-associated dementia: Chemokine receptors, excitotoxicity, and beyond. Journal Of NeuroVirology 2004, 10: 97-101. PMID: 14982746, DOI: 10.1080/753312759.Peer-Reviewed Original ResearchMeSH KeywordsAIDS Dementia ComplexApoptosisHIV-1HumansNeuronsNeurotoxinsReceptors, ChemokineSignal TransductionConceptsNeuronal damageChemokine receptorsN-methyl-D-aspartate (NMDA) receptor-mediated excitotoxicityHuman immunodeficiency virus-1 (HIV-1) infectionHuman immunodeficiency virus type 1Immunodeficiency virus type 1Applicable therapeutic interventionReceptor-mediated excitotoxicityVirus-1 infectionVirus type 1HIV infectionInflammatory factorsHIV-1Therapeutic interventionsType 1Downstream mechanismsExcitotoxicityDementiaInfectionReceptorsNeuropathologyPathwayDamage
2003
Nitric oxide signaling regulates mitochondrial number and function
Bossy-Wetzel E, Lipton S. Nitric oxide signaling regulates mitochondrial number and function. Cell Death & Differentiation 2003, 10: 757-760. PMID: 12815458, DOI: 10.1038/sj.cdd.4401244.Peer-Reviewed Original Research
2001
Erythropoietin-mediated neuroprotection involves cross-talk between Jak2 and NF-κB signalling cascades
Digicaylioglu M, Lipton S. Erythropoietin-mediated neuroprotection involves cross-talk between Jak2 and NF-κB signalling cascades. Nature 2001, 412: 641-647. PMID: 11493922, DOI: 10.1038/35088074.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCell NucleusCells, CulturedDNAErythropoietinGenes, ReporterJanus Kinase 2NeuronsNeuroprotective AgentsNF-kappa BNitric OxideN-MethylaspartateProtein BindingProtein TransportProtein-Tyrosine KinasesProto-Oncogene ProteinsRatsReceptors, ErythropoietinSignal TransductionSuperoxide DismutaseTumor Necrosis Factor-alphaConceptsHypoxia-inducible factor-1EPO receptorForm of JAK2Transcription factor hypoxia-inducible factor-1NF-κB-dependent transcriptionNF-κB functionActivation of JAK2Subsequent nuclear translocationTranscription factor NF-κBNF-κBFactor NF-κBSignaling cascadesNitric oxideKinase 2NF-κB signaling cascadesHypoxic-ischemic preconditioningNuclear translocationNeuroprotective genesFactor 1JAK2Neuroprotective pathwaysNeuronal apoptosisCerebrocortical neuronsEPO effectsDegenerative damage
2000
Role of p38 Mitogen-Activated Protein Kinase in Axotomy-Induced Apoptosis of Rat Retinal Ganglion Cells
Kikuchi M, Tenneti L, Lipton S. Role of p38 Mitogen-Activated Protein Kinase in Axotomy-Induced Apoptosis of Rat Retinal Ganglion Cells. Journal Of Neuroscience 2000, 20: 5037-5044. PMID: 10864961, PMCID: PMC6772303, DOI: 10.1523/jneurosci.20-13-05037.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisAxonal TransportAxotomyCell NucleusCell SurvivalDizocilpine MaleateEnzyme InhibitorsFluorescent DyesImidazolesKineticsMaleMitogen-Activated Protein KinasesNeuroprotective AgentsOptic NerveP38 Mitogen-Activated Protein KinasesPhosphorylationPyridinesRatsRats, Long-EvansRetinal Ganglion CellsSignal TransductionStilbamidinesTime FactorsConceptsRetinal ganglion cellsProtein kinaseP38 Mitogen-Activated Protein KinaseMitogen-Activated Protein KinaseMAP kinase activationIntracellular signal transductionRole of p38P38 MAP kinase activationApoptotic cell deathDose-dependent mannerP38 MAP kinase inhibitorMAP kinase inhibitorRGC apoptosisOptic nerveGanglion cellsSignal transductionNMDA receptorsAxotomy-induced apoptosisApoptotic signalingKinase activationP38 inhibitorRat retinal ganglion cellsCell deathCell typesOptic nerve traumaAntiapoptotic role of the p38 mitogen-activated protein kinase–myocyte enhancer factor 2 transcription factor pathway during neuronal differentiation
Okamoto S, Krainc D, Sherman K, Lipton S. Antiapoptotic role of the p38 mitogen-activated protein kinase–myocyte enhancer factor 2 transcription factor pathway during neuronal differentiation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 7561-7566. PMID: 10852968, PMCID: PMC16585, DOI: 10.1073/pnas.130502697.Peer-Reviewed Original ResearchConceptsMyocyte enhancer factor 2Mitogen-activated protein kinase p38alphaNeuronal differentiationDominant-negative p38alphaProtein kinase p38alphaDominant-negative formTranscription factor pathwaysMADS familyMEF2 familyMEF2 pathwayCell divisionTranscription factorsMyogenic phenotypeExpression patternsMyogenic factorsAntiapoptotic roleCell deathMammalian cerebral cortexP38alphaApoptotic deathNegative formPrecursor cellsFactor 2Factor pathwayApoptosis
1999
Signaling Events in NMDA Receptor‐Induced Apoptosis in Cerebrocortical Cultures
BUDD S, LIPTON S. Signaling Events in NMDA Receptor‐Induced Apoptosis in Cerebrocortical Cultures. Annals Of The New York Academy Of Sciences 1999, 893: 261-264. PMID: 10672244, DOI: 10.1111/j.1749-6632.1999.tb07832.x.Peer-Reviewed Original Research
1998
Calcium tsunamis: do astrocytes transmit cell death messages via gap junctions during ischemia?
