2012
ALDH1A 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 miceMolecular mechanisms of ALDH3A1-mediated cellular protection against 4-hydroxy-2-nonenal
Black W, Chen Y, Matsumoto A, Thompson DC, Lassen N, Pappa A, Vasiliou V. Molecular mechanisms of ALDH3A1-mediated cellular protection against 4-hydroxy-2-nonenal. Free Radical Biology And Medicine 2012, 52: 1937-1944. PMID: 22406320, PMCID: PMC3457646, DOI: 10.1016/j.freeradbiomed.2012.02.050.Peer-Reviewed Original ResearchConceptsAldehyde dehydrogenasesOxidative stress responseCellular defense mechanismsOxidative stressHuman ALDH3A1Proteasome functionMolecular mechanismsPrevents apoptosisStress responseCellular protectionLipid peroxidationAdverse effectsWestern blot analysisAldehydic moleculesGlutathione homeostasisALDH3A1 expressionCell viability assaysMetabolic functionsALDH3A1Blot analysisDefense mechanismsProtein adduct formationCell linesCell viabilityViability assays
2005
Butylhydroquinone Protects Cells Genetically Deficient in Glutathione Biosynthesis from Arsenite-Induced Apoptosis Without Significantly Changing Their Prooxidant Status
Kann S, Estes C, Reichard JF, Huang MY, Sartor MA, Schwemberger S, Chen Y, Dalton TP, Shertzer HG, Xia Y, Puga A. Butylhydroquinone Protects Cells Genetically Deficient in Glutathione Biosynthesis from Arsenite-Induced Apoptosis Without Significantly Changing Their Prooxidant Status. Toxicological Sciences 2005, 87: 365-384. PMID: 16014739, DOI: 10.1093/toxsci/kfi253.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisArsenitesBlotting, WesternCell SurvivalCells, CulturedDNA, ComplementaryElectrophoretic Mobility Shift AssayFibroblastsGene Expression RegulationGlutamate-Cysteine LigaseGlutathioneHydroquinonesMiceMice, KnockoutNF-kappa BOligonucleotide Array Sequence AnalysisOxidantsOxidative StressRNATetrazolium SaltsThiazolesConceptsMouse embryo fibroblastsGlutathione biosynthesisGlobal gene expression profilesAntioxidant responseCell cycle regulationArsenite-induced apoptosisEffective antioxidant responseArsenic-induced apoptosisGene expression profilesExpression of genesGlutamate-cysteine ligaseOxidative stressProtein biosynthesisRole of glutathioneCycle regulationRate-limiting enzymeGene deregulationExpression profilesArsenic-induced oxidative stressEmbryo fibroblastsInduces oxidative stressModifier subunitApoptotic deathDNA damageToxicity of arsenic