2022
Proteomic profiling reveals an association between ALDH and oxidative phosphorylation and DNA damage repair pathways in human colon adenocarcinoma stem cells
Wang Y, Chen Y, Garcia-Milian R, Golla JP, Charkoftaki G, Lam TT, Thompson DC, Vasiliou V. Proteomic profiling reveals an association between ALDH and oxidative phosphorylation and DNA damage repair pathways in human colon adenocarcinoma stem cells. Chemico-Biological Interactions 2022, 368: 110175. PMID: 36162455, PMCID: PMC9891852, DOI: 10.1016/j.cbi.2022.110175.Peer-Reviewed Original ResearchConceptsCancer stem cellsProteomic profilingOxidative phosphorylationLabel-free quantitative proteomic analysisDNA damage repair pathwaysQuantitative proteomic analysisAldehyde dehydrogenase familyColon cancer stem cellsCOLO320DM cellsStem cellsNucleotide excision repairDamage repair pathwaysIngenuity Pathway AnalysisCell populationsProteomic analysisProteomic datasetsDehydrogenase familyMetabolic switchProteomic studiesRepair pathwaysCellular pathwaysALDH enzymatic activityCellular survivalExcision repairALDH activity
2019
Expression, purification and crystallization of the novel Xenopus tropicalis ALDH16B1, a homologue of human ALDH16A1
Pantouris G, Dioletis E, Chen Y, Thompson DC, Vasiliou V, Lolis EJ. Expression, purification and crystallization of the novel Xenopus tropicalis ALDH16B1, a homologue of human ALDH16A1. Chemico-Biological Interactions 2019, 304: 168-172. PMID: 30894314, PMCID: PMC6746316, DOI: 10.1016/j.cbi.2019.03.009.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAnimalsBiocatalysisChromatography, GelCrystallography, X-RayHumansModels, MolecularProtein ConformationXenopusXenopus ProteinsConceptsAldehyde dehydrogenaseCritical Cys residuesPreliminary crystallographic analysisGenomic analysisSf9 cellsCys residuesALDH16A1Novel familyLower animalsSize exclusion chromatographyActive siteStructure determinationMetabolomics studiesCrystallographic analysisCellsMammalsHomologuesGenesExclusion chromatographyFishStructural characteristicsFrogsPathogenesis of goutUnique structural characteristicsResiduesIntegrated multi-omics approach reveals a role of ALDH1A1 in lipid metabolism in human colon cancer cells
Charkoftaki G, Thompson DC, Golla JP, Garcia-Milian R, Lam TT, Engel J, Vasiliou V. Integrated multi-omics approach reveals a role of ALDH1A1 in lipid metabolism in human colon cancer cells. Chemico-Biological Interactions 2019, 304: 88-96. PMID: 30851239, PMCID: PMC7988342, DOI: 10.1016/j.cbi.2019.02.030.Peer-Reviewed Original Research
2017
Aldehyde dehydrogenase 1B1: a novel immunohistological marker for colorectal cancer
Matsumoto A, Arcaroli J, Chen Y, Gasparetto M, Neumeister V, Thompson DC, Singh S, Smith C, Messersmith W, Vasiliou V. Aldehyde dehydrogenase 1B1: a novel immunohistological marker for colorectal cancer. British Journal Of Cancer 2017, 117: 1537-1543. PMID: 28881356, PMCID: PMC5680456, DOI: 10.1038/bjc.2017.304.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialBiomarkers, TumorColorectal NeoplasmsHumansImmunohistochemistryConceptsCRC markersTumor tissueNormal tissuesCell linesHuman CRC explantsCRC cell linesColorectal cancer markersAldehyde dehydrogenase 1A1CRC explantsImmunohistological biomarkersColorectal cancerCRC biomarkersImmunohistological markersTissue microarraySolid tumorsLow expressionMicroarray findingsGenetic alterationsALDH isozymesCell populationsALDH1A1CRCMRNA analysisCancer markersMarkersTranscriptomic analysis and plasma metabolomics in Aldh16a1-null mice reveals a potential role of ALDH16A1 in renal function
