Search results for "uci"

showing 10 items of 5317 documents

A compound-based proteomic approach discloses 15-ketoatractyligenin methyl ester as a new PPARγ partial agonist with anti-proliferative ability

2017

AbstractProteomics based approaches are emerging as useful tools to identify the targets of bioactive compounds and elucidate their molecular mechanisms of action. Here, we applied a chemical proteomic strategy to identify the peroxisome proliferator-activated receptor γ (PPARγ) as a molecular target of the pro-apoptotic agent 15-ketoatractyligenin methyl ester (compound 1). We demonstrated that compound 1 interacts with PPARγ, forms a covalent bond with the thiol group of C285 and occupies the sub-pocket between helix H3 and the β-sheet of the ligand-binding domain (LBD) of the receptor by Surface Plasmon Resonance (SPR), mass spectrometry-based studies and docking experiments. 1 displayed…

Transcriptional Activation0301 basic medicinenatural productTime FactorsPeroxisome proliferator-activated receptorApoptosisLigandsPartial agonistArticleRosiglitazonePPAR_gammaJurkat Cells03 medical and health sciencesTransactivation0302 clinical medicineproteomicsHumansBinding siteReceptorMode of actionPI3K/AKT/mTOR pathwayCell Proliferationchemistry.chemical_classificationBinding SitesMultidisciplinaryProtein StabilityProtein Proliferator-Activated-Receptor PPARs Ligand-Binding Domain Chemical Proteomics Accurate Docking Pi3k/Akt Pathway Drug Discovery Anticancer compoundsReproducibility of ResultsEstersSurface Plasmon ResonanceMolecular Docking SimulationPPAR gammaKineticsHEK293 Cells030104 developmental biologychemistryBiochemistryDocking (molecular)030220 oncology & carcinogenesisThermodynamicsThiazolidinedionesproteomics PPAR_gamma natural productDiterpenes KauraneHT29 CellsScientific Reports
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Dihydroquercetin (DHQ) induced HO-1 and NQO1 expression against oxidative stress through the Nrf2-dependent antioxidant pathway.

2013

Dihydroquercetin (DHQ) is a well-known antioxidant agent. In the present investigation, we reported for the first time that DHQ stimulates the expression of phase II detoxifying enzymes through the Nrf2-dependent signaling pathway. The IC50 values of DHQ for reduction of 2,2-diphenyl-1-picrylhydrazol (DPPH), reducing power assay, lipid peroxidation assay, and xanthine oxidase inhibition were 5.96, 4.31, 2.03, and 13.24 μM, respectively. DHQ possessed considerable protective activity from oxidative DNA damage. A luciferase reporter assay also demonstrated that DHQ-activated signaling resulted in the increased transcriptional activity of Nrf2 through binding to the ARE (antioxidant response e…

Transcriptional ActivationAntioxidantNF-E2-Related Factor 2medicine.medical_treatmentLarixmedicine.disease_causeAntioxidantsLipid peroxidationchemistry.chemical_compoundmedicineNAD(P)H Dehydrogenase (Quinone)HumansAntioxidant Response ElementsLuciferaseXanthine oxidaseProtein kinase BChemistryPlant ExtractsGeneral ChemistryHep G2 CellsMolecular biologyAntioxidant Response ElementsUp-RegulationOxidative StressBiochemistryQuercetinNAD+ kinaseGeneral Agricultural and Biological SciencesOxidative stressHeme Oxygenase-1Signal TransductionJournal of agricultural and food chemistry
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Recruitment of HIF-1α and HIF-2α to common target genes is differentially regulated in neuroblastoma: HIF-2α promotes an aggressive phenotype

2006

In neuroblastoma specimens, HIF-2alpha but not HIF-1alpha is strongly expressed in well-vascularized areas. In vitro, HIF-2alpha protein was stabilized at 5% O2 (resembling end capillary oxygen conditions) and, in contrast to the low HIF-1alpha activity at this oxygen level, actively transcribed genes like VEGF. Under hypoxia (1% O2), HIF-1alpha was transiently stabilized and primarily mediated acute responses, whereas HIF-2alpha protein gradually accumulated and governed prolonged hypoxic gene activation. Knockdown of HIF-2alpha reduced growth of neuroblastoma tumors in athymic mice. Furthermore, high HIF-2alpha protein levels were correlated with advanced clinical stage and high VEGF expr…

Transcriptional ActivationCancer ResearchProcollagen-Proline DioxygenaseAggressive phenotypeCELLCYCLEBiologyMiceNeuroblastomaNeuroblastomaBasic Helix-Loop-Helix Transcription FactorsTumor Cells CulturedmedicineAnimalsHumansRNA MessengerChildHypoxiaGeneOligonucleotide Array Sequence AnalysisRegulation of gene expressionGene knockdownGene Expression ProfilingCell BiologyCell cycleHypoxia (medical)Hypoxia-Inducible Factor 1 alpha Subunitmedicine.diseaseIn vitroGene Expression Regulation NeoplasticOxygenPhenotypeOncologyImmunologyCancer researchFemalemedicine.symptomNeoplasm TransplantationCancer Cell
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Mechanism of leptin expression in breast cancer cells: role of hypoxia-inducible factor-1α

