2013
Regulation of HA14‐1 mediated oxidative stress, toxic response, and autophagy by curcumin to enhance apoptotic activity in human embryonic kidney cells
Ranjan K, Sharma A, Surolia A, Pathak C. Regulation of HA14‐1 mediated oxidative stress, toxic response, and autophagy by curcumin to enhance apoptotic activity in human embryonic kidney cells. BioFactors 2013, 40: 157-169. PMID: 23559532, DOI: 10.1002/biof.1098.Peer-Reviewed Original ResearchMeSH KeywordsAntineoplastic AgentsApoptosisAutophagyBenzopyransCaspase 3CatalaseCell ProliferationCell SurvivalCurcuminDrug Resistance, NeoplasmDrug SynergismHEK293 CellsHumansMembrane Potential, MitochondrialNitrilesOxidative StressProto-Oncogene Proteins c-bcl-2Reactive Oxygen SpeciesSuperoxide DismutaseTranscription Factor RelAConceptsHuman embryonic kidney cellsHA14-1Embryonic kidney cellsProcess of autophagyHEK 293T cellsOxidative stressAntiapoptotic protein Bcl-2Kidney cellsProtein Bcl-2Toxic responsePromotion of malignancyAugmentation of apoptosisGeneration of ROSSignaling mechanismAntiapoptotic proteinsCell deathCancerous cell linesApoptotic activityCell proliferationBcl-2Cell linesPathological consequencesROS generationApoptosisROS
2012
A stapled BIM peptide overcomes apoptotic resistance in hematologic cancers
LaBelle JL, Katz SG, Bird GH, Gavathiotis E, Stewart ML, Lawrence C, Fisher JK, Godes M, Pitter K, Kung AL, Walensky LD. A stapled BIM peptide overcomes apoptotic resistance in hematologic cancers. Journal Of Clinical Investigation 2012, 122: 2018-2031. PMID: 22622039, PMCID: PMC3366394, DOI: 10.1172/jci46231.Peer-Reviewed Original ResearchConceptsBcl-2 family proteinsCell deathFamily proteinsPro-apoptotic Bcl-2 family proteinsBcl-2 protein familyBcl-2-interacting mediatorBcl-2 family pathwayHydrocarbon-stapled peptidesCell death mechanismsCancer cellsCellular lifeHematologic cancer cellsProtein familyDeath domainBH3 helixBim BH3Bim peptidesDeath mechanismsApoptotic blockadesApoptotic resistanceFamily pathwaySurvival pathwaysAntiapoptotic proteinsProapoptotic activityHuman AML xenograft model
2009
siRNA-based targeting of antiapoptotic genes can reverse chemoresistance in P-glycoprotein expressing chondrosarcoma cells
Kim DW, Kim KO, Shin MJ, Ha JH, Seo SW, Yang J, Lee FY. siRNA-based targeting of antiapoptotic genes can reverse chemoresistance in P-glycoprotein expressing chondrosarcoma cells. Molecular Cancer 2009, 8: 28. PMID: 19445670, PMCID: PMC2689171, DOI: 10.1186/1476-4598-8-28.Peer-Reviewed Original ResearchMeSH KeywordsAntineoplastic AgentsApoptosisATP Binding Cassette Transporter, Subfamily B, Member 1bcl-X ProteinBone NeoplasmsCell Line, TumorChondrosarcomaDoxorubicinDrug Resistance, NeoplasmFlow CytometryGene SilencingGenes, bcl-2HumansImmunoblottingReverse Transcriptase Polymerase Chain ReactionRNA, Small InterferingX-Linked Inhibitor of Apoptosis ProteinConceptsAntiapoptotic proteinsChondrosarcoma cellsAntiapoptotic genesPharmacologic inhibitorsCell survival proteinsChondrosarcoma cell linesSurvival proteinsP-glycoproteinSiRNA knockdownCell typesProteinMechanisms of chemoresistanceCell linesGenesCommon mechanismChemoresistanceSiRNACellsP-glycoprotein inhibitionTherapeutic strategiesInhibitorsKnockdownApoptosisJJ012ConclusionThese findings
2008
Vorinostat and Sorafenib Synergistically Kill Tumor Cells via FLIP Suppression and CD95 Activation
Zhang G, Park MA, Mitchell C, Hamed H, Rahmani M, Martin AP, Curiel DT, Yacoub A, Graf M, Lee R, Roberts JD, Fisher PB, Grant S, Dent P. Vorinostat and Sorafenib Synergistically Kill Tumor Cells via FLIP Suppression and CD95 Activation. Clinical Cancer Research 2008, 14: 5385-5399. PMID: 18765530, PMCID: PMC2561272, DOI: 10.1158/1078-0432.ccr-08-0469.Peer-Reviewed Original ResearchConceptsPancreatic adenocarcinoma cellsLong-term colony formation assaysCaspase-8C-FLIPExtracellular signal-regulated kinase 1/2Full-length BidSignal-regulated kinase 1/2Activation of BaxKnockdown of CD95Multiple antiapoptotic proteinsExpression of BimColony formation assaysAdenocarcinoma cellsVorinostat treatmentCD95 activationKill tumor cellsProapoptotic signalsProtease pathwayKinase 1/2Caspase-9Cathepsin proteasesAntiapoptotic proteinsBcl-xLFADD expressionMcl-1
2001
Interleukin-11 Up-Regulates Survivin Expression in Endothelial Cells through a Signal Transducer and Activator of Transcription-3 Pathway
Mahboubi K, Li F, Plescia J, Kirkiles-Smith N, Mesri M, Du Y, Carroll J, Elias J, Altieri D, Pober J. Interleukin-11 Up-Regulates Survivin Expression in Endothelial Cells through a Signal Transducer and Activator of Transcription-3 Pathway. Laboratory Investigation 2001, 81: 327-334. PMID: 11310826, DOI: 10.1038/labinvest.3780241.Peer-Reviewed Original ResearchMeSH KeywordsDNA-Binding ProteinsEndothelium, VascularGene ExpressionHumansInhibitor of Apoptosis ProteinsInterleukin-11Microtubule-Associated ProteinsNeoplasm ProteinsPhosphorylationProteinsRNA, MessengerSerineSignal TransductionSTAT1 Transcription FactorSTAT3 Transcription FactorSurvivinTrans-ActivatorsTranscription, GeneticTransgenesUmbilical VeinsConceptsSignal transducerProtein kinase B/AktDominant-negative STAT3 mutantActivator of transcriptionSurvivin mRNA expressionTranscription 3 (STAT3) pathwayIL-11Survivin protein expressionSTAT3 mutantStimulation of serumProtein expression levelsSurvivin inductionSurvivin expressionAntiapoptotic proteinsInduces expressionMRNA expressionExpression levelsSurvivin proteinProtein expressionCritical mediatorMaximal inductionExpressionSurvivin mRNAProteinDose-dependent manner
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