Charkoftaki G, Chen Y, Han M, Sandoval M, Yu X, Zhao H, Orlicky DJ, Thompson DC, Vasiliou V. Transcriptomic analysis and plasma metabolomics in Aldh16a1-null mice reveals a potential role of ALDH16A1 in renal function. Chemico-Biological Interactions 2017, 276: 15-22. PMID: 28254523, PMCID: PMC5725231, DOI: 10.1016/j.cbi.2017.02.013.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAnimalsDown-RegulationGene Expression ProfilingKidneyLipidsMetabolomicsMiceMice, Inbred C57BLMice, KnockoutMonocarboxylic Acid TransportersMultidrug Resistance-Associated ProteinsMutation, MissenseSequence Analysis, RNASodium-Phosphate Cotransporter Proteins, Type IUp-RegulationConceptsUric acid homeostasisPlasma metabolomicsElevated serum uric acid levelsSerum uric acid levelsDistal convoluted tubule cellsAcid homeostasisUric acid levelsZone 3 hepatocytesConvoluted tubule cellsSingle nucleotide variantsRenal functionKO miceLipid profileKnockout miceMissense single nucleotide variantsTubule cellsRNA-seq analysisKidneyMouse linesAcid levelsMicePotential roleLipid metabolic processMetabolomic analysisCellular lipids
2016
Corneal haze phenotype in Aldh3a1-null mice: In vivo confocal microscopy and tissue imaging mass spectrometry
Chen Y, Jester JV, Anderson DM, Marchitti SA, Schey KL, Thompson DC, Vasiliou V. Corneal haze phenotype in Aldh3a1-null mice: In vivo confocal microscopy and tissue imaging mass spectrometry. Chemico-Biological Interactions 2016, 276: 9-14. PMID: 28038895, DOI: 10.1016/j.cbi.2016.12.017.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAnimalsCorneaCorneal DiseasesCorneal StromaDiazepam Binding InhibitorDisease Models, AnimalDynamic Light ScatteringEpitheliumEpithelium, CornealHistonesLens, CrystallineLipidsMiceMice, Inbred C57BLMice, KnockoutMicroscopy, ConfocalPhenotypeSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationConceptsImaging mass spectrometryCorneal crystallinsNon-catalytic functionsAcyl-CoA binding proteinFirst genetic animal modelCellular transparencyCorneal epithelial homeostasisCorneal hazeEndogenous proteinsKO miceLipid localizationMixed genetic backgroundKnockout miceCorneal phenotypeEpithelial homeostasisProtein profilesWild-type corneasBinding proteinFunctional roleGenetic backgroundLens cataractMass spectrometryConfocal microscopyMolecular changesPhenotypeALDH3A1 Plays a Functional Role in Maintenance of Corneal Epithelial Homeostasis
Koppaka V, Chen Y, Mehta G, Orlicky DJ, Thompson DC, Jester JV, Vasiliou V. ALDH3A1 Plays a Functional Role in Maintenance of Corneal Epithelial Homeostasis. PLOS ONE 2016, 11: e0146433. PMID: 26751691, PMCID: PMC4708999, DOI: 10.1371/journal.pone.0146433.Peer-Reviewed Original ResearchConceptsCorneal cell proliferationCorneal epithelial homeostasisCell proliferationALDH3A1 expressionEpithelial homeostasisHuman corneal epithelial cell lineDouble knockout miceAnti-proliferation effectCorneal epithelial cell lineCorneal epithelial proliferationAldehyde dehydrogenase 1A1Epithelial cell lineCorneal differentiation markersInner ocular tissuesInverse associationFunctional roleEpithelial proliferationKnockout miceP53 expressionCorneal epitheliumOcular tissuesMouse corneaCalcium concentrationMRNA levelsEpithelial differentiationAldehyde Dehydrogenase 1B1 as a Modulator of Pancreatic Adenocarcinoma
