2022
Oxidative stress induces inflammation of lens cells and triggers immune surveillance of ocular tissues
Thompson B, Davidson EA, Chen Y, Orlicky DJ, Thompson DC, Vasiliou V. Oxidative stress induces inflammation of lens cells and triggers immune surveillance of ocular tissues. Chemico-Biological Interactions 2022, 355: 109804. PMID: 35123994, PMCID: PMC9136680, DOI: 10.1016/j.cbi.2022.109804.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteineAnimalsButhionine SulfoximineCell LineChemokine CCL7CytokinesDown-RegulationEpithelial CellsEpithelial-Mesenchymal TransitionEyeGlutamate-Cysteine LigaseImmunity, InnateLens, CrystallineLeukocytesMiceMice, Inbred C57BLMice, KnockoutOxidative StressReactive Oxygen SpeciesUp-RegulationConceptsPosterior capsule opacificationCytokine expressionKO miceImmune surveillanceOxidative stressLens epithelial cellsOcular structuresLens cellsDevelopment of PCOEpithelial cellsInnate immune cellsExpression of cytokinesEx vivo inductionOcular surface tissuesExpression of markersImmune response genesCON miceControl miceCapsule opacificationImmune cellsPostnatal dayΑ-SMAMouse modelOcular tissuesVivo induction
2013
ALDH16A1 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
Molecular 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
2010
Aldehyde Dehydrogenase 1B1: Molecular Cloning and Characterization of a Novel Mitochondrial Acetaldehyde-Metabolizing Enzyme
Stagos D, Chen Y, Brocker C, Donald E, Jackson BC, Orlicky DJ, Thompson DC, Vasiliou V. Aldehyde Dehydrogenase 1B1: Molecular Cloning and Characterization of a Novel Mitochondrial Acetaldehyde-Metabolizing Enzyme. Drug Metabolism And Disposition 2010, 38: 1679-1687. PMID: 20616185, PMCID: PMC2957164, DOI: 10.1124/dmd.110.034678.Peer-Reviewed Original ResearchMeSH KeywordsAcetaldehydeAldehyde DehydrogenaseAldehyde Dehydrogenase 1 FamilyAldehyde Dehydrogenase, MitochondrialAmino Acid SequenceAnimalsBaculoviridaeBlotting, WesternCell LineCloning, MolecularEthanolGenetic VectorsHumansImmunohistochemistryInsectaMaleMiceMice, Inbred C57BLMice, KnockoutMitochondriaMolecular Sequence DataNADOrgan SpecificityOxidation-ReductionPlasmidsRecombinant ProteinsReverse Transcriptase Polymerase Chain ReactionSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization