Search results for "WES"

showing 10 items of 1585 documents

cIAP1 regulates TNF-mediated cdc42 activation and filopodia formation

2013

International audience; umour necrosis factor-α (TNF) is a cytokine endowed with multiple functions, depending on the cellular and environmental context. TNF receptor engagement induces the formation of a multimolecular complex including the TNFR-associated factor TRAF2, the receptor-interaction protein kinase RIP1 and the cellular inhibitor of apoptosis cIAP1, the latter being essential for NF-κB activation. Here, we show that cIAP1 also regulates TNF-induced actin cytoskeleton reorganization through a cdc42-dependent, NF-κB-independent pathway. Deletion of cIAP1 prevents TNF-induced filopodia and cdc42 activation. The expression of cIAP1 or its E3-ubiquitin ligase-defective mutant restore…

Cancer ResearchLung NeoplasmsBlotting WesternFluorescent Antibody Techniquemacromolecular substancesCDC42BiologyTransfectionInhibitor of Apoptosis ProteinsMice03 medical and health sciences0302 clinical medicineCell AdhesionGeneticsAnimalsHumansImmunoprecipitationNeoplasm InvasivenessPseudopodia[SPI.NANO]Engineering Sciences [physics]/Micro and nanotechnologies/Microelectronicscdc42 GTP-Binding ProteinMolecular Biology030304 developmental biology0303 health sciencesTumor Necrosis Factor-alphaActin cytoskeleton reorganizationCell PolarityActin remodelingSurface Plasmon ResonanceActin cytoskeletonCell biologyActin CytoskeletonDisease Models AnimalHEK293 CellsCdc42 GTP-Binding Protein030220 oncology & carcinogenesisNIH 3T3 CellsHeterografts[ SPI.NANO ] Engineering Sciences [physics]/Micro and nanotechnologies/MicroelectronicsPseudopodiaSignal transductionFilopodiaSignal TransductionOncogene
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Expression of Hugl-1 is strongly reduced in malignant melanoma.

2005

The human gene Hugl-1 (Llgl/Lgl1) has significant homology to the Drosophila tumor suppressor gene lethal(2)giant larvae (lgl). The lgl gene codes for a cortical cytoskeleton protein, Lgl, that is involved in maintaining cell polarity and epithelial integrity. We speculate that Hugl-1 might play a role in epithelial-mesenchymal transition (EMT) and that loss of Hugl-1 expression plays a role in the development or progression of malignant melanoma. Thus, we evaluated melanoma cell lines and tissue samples of malignant melanoma for loss of Hugl-1 transcription. We found that Hugl-1 was downregulated or lost in all cell lines and in most of the tumor samples analysed, and that these losses wer…

Cancer ResearchMMP2Tumor suppressor geneMatrix Metalloproteinases Membrane-AssociatedTranscription GeneticCellBlotting WesternDown-RegulationBiologyTransfectionEpitheliumCell MovementCell Line TumorGeneticsmedicineCell AdhesionMatrix Metalloproteinase 14HumansNeoplasm InvasivenessTissue DistributionRNA MessengerCell adhesionMolecular BiologyMelanomaReverse Transcriptase Polymerase Chain ReactionMelanomaProteinsCell migrationmedicine.diseaseCadherinsImmunohistochemistryMatrix MetalloproteinasesGene Expression Regulation NeoplasticCytoskeletal Proteinsmedicine.anatomical_structureMicroscopy FluorescenceCell cultureImmunologyCancer researchDisease ProgressionMMP14Matrix Metalloproteinase 2RNAOncogene
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Multivalent DR5 peptides activate the TRAIL death pathway and exert tumoricidal activity.

2010

Abstract Ongoing clinical trials are exploring anticancer approaches based on signaling by TRAIL, a ligand for the cell death receptors DR4 and DR5. In this study, we report on the selective apoptotic effects of multivalent DR5 binding peptides (TRAILmim/DR5) on cancer cells in vitro and in vivo. Surface plasmon resonance revealed up to several thousand-fold increased affinities of TRAILmim/DR5-receptor complexes on generation of divalent and trivalent molecules, the latter of which was achieved with a conformationally restricted adamantane core. Notably, only multivalent molecules triggered a substantial DR5-dependent apoptotic response in vitro. In tumor models derived from human embryoni…