Singh S, Arcaroli JJ, Orlicky DJ, Chen Y, Messersmith WA, Bagby S, Purkey A, Quackenbush KS, Thompson DC, Vasiliou V. Aldehyde Dehydrogenase 1B1 as a Modulator of Pancreatic Adenocarcinoma. Pancreas 2016, 45: 117-122. PMID: 26566217, PMCID: PMC5175203, DOI: 10.1097/mpa.0000000000000542.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAnimalsBiomarkers, TumorCarcinoma, Pancreatic DuctalCell Line, TumorCell ProliferationFemaleGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticHumansImmunohistochemistryMice, NudeNeoplasm InvasivenessPancreatic NeoplasmsRNA InterferenceSignal TransductionTissue Array AnalysisTransfectionTumor BurdenUp-RegulationConceptsALDH1B1 expressionPancreatic cancerPancreatic adenocarcinomaTissue microarrayHuman pancreatic cancer cell linesPancreatic cancer cell linesPancreatic cancer patientsPancreatic ductal carcinomaHuman pancreatic cancerAldehyde dehydrogenase 1B1Potential modulatory rolePancreatic cancer cellsNormal human pancreasCell linesCancer cell linesDuctal carcinomaCancer patientsModulatory roleHuman pancreasGlandular cellsTumor cellsProtein expressionCancer cellsGreater expressionAdenocarcinoma
2015
Dead enzymes in the aldehyde dehydrogenase gene family: role in drug metabolism and toxicology
Jackson BC, Thompson DC, Charkoftaki G, Vasiliou V. Dead enzymes in the aldehyde dehydrogenase gene family: role in drug metabolism and toxicology. Expert Opinion On Drug Metabolism & Toxicology 2015, 11: 1839-1847. PMID: 26558415, PMCID: PMC4937717, DOI: 10.1517/17425255.2016.1108406.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAllosteric RegulationAnimalsCatalysisDrug-Related Side Effects and Adverse ReactionsHumansIsoenzymesPharmaceutical PreparationsConceptsAldehyde dehydrogenase gene familiesDehydrogenase gene familyDead enzymesGene familyActive enzymeProtein-protein interactionsTotal enzyme populationNon-enzymatic functionsALDH proteinsAvailability of substratesSubcellular spaceGene productsKey residuesProtein recordsCatalytic activityEnzyme populationPathophysiological functionsAllosteric modulationEnzymeBiological actionsProteinBiological activityComputational analysisALDHFamilyALDH1B1 links alcohol consumption and diabetes
Singh S, Chen Y, Matsumoto A, Orlicky DJ, Dong H, Thompson DC, Vasiliou V. ALDH1B1 links alcohol consumption and diabetes. Biochemical And Biophysical Research Communications 2015, 463: 768-773. PMID: 26086111, PMCID: PMC4517591, DOI: 10.1016/j.bbrc.2015.06.011.Peer-Reviewed Original ResearchMeSH KeywordsAlcohol DrinkingAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAnimalsBase SequenceDiabetes Mellitus, ExperimentalDNA PrimersEthanolGlucoseHomeostasisMiceMice, KnockoutReal-Time Polymerase Chain ReactionReverse Transcriptase Polymerase Chain ReactionConceptsKO miceDevelopment of diabetesBlood glucose levelsBlood acetaldehyde levelsAldehyde dehydrogenase 1B1Knockout mouse lineGlucose levelsPharmacokinetic analysisMouse modelGlucose homeostasisKnockout miceAlcohol consumptionAcetaldehyde levelsAcetaldehyde metabolismGood healthMouse linesALDH2 proteinMiceALDH isozymesAlcohol sensitivityDiabetesStem cellsALDH1B1Physiological functionsMitochondrial enzymesALDH1B1 Is Crucial for Colon Tumorigenesis by Modulating Wnt/β-Catenin, Notch and PI3K/Akt Signaling Pathways
