2016
Heme oxygenase 1 protects ethanol-administered liver tissue in Aldh2 knockout mice
Matsumoto A, Thompson D, Chen Y, Vasiliou V, Kawamoto T, Ichiba M. Heme oxygenase 1 protects ethanol-administered liver tissue in Aldh2 knockout mice. Alcohol 2016, 52: 49-54. PMID: 27139237, DOI: 10.1016/j.alcohol.2016.02.004.Peer-Reviewed Original ResearchConceptsAldh2 knockout miceStress-related proteinsOxidative stress-related proteinsAlanine transaminaseAnti-oxidative proteinsKnockout miceHealthy individualsHepatic tumor necrosis factor alphaLiver tissueProtective factorsTumor necrosis factor alphaSerum alanine transaminaseRecent epidemiological studiesNecrosis factor alphaWild-type miceHeme oxygenase-1Cytochrome P450 2E1ALDH2 proteinProteinAldehyde dehydrogenase 2 geneHepatic malondialdehydeMechanistic explanationInflammatory cytokinesEthanol administrationMechanistic hypotheses
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
2010
Structural and Functional Modifications of Corneal Crystallin ALDH3A1 by UVB Light
Estey T, Chen Y, Carpenter JF, Vasiliou V. Structural and Functional Modifications of Corneal Crystallin ALDH3A1 by UVB Light. PLOS ONE 2010, 5: e15218. PMID: 21203538, PMCID: PMC3006428, DOI: 10.1371/journal.pone.0015218.Peer-Reviewed Original ResearchConceptsActive site CysNon-native aggregationNon-covalent interactionsAldehyde dehydrogenase 3A1MALDI-TOF mass spectrometryMammalian corneal epitheliumCorneal crystallinsSpectroscopic studiesChemical modificationUV-induced damageCys residuesGlucose-6-phosphate dehydrogenaseTertiary structureMass spectrometryMultifaceted roleResult of aggregationALDH3A1Enzymatic activityCorneal proteinsUV-induced inactivationOxidative stressProteinFunctional modificationsResiduesDirect absorption
2008
Knock-In Mouse Lines Expressing either Mitochondrial or Microsomal CYP1A1: Differing Responses to Dietary Benzo[a]pyrene as Proof of Principle
Dong H, Dalton TP, Miller ML, Chen Y, Uno S, Shi Z, Shertzer HG, Bansal S, Avadhani NG, Nebert DW. Knock-In Mouse Lines Expressing either Mitochondrial or Microsomal CYP1A1: Differing Responses to Dietary Benzo[a]pyrene as Proof of Principle. Molecular Pharmacology 2008, 75: 555-567. PMID: 19047483, PMCID: PMC2684908, DOI: 10.1124/mol.108.051888.Peer-Reviewed Original ResearchConceptsMitochondrial importCryptic targeting signalMitochondrial-targeting signalSignal recognition particleInner mitochondrial membraneDifferent substrate specificitiesMouse linesCYP1A1 proteinTargeting signalsRecognition particleCYP1A1 enzymeSubstrate specificityMitochondrial membraneEndoplasmic reticulumBaP toxicityPhysiological functionsTerminal processingProteinCytosolic peptidasesProof of principleMutationsEnzymeInducer propertiesCYP1B1 mRNAMicrosomal CYP1A1