Cancer ResearchMembrane transport and intracellular motility [NCMLS 5]Apoptosis[CHIM.THER]Chemical Sciences/Medicinal Chemistry[ SDV.CAN ] Life Sciences [q-bio]/CancerTNF-Related Apoptosis-Inducing LigandMice0302 clinical medicineStilbenesReceptorCells Cultured0303 health sciencesDrug Synergism[ CHIM.THER ] Chemical Sciences/Medicinal ChemistryLigand (biochemistry)Tumor Burden3. Good healthMitochondrial medicine [IGMD 8]Oncology030220 oncology & carcinogenesisColonic NeoplasmsFemaleOligopeptidesSignal Transductionmedicine.medical_specialtyProgrammed cell deathBlotting WesternMolecular Sequence DataMice Nude[SDV.CAN]Life Sciences [q-bio]/CancerCell Line03 medical and health sciencesIn vivoInternal medicinemedicineAnimalsHumansAmino Acid Sequence030304 developmental biologybusiness.industrySurface Plasmon ResonanceHCT116 CellsAntineoplastic Agents PhytogenicXenograft Model Antitumor AssaysIn vitroReceptors TNF-Related Apoptosis-Inducing LigandEndocrinologyResveratrolCell cultureApoptosisCancer cellCancer researchbusiness
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Redistribution of CD95, DR4 and DR5 in rafts accounts for the synergistic toxicity of resveratrol and death receptor ligands in colon carcinoma cells.

2004

The natural phytoalexin resveratrol (3, 5, 4'-trihydroxystilbene) exhibits both chemopreventive and antitumor activities through a variety of mechanisms. We have shown previously that resveratrol-induced apoptosis of a human colon cancer cell line involved the redistribution of CD95 (Fas/Apo-1) into lipid rafts. Here, we show that, in colon cancer cells that resist to resveratrol-induced apoptosis, the polyphenol also induces a redistribution of death receptors into lipid rafts. This effect sensitizes these tumor cells to death receptor-mediated apoptosis. In resveratrol-treated cells, tumor necrosis factor (TNF), anti-CD95 antibodies and TNF-related apoptosis-inducing ligand (TRAIL) activa…

Cancer ResearchNystatinTime FactorsApoptosisResveratrolmedicine.disease_causeLigandsReceptors Tumor Necrosis FactorTNF-Related Apoptosis-Inducing Ligandchemistry.chemical_compoundStilbenesReceptorLipid raftCaspaseMembrane GlycoproteinsbiologyFas receptorFlow CytometryLipidsMitochondriaProto-Oncogene Proteins c-bcl-2CaspasesColonic Neoplasmslipids (amino acids peptides and proteins)Tumor necrosis factor alphaSignal Transductionmedicine.medical_specialtyBlotting WesternTransfectionMembrane MicrodomainsInternal medicineCell Line TumorGeneticsmedicineHumansfas ReceptorMolecular BiologyTumor Necrosis Factor-alphaCarcinomaLipid MetabolismAntineoplastic Agents PhytogenicReceptors TNF-Related Apoptosis-Inducing LigandEndocrinologychemistryApoptosisResveratrolCancer researchbiology.proteinCarcinogenesisApoptosis Regulatory ProteinsOncogene
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Hsp60 and Hsp10 down-regulation predicts bronchial epithelial carcinogenesis in smokers with chronic obstructive pulmonary disease.

2006

BACKGROUND. The relation between smoking, chronic obstructive pulmonary disease (COPD), and lung cancer (LC) is an open field of investigation. A higher frequency of adenocarcinoma has been reported in patients with COPD. Heat shock proteins (Hsps) are implicated in tumoral cell growth and differentiation. The aim of the present study was to investigate the expression of Hsp60 and Hsp10 in bronchial biopsies from smokers with COPD and in 10 lung cancer patients and to evaluate the association between Hsps expression and carcinogenetic steps of LC. METHODS. An immunohistochemical study was performed for Hsp60 and Hsp10 in bronchial biopsies from 35 COPD (postbronchodilator forced expiratory …