Singh S, Arcaroli J, Chen Y, Thompson DC, Messersmith W, Jimeno A, Vasiliou V. ALDH1B1 Is Crucial for Colon Tumorigenesis by Modulating Wnt/β-Catenin, Notch and PI3K/Akt Signaling Pathways. PLOS ONE 2015, 10: e0121648. PMID: 25950950, PMCID: PMC4423958, DOI: 10.1371/journal.pone.0121648.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAnimalsCell Line, TumorColonic NeoplasmsGene Expression Regulation, NeoplasticHCT116 CellsHT29 CellsHumansMiceNeoplasm TransplantationPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktReceptors, NotchRNA, Small InterferingSignal TransductionSpheroids, CellularWnt Signaling PathwayConceptsWnt/β-cateninPI3K/AktΒ-cateninSW-480 cellsColon cancer tumorigenesisWnt reporter activityPattern of expressionPI3K/Akt Signaling PathwayDual-luciferase reporterPI3K/Akt signal pathwayAkt Signaling PathwayTranscription factorsAkt signal pathwayNude mouse xenograft tumor modelColon tumorigenesisGene promoterColon adenocarcinoma cell lineMouse xenograft tumor modelALDH1B1 expressionAldehyde dehydrogenase 1B1Signaling pathwaysLuciferase reporterSize of spheroidsAdenocarcinoma cell lineXenograft tumor model
2014
Human ALDH1B1 Polymorphisms may Affect the Metabolism of Acetaldehyde and All-trans retinaldehyde—In Vitro Studies and Computational Modeling
Jackson BC, Reigan P, Miller B, Thompson DC, Vasiliou V. Human ALDH1B1 Polymorphisms may Affect the Metabolism of Acetaldehyde and All-trans retinaldehyde—In Vitro Studies and Computational Modeling. Pharmaceutical Research 2014, 32: 1648-1662. PMID: 25413692, PMCID: PMC4382438, DOI: 10.1007/s11095-014-1564-3.Peer-Reviewed Original ResearchAcetaldehydeAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAldehydesAmino Acid SequenceComputer SimulationHumansModels, BiologicalModels, MolecularMolecular Sequence DataNitroglycerinPolymorphism, GeneticProtein ConformationRetinaldehydeSubstrate SpecificityAcetaldehyde and Retinaldehyde-Metabolizing Enzymes in Colon and Pancreatic Cancers
Singh S, Arcaroli J, Thompson DC, Messersmith W, Vasiliou V. Acetaldehyde and Retinaldehyde-Metabolizing Enzymes in Colon and Pancreatic Cancers. Advances In Experimental Medicine And Biology 2014, 815: 281-294. PMID: 25427913, PMCID: PMC4347404, DOI: 10.1007/978-3-319-09614-8_16.Peer-Reviewed Original ResearchMeSH KeywordsAcetaldehydeAldehyde DehydrogenaseCell ProliferationColorectal NeoplasmsHumansPancreatic NeoplasmsRetinaldehydeTretinoinConceptsPancreatic cancerColorectal cancerRetinoic acidChronic alcohol consumptionImportant risk factorCancer-related deathCancer stem cellsProgression of cancerPoor prognosisEventual prognosisRisk factorsAlcohol consumptionCancerImportant mechanistic roleTumor developmentRetinaldehyde dehydrogenasesCancer initiationPrognosisColonTumorsStem cellsProgressionBiomarkersALDH1A1Mechanistic role
2013
Aldehyde dehydrogenase 3A1 protects airway epithelial cells from cigarette smoke-induced DNA damage and cytotoxicity