Budd S, Lipton S. Calcium tsunamis: do astrocytes transmit cell death messages via gap junctions during ischemia? Nature Neuroscience 1998, 1: 431-432. PMID: 10196536, DOI: 10.1038/2147.Peer-Reviewed Original ResearchRole of Caspases in N‐Methyl‐d‐Aspartate‐Induced Apoptosis in Cerebrocortical Neurons
Tenneti L, D'Emilia D, Troy C, Lipton S. Role of Caspases in N‐Methyl‐d‐Aspartate‐Induced Apoptosis in Cerebrocortical Neurons. Journal Of Neurochemistry 1998, 71: 946-959. PMID: 9721720, DOI: 10.1046/j.1471-4159.1998.71030946.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid Chloromethyl KetonesAnimalsApoptosisCalciumCaspase 1Cells, CulturedCerebral CortexCysteine EndopeptidasesCysteine Proteinase InhibitorsIntracellular MembranesLipid PeroxidesMembrane PotentialsMitochondriaNeuronsN-MethylaspartateRatsRats, Sprague-DawleyReactive Oxygen SpeciesSignal TransductionConceptsInterleukin-1beta-converting enzymeMitochondrial membrane potentialReactive oxygen speciesRole of caspasesZ-VAD-FMKROS formationMembrane potentialReceptor activationCaspase activationDownstream eventsPseudosubstrate peptideNeuronal apoptosisMitochondrial depolarizationCysteine proteasesLipid peroxidationCaspasesCerebrocortical neuronsSubstrate cleavageIntracellular processesForm of deathN-methyl-D-aspartate (NMDA) receptor activationCortical neuronal apoptosisApoptosisCatalytic siteNMDA receptor activationCalcium, free radicals and excitotoxins in neuronal apoptosis
Lipton S, Nicotera P. Calcium, free radicals and excitotoxins in neuronal apoptosis. Cell Calcium 1998, 23: 165-171. PMID: 9601612, DOI: 10.1016/s0143-4160(98)90115-4.Peer-Reviewed Original Research
1997
(S)NO Signals: Translocation, Regulation, and a Consensus Motif
Stamler J, Toone E, Lipton S, Sucher N. (S)NO Signals: Translocation, Regulation, and a Consensus Motif. Neuron 1997, 18: 691-696. PMID: 9182795, DOI: 10.1016/s0896-6273(00)80310-4.Peer-Reviewed Original ResearchJanus faces of NF-κB: Neurodestruction versus neuroprotection
Lipton S. Janus faces of NF-κB: Neurodestruction versus neuroprotection. Nature Medicine 1997, 3: 20-22. PMID: 8986730, DOI: 10.1038/nm0197-20.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, CDAnti-Inflammatory Agents, Non-SteroidalApoptosisAspirinCell DeathCerebrovascular DisordersCyclooxygenase InhibitorsDose-Response Relationship, DrugHumansNeuronsNF-kappa BReactive Oxygen SpeciesReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ISignal TransductionTumor Necrosis Factor-alpha
1996
Cytoskeletal Breakdown and Apoptosis Elicited by NO Donors in Cerebellar Granule Cells Require NMDA Receptor Activation
Bonfoco E, Leist M, Zhivotovsky B, Orrenius S, Lipton S, Nicotera P. Cytoskeletal Breakdown and Apoptosis Elicited by NO Donors in Cerebellar Granule Cells Require NMDA Receptor Activation. Journal Of Neurochemistry 1996, 67: 2484-2493. PMID: 8931482, DOI: 10.1046/j.1471-4159.1996.67062484.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisAstrocytesCalciumCells, CulturedCerebellumCysteineCytoskeletonDizocilpine MaleateDNA FragmentationEnzyme InhibitorsExcitatory Amino Acid AntagonistsNitric OxidePenicillaminePotassiumRatsRats, Sprague-DawleyReceptors, N-Methyl-D-AspartateSignal TransductionS-Nitroso-N-AcetylpenicillamineS-NitrosothiolsTyrosineConceptsCultured cerebellar granule cellsNMDA receptor activationCerebellar granule cellsCytoskeletal breakdownGranule cellsReceptor activationUncompetitive NMDA receptor antagonistsD-aminophosphonovaleric acidNecrosis of neuronsS-nitrosocysteineNO donor S-nitrosocysteineNMDA receptor antagonistNitric oxide donorTyrosine nitrationReceptor antagonistMK-801Astroglial cellsOxide donorIntracellular Ca2NO donorBreakdown of microtubulesCerebellar astroglial cellsApoptosisUnderwent apoptosisCytoskeletal alterations