2023
Multi-omics profiling reveals cellular pathways and functions regulated by ALDH1B1 in colon cancer cells
Wang Y, Popovic Z, Charkoftaki G, Garcia-Milian R, Lam T, Thompson D, Chen Y, Vasiliou V. Multi-omics profiling reveals cellular pathways and functions regulated by ALDH1B1 in colon cancer cells. Chemico-Biological Interactions 2023, 384: 110714. PMID: 37716420, PMCID: PMC10807983, DOI: 10.1016/j.cbi.2023.110714.Peer-Reviewed Original ResearchColon cancer cellsCellular stress response pathwaysStress response pathwaysMulti-omics analysisCancer cellsSecond messenger signalingMulti-omics profilingNew molecular informationFunctional annotationCellular functionsResponse pathwaysKinase signalingCellular pathwaysColon adenocarcinoma cell lineHuman colon adenocarcinoma cell lineApoptosis signalingEnrichment analysisAldehyde dehydrogenase 1B1Molecular signaturesAdenocarcinoma cell lineMolecular informationSignalingNovel targetProtein expressionCell lines
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 ResearchConceptsCRC 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 markersMarkers
2016
Aldehyde 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
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
2005
Cytokines differentially regulate the synthesis of prostanoid and nitric oxide mediators in tumorigenic versus non-tumorigenic mouse lung epithelial cell lines
Dwyer-Nield L, Srebernak M, Barrett B, Ahn J, Cosper P, Meyer A, Kisley L, Bauer A, Thompson D, Malkinson A. Cytokines differentially regulate the synthesis of prostanoid and nitric oxide mediators in tumorigenic versus non-tumorigenic mouse lung epithelial cell lines. Carcinogenesis 2005, 26: 1196-1206. PMID: 15746162, DOI: 10.1093/carcin/bgi061.Peer-Reviewed Original ResearchConceptsMouse lung epithelial cell lineLung epithelial cell lineInducible NO synthaseBiosynthetic enzymesEpithelial cell lineCell linesProstaglandin E2Lung tumor-derived cell linesTumor-derived cell linesNon-tumorigenic linesNitric oxidePG biosynthetic enzymesCytokine exposureInhibition of iNOSNormal lung cellsCyclooxygenase-2 activityPhysiological relevanceLung tumor formationLung tumor growthMouse lung tumorsSpontaneous transformantsTumor formationCritical mediatorControl lungsEpithelial cells
2000
Growth inhibition in G1 and altered expression of cyclin D1 and p27kip‐1 after forced connexin expression in lung and liver carcinoma cells
Koffler L, Roshong S, Park I, Cesen‐Cummings K, Thompson D, Dwyer‐Nield L, Rice P, Mamay C, Malkinson A, Ruch R. Growth inhibition in G1 and altered expression of cyclin D1 and p27kip‐1 after forced connexin expression in lung and liver carcinoma cells. Journal Of Cellular Biochemistry 2000, 79: 347-354. PMID: 10972973, DOI: 10.1002/1097-4644(20001201)79:3<347::aid-jcb10>3.0.co;2-2.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarcinomaCell CommunicationCell Cycle ProteinsCell DivisionConnexinsCyclin D1Cyclin-Dependent Kinase Inhibitor p27CytokinesDiffusionFluorescent DyesG1 PhaseGap JunctionsGene Expression Regulation, NeoplasticLiver Neoplasms, ExperimentalLung NeoplasmsMiceMicrotubule-Associated ProteinsNeoplasm ProteinsNitric OxideProtein KinasesRatsReceptors, Growth FactorRecombinant Fusion ProteinsTransfectionTumor Cells, CulturedTumor Suppressor ProteinsConceptsGap junctional intercellular communicationRat liver epithelial cellsConnexin expressionE9 cellsLiver epithelial cellsGrowth controlDefective growth controlCyclin D1Growth-related functionsTransfection of Cx43Cell cycle regulatorsCell linesEpithelial cellsGap junction proteinCarcinoma cellsMouse lung carcinoma cellsJunctional intercellular communicationLess cyclin D1Cell cycle distributionCycle regulatorsForced expressionIntercellular communicationS phaseP27kip-1Lung carcinoma cells
1998
Cytokine-induced nitric oxide formation in normal but not in neoplastic murine lung epithelial cell lines
Thompson D, Porter S, Bauer A, Das K, Ou B, Dwyer-Nield L, White C, Malkinson A. Cytokine-induced nitric oxide formation in normal but not in neoplastic murine lung epithelial cell lines. American Journal Of Physiology 1998, 274: l922-l932. PMID: 9609731, DOI: 10.1152/ajplung.1998.274.6.l922.Peer-Reviewed Original ResearchConceptsLung epithelial cell lineEpithelial cell lineLung epithelial cellsNontumorigenic cellsCell linesMurine lung epithelial cell lineEpithelial cellsMurine lung epithelial cellsTumorigenic counterpartsMRNA stabilityE10 cellsTumorigenic cellsWestern blot analysisProtein synthesisNormal progenitor cellsCell's abilityINOS regulationNuclear factor-kappaB activationProgenitor cellsCytokine-induced NO synthesisSpontaneous transformantsBlot analysisInducible NO synthaseMurine linesTransformation alters