Jang JH, Bruse S, Liu Y, Duffy V, Zhang C, Oyamada N, Randell S, Matsumoto A, Thompson DC, Lin Y, Vasiliou V, Tesfaigzi Y, Nyunoya T. Aldehyde dehydrogenase 3A1 protects airway epithelial cells from cigarette smoke-induced DNA damage and cytotoxicity. Free Radical Biology And Medicine 2013, 68: 80-86. PMID: 24316006, PMCID: PMC3941192, DOI: 10.1016/j.freeradbiomed.2013.11.028.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAldehydesApoptosisBronchiCell SurvivalCells, CulturedDNA DamageEpithelial CellsHumansRNA, Small InterferingSmokingConceptsHuman bronchial epithelial cellsImmortalized human bronchial epithelial cellsCigarette smokeALDH enzymatic activityCigarette smoke-induced DNA damageAldehyde dehydrogenase 3A1Smoke-induced DNA damagePrimary human bronchial epithelial cellsEpithelial cellsCSE-exposed cellsCSE-induced cytotoxicityBronchial epithelial cellsDNA damageExtract exposureMRNA levelsEffects of overexpressionALDH16A1 is a novel non-catalytic enzyme that may be involved in the etiology of gout via protein–protein interactions with HPRT1
Vasiliou V, Sandoval M, Backos DS, Jackson BC, Chen Y, Reigan P, Lanaspa MA, Johnson RJ, Koppaka V, Thompson DC. ALDH16A1 is a novel non-catalytic enzyme that may be involved in the etiology of gout via protein–protein interactions with HPRT1. Chemico-Biological Interactions 2013, 202: 22-31. PMID: 23348497, PMCID: PMC3746320, DOI: 10.1016/j.cbi.2012.12.018.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsSingle nucleotide polymorphismsSuch protein-protein interactionsCoiled-coil domainImportant cysteine residuesMissense single nucleotide polymorphismMost mammalian speciesALDH domainHuman cell linesALDH16A1Cysteine residuesMammalian speciesProtein structureUnique memberKey enzymeEtiology of goutGenesNucleotide polymorphismsHPRT activityProteinAcid metabolismCell linesLong formIntriguing possibilityLower animals
2012
Comparative genomics, molecular evolution and computational modeling of ALDH1B1 and ALDH2
Jackson BC, Holmes RS, Backos DS, Reigan P, Thompson DC, Vasiliou V. Comparative genomics, molecular evolution and computational modeling of ALDH1B1 and ALDH2. Chemico-Biological Interactions 2012, 202: 11-21. PMID: 23247008, PMCID: PMC3687035, DOI: 10.1016/j.cbi.2012.11.022.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAmino Acid SequenceAnimalsAnuraComputer SimulationEvolution, MolecularGenomicsHumansMiceModels, MolecularMolecular Sequence DataPhylogenyProtein Interaction Domains and MotifsProtein Structure, TertiarySequence AlignmentConceptsMitochondrial enzymesGenomes of birdsRepresentative vertebrate speciesProtein-protein interactionsAmino acid sequenceVertebrate genomesComparative genomicsMolecular evolutionALDH2 geneEarly vertebratesVertebrate speciesPhylogenetic analysisBioinformatics analysisAcid sequenceMammalian speciesSubunit sequencesBiological aldehydesHuman ALDH2Coenzyme bindingInactivating mutationALDH2 mutantGenesALDH1B1HeterotetramerizationGenomeAldehyde dehydrogenases in cellular responses to oxidative/electrophilicstress
Singh S, Brocker C, Koppaka V, Chen Y, Jackson BC, Matsumoto A, Thompson DC, Vasiliou V. Aldehyde dehydrogenases in cellular responses to oxidative/electrophilicstress. Free Radical Biology And Medicine 2012, 56: 89-101. PMID: 23195683, PMCID: PMC3631350, DOI: 10.1016/j.freeradbiomed.2012.11.010.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAldehyde DehydrogenaseAnimalsBacteriaCaenorhabditis elegansHumansNeoplastic Stem CellsOxidative StressPlantsReactive Oxygen SpeciesSaccharomyces cerevisiaeConceptsReactive oxygen speciesOxidative stressMulticellular speciesEukaryotic organismsElectrophilic stressExogenous aldehydesCancer stem cellsLiving systemsStress responseCellular responsesEnvironmental stressorsSimilar functionsAldehyde scavengerSpeciesStem cellsLipid peroxidationROS loadOxygen speciesElevated oxidative stressLipid membranesALDHALDH expressionOrganismsPathological processesPathological conditionsAldehyde dehydrogenases: From eye crystallins to metabolic disease and cancer stem cells