Cancer ResearchPathologymedicine.medical_specialtyLung NeoplasmsAdenosquamous carcinomaBlotting WesternDown-Regulationchemical and pharmacologic phenomenaRespiratory MucosaAdenocarcinomaCarcinoma AdenosquamousPulmonary Disease Chronic ObstructivemedicineChaperonin 10HumansLung cancerAgedsmoking chaperone expression lung obstruction lung tumorsCOPDSettore BIO/16 - Anatomia Umanabusiness.industryRespiratory diseaseSmokingCancerChaperonin 60Middle Agedmedicine.diseasePrognosisSquamous metaplasiarespiratory tract diseasesCarcinoma BronchogenicOncologyDysplasiaDisease ProgressionAdenocarcinomabusinessCancer
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The expression of HSP60 and HSP10 in large bowel carcinomas with lymph node metastase

2005

Abstract Background The involvement of Heat Shock Proteins (HSP) in cancer development and progression is a widely debated topic. The objective of the present study was to evaluate the presence and expression of HSP60 and HSP10 in a series of large bowel carcinomas and locoregional lymph nodes with and without metastases. Methods 82 Astler and Coller's stage C2 colorectal cancers, of which 48 well-differentiated and 34 poorly-differentiated, were selected along with 661 lymph nodes, including 372 with metastases and 289 with reactive hyperplasia only, from the same tumours. Primitive tumours and both metastatic and reactive lymph nodes were studied; specifically, three different compartment…

Cancer ResearchPathologymedicine.medical_specialtyTime FactorsColonColorectal cancerBlotting Westernlcsh:RC254-282Surgical oncologyIntestinal NeoplasmsBiomarkers TumorChaperonin 10GeneticsmedicineCarcinomaHumansIntestine LargeNeoplasm MetastasisStage (cooking)Lymph nodeInflammationAnalysis of VarianceHyperplasiabusiness.industryCarcinomaCell DifferentiationChaperonin 60Hyperplasialcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensmedicine.diseaseImmunohistochemistryGene Expression Regulation Neoplasticmedicine.anatomical_structureOncologyLymphatic MetastasisDisease ProgressionImmunohistochemistryhspLymph NodesLymphbusinessResearch ArticleBMC Cancer
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Diorganotin(IV) and triorganotin(IV) complexes of meso-tetra(4-sulfonatophenyl) porphine induce apoptosis in A375 human melanoma cells

2006

The cytotoxic effect of several diorganotin(IV) and triorganotin(IV)-meso-tetra(4-sulfonatophenyl)porphine derivatives was tested and only the (Bu(2)Sn)(2)TPPS and the (Bu(3)Sn)(4)TPPS showed cytotoxicity on A375 human melanoma cells. To examine the pathway of (Bu(2)Sn)(2)TPPS or (Bu(3)Sn)(4)TPPS induced A375 cell death, DNA fragmentation analysis, Annexin V binding and PI uptake as well as caspases activation analysis by Western blot were carried out. A375 cells treated exhibited several typical characteristics of apoptosis. Both the (Bu(2)Sn)(2)TPPS and the (Bu(3)Sn)(4)TPPS compounds activate caspase-8 and caspase-9 leading to caspase-3 activation. Thus, we propose that these two porphiri…

Cancer ResearchPorphyrinsCytotoxicityMelamoma cellAntineoplastic AgentsApoptosisDNA FragmentationWestern blotAnnexinCell Line TumorOrganotin CompoundsPimedicineHumansCytotoxic T cellCytotoxicityMelanomaCaspasebiologymedicine.diagnostic_testTriorganotin(IV)ApoptosiFlow CytometryMolecular biologyMicroscopy FluorescenceOncologyApoptosisCaspasesbiology.proteinDNA fragmentationDiorganotin(IV)
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In BCR-ABL-positive cells, STAT-5 tyrosine-phosphorylation integrates signals induced by imatinib mesylate and Ara-C.

2003

In BCR-ABL-positive cells, the transcription factor STAT-5 is constitutively activated by tyrosine phosphorylation. STAT-5 activation results in upregulation of bcl-X(L) and increased resistance to induction of apoptosis. Here, we investigated the effects of imatinib mesylate and cytosine arabinoside (Ara-C) on STAT-5 tyrosine-phosphorylation, cellular proliferation and induction of apoptosis in cell lines and primary hematopoietic cells. Imatinib mesylate treatment strongly suppressed STAT-5 tyrosine-phosphorylation in K562 and primary CML blasts. In contrast to JAK-2 and PI-3-kinase inhibition, exposure of K562 cells to imatinib mesylate resulted in obvious suppression of proliferation. R…