Vasiliou V, Thompson DC, Smith C, Fujita M, Chen Y. Aldehyde dehydrogenases: From eye crystallins to metabolic disease and cancer stem cells. Chemico-Biological Interactions 2012, 202: 2-10. PMID: 23159885, PMCID: PMC4128326, DOI: 10.1016/j.cbi.2012.10.026.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAldehyde DehydrogenaseAnimalsCrystallinsHumansLens, CrystallineMetabolic DiseasesNeoplastic Stem CellsConceptsAldehyde dehydrogenaseHuman ALDH genesALDH gene familyNon-catalytic activitiesEukaryotic genomesGene familyALDH genesCancer stem cellsMolecular basisDependent enzymesStem cellsAldehyde metabolismOxidative stressNicotinamide adenine dinucleotideOxidation of aldehydesPathophysiological processesAdenine dinucleotideDehydrogenaseMetabolic diseasesGenomeImportant roleEmbryogenesisGenesStructural elementsCrystallinsOcular aldehyde dehydrogenases: Protection against ultraviolet damage and maintenance of transparency for vision
Chen Y, Thompson DC, Koppaka V, Jester JV, Vasiliou V. Ocular aldehyde dehydrogenases: Protection against ultraviolet damage and maintenance of transparency for vision. Progress In Retinal And Eye Research 2012, 33: 28-39. PMID: 23098688, PMCID: PMC3570594, DOI: 10.1016/j.preteyeres.2012.10.001.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAnimalsCorneaEye InjuriesHumansLens, CrystallineRetinal DehydrogenaseUltraviolet RaysConceptsAldehyde dehydrogenasePutative regulatory functionTaxon-specific mannerNon-catalytic functionsRetinoic acid signalingALDH proteinsMaintenance of transparencyCellular transparencyAcid signalingCorneal crystallinsExogenous aldehydesEye developmentOxygen-induced damageCorneal cell proliferationStructural roleRegulatory functionsException of rabbitsMost mammalsRetinaldehyde dehydrogenasesLens crystallinsALDH1A1 proteinMammalian corneaAnimal speciesCell proliferationDependent oxidationALDH1A Isozymes are Markers of Human Melanoma Stem Cells and Potential Therapeutic Targets
Luo Y, Dallaglio K, Chen Y, Robinson WA, Robinson SE, McCarter MD, Wang J, Gonzalez R, Thompson DC, Norris DA, Roop DR, Vasiliou V, Fujita M. ALDH1A Isozymes are Markers of Human Melanoma Stem Cells and Potential Therapeutic Targets. Stem Cells 2012, 30: 2100-2113. PMID: 22887839, PMCID: PMC3448863, DOI: 10.1002/stem.1193.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde OxidoreductasesAnimalsApoptosisCell Transformation, NeoplasticDacarbazineDrug Resistance, NeoplasmFemaleGene Expression Regulation, NeoplasticGene SilencingHumansIsoenzymesMelanomaMiceMice, Inbred NODMice, SCIDNeoplasm TransplantationNeoplastic Stem CellsResponse ElementsRetinal DehydrogenaseRNA, Small InterferingSkin NeoplasmsTemozolomideTretinoinConceptsCancer stem cellsPositive melanoma cellsMelanoma cellsTherapeutic targetBiomarkers of CSCsHuman melanomaPatient-derived tumor specimensMelanoma cancer stem cellsNOD/SCID miceALDH-negative cellsHigh aldehyde dehydrogenase (ALDH) activityALDH isozymesNonobese diabetic/Potential therapeutic targetDrug-induced cell deathAttractive therapeutic targetNew molecular targetsHuman melanoma cellsStem cellsMelanoma stem cellsAldehyde dehydrogenase activityHuman melanoma stem cellsNSG miceCell cycle arrestImmunodeficiency mice