Cancer ResearchProgrammed cell deathBlotting WesternFusion Proteins bcr-ablDown-RegulationAntineoplastic AgentsApoptosisBiologyPiperazineschemistry.chemical_compoundDownregulation and upregulationhemic and lymphatic diseasesLeukemia Myelogenous Chronic BCR-ABL PositivemedicineIn Situ Nick-End LabelingSTAT5 Transcription FactorHumansEnzyme InhibitorsPhosphorylationCell growthCytarabineImatinibTyrosine phosphorylationDrug SynergismHematologyDNAU937 CellsProtein-Tyrosine KinasesMilk ProteinsPrecipitin TestsDNA-Binding ProteinsImatinib mesylatePyrimidinesOncologychemistryApoptosisCaspasesBenzamidesCancer researchImatinib MesylateTrans-ActivatorsTyrosinePoly(ADP-ribose) PolymerasesK562 CellsCell Divisionmedicine.drugK562 cellsSignal TransductionLeukemia
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Hsp72 controls bortezomib-induced HepG2 cell death via interaction with pro-apoptotic factors.

2007

The proteasome inhibitor bortezomib is an efficacious inducer of apoptosis in the hepatoma HepG2 cell line. This study shows that bortezomib increased in these cells the level of the survival factor Hsp72 in a time- and dose-dependent manner. In a first phase of treatment, Hsp72 rapidly increased so that at 24 h of incubation with 50 nM bortezomib its level was approximately five-fold higher than the control. In this phase Hsp72 seemed to play a role in preventing HepG2 cell death, since it interacted with and sequestered the pro-apoptotic factors p53, AIF, Bax and Apaf-1. During a second day of treatment, although the nuclear levels of Hsp72, p53 and AIF increased, the interaction of Hsp72…

Cancer ResearchProgrammed cell deathCarcinoma HepatocellularTime FactorsCellBlotting WesternApoptosisHSP72 Heat-Shock ProteinsAmino Acid Chloromethyl KetonesBortezomibCell Line TumormedicineHumansImmunoprecipitationProtease Inhibitorscardiovascular diseasesCaspasebcl-2-Associated X ProteinOncogenebiologyBortezomibReverse Transcriptase Polymerase Chain ReactionLiver NeoplasmsApoptosis Inducing Factorproteasome inhibitor hepatocarcinoma apoptosisGeneral MedicineCell cycleBoronic Acidsmedicine.anatomical_structureApoptotic Protease-Activating Factor 1OncologyApoptosisPyrazinesProteasome inhibitorCancer researchbiology.proteinTumor Suppressor Protein p53Apoptosis Regulatory Proteinsmedicine.drugProtein Binding
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Sodium phenylbutyrate induces apoptosis in human retinoblastoma Y79 cells: The effect of combined treatment with the topoisomerase I-inhibitor topote…

2001

Our results demonstrate that sodium phenylbutyrate, a compound with a low degree of toxicity, exerted a cytotoxic effect on human retinoblastoma Y79 cells in a time- and dose-dependent manner. Treatment of Y79 cells for 72 h with phenylbutyrate reduced cell viability by 63% at 2 mM and 90% at 4 mM. Cell death caused by phenylbutyrate exhibited the typical features of apoptosis, as shown by light and fluorescent microscopy. Western blot analysis demonstrated that exposure of Y79 cells to phenylbutyrate decreased the level of the antiapoptotic factor Bcl-2 and induced the activation of caspase-3, a key enzyme in the execution phase of apoptosis. Moreover, treatment with phenylbutyrate markedl…

Cancer ResearchProgrammed cell deathCell SurvivalBlotting WesternApoptosisPhenylbutyrateHistonesSettore BIO/10 - BiochimicamedicineTumor Cells CulturedHumansretinoblastoma apoptosis sodium phenylbutirateViability assayEnzyme InhibitorsbiologyCaspase 3TopoisomeraseRetinoblastomaSodium phenylbutyrateAcetylationDrug SynergismCell cyclePhenylbutyrateseye diseasesEnzyme ActivationOncologyProto-Oncogene Proteins c-bcl-2ApoptosisCaspasesbiology.proteinCancer researchTopotecanDrug Therapy CombinationTopoisomerase I InhibitorsTumor Suppressor Protein p53Topotecanmedicine.drug
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