2007

We reported previously that the obesity hormone leptin is overexpressed in breast cancer biopsies. Here, we investigated molecular mechanisms involved in this process, focusing on conditions that are associated with obesity, that is, hyperinsulinemia and induction of hypoxia. By using quantitative real-time PCR, immunofluorescent detection of proteins and enzyme-linked immunosorbent assays, we found that treatment of MCF-7 breast cancer cells with high doses of insulin or the hypoxia-mimetic agent CoCl2, or culturing the cells under hypoxic conditions significantly increased the expression of leptin mRNA and protein. Notably, the greatest leptin mRNA and protein expression were observed und…

Transcriptional ActivationCancer Researchmedicine.medical_specialtyActive Transport Cell NucleusBreast NeoplasmsBiologymedicine.disease_causeleptinbreast cancerInternal medicineCoactivatorGene expressionTumor Cells CulturedGeneticsmedicineHumansInsulinHIFp300-CBP Transcription FactorsPromoter Regions GeneticMolecular BiologyCell NucleusRegulation of gene expressionBinding SitesLeptin receptorLeptinPromoterCobaltHypoxia-Inducible Factor 1 alpha SubunitCell HypoxiaGene Expression Regulation NeoplasticEndocrinologyhyperinsulinemiaCarcinogenesisChromatin immunoprecipitationhormones hormone substitutes and hormone antagonistsProtein BindingOncogene
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Reduction of Cardiac Fibrosis by Interference With YAP-Dependent Transactivation

2022

Background: Conversion of cardiac stromal cells into myofibroblasts is typically associated with hypoxia conditions, metabolic insults, and/or inflammation, all of which are predisposing factors to cardiac fibrosis and heart failure. We hypothesized that this conversion could be also mediated by response of these cells to mechanical cues through activation of the Hippo transcriptional pathway. The objective of the present study was to assess the role of cellular/nuclear straining forces acting in myofibroblast differentiation of cardiac stromal cells under the control of YAP (yes-associated protein) transcription factor and to validate this finding using a pharmacological agent that interf…

Transcriptional ActivationPhysiologyfibrosismyofibroblastsVerteporfinheart failureYAP-Signaling ProteinsSettore MED/11 - Malattie dell'Apparato CardiovascolareSettore MED/23 - Chirurgia Cardiacafibrosis; heart failure; myofibroblasts; stromal cell; transcription factorsstromal cellPhosphoproteinscell mechanics; fibrosis; heart failure; myofibroblasts; stromal cell; YAP transcription factor;MiceYAP transcription factorcell mechanicsSettore CHIM/09 - Farmaceutico Tecnologico Applicativotranscription factorsTrans-ActivatorsAnimalsHumansCardiology and Cardiovascular MedicineAdaptor Proteins Signal Transducing
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Role of reactive oxygen species in the regulation of HIF-1 by prolyl hydroxylase 2 under mild hypoxia

2012

The function and survival of eukaryotic cells depends on a constant and sufficient oxygen supply. Cells recognize and respond to hypoxia by accumulation of the transcription factor hypoxia-inducible factor 1 (HIF-1), composed of an oxygen-sensitive HIF-1α and a constitutive HIF-1β subunit. Besides physiology, HIF-1 induction is involved in major pathological processes such as cardiovascular disease, inflammation and cancer, which are associated with the formation of reactive oxygen species (ROS). ROS have been reported to affect HIF-1 activity but the role for ROS in regulating HIF-1 has not been definitely settled. In order to shed light on the redox-regulation of HIF-1 by ROS, we studied …

Transcriptional ActivationProcollagen-Proline DioxygenaseMedizinBiologyTransfectionBiochemistryHypoxia-Inducible Factor-Proline DioxygenasesTransactivationCell Line TumormedicineHumansRNA Small InterferingTranscription factorchemistry.chemical_classificationRegulation of gene expressionReactive oxygen speciesGene knockdownGeneral MedicineTransfectionHydrogen PeroxideHypoxia (medical)Cell HypoxiaCell biologyHypoxia-inducible factorschemistryBiochemistryHypoxia-Inducible Factor 1medicine.symptomReactive Oxygen SpeciesOxidation-Reduction
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Role of hepatocyte nuclear factor 3γ in the expression of human CYP2C genes

2004

Hepatocyte nuclear factor 3 gamma (HNF-3 gamma) is an important transcription factor for the maintenance of specific liver functions. However, its relevance in the expression of human cytochrome P450 (CYP) genes has not yet been explored. Several HNF3 putative binding sites can be identified in human CYP2C 5'-flanking regions. Gene reporter experiments with proximal promoters revealed that HNF-3 gamma transactivated CYP2C8, CYP2C9, and CYP2C19 (25-, 4-, and 4-fold, respectively), but it did not transactivate CYP2C18. However, overexpression of HNF-3 gamma in hepatoma cells by means of a recombinant adenovirus induced CYP2C9, CYP2C18, and CYP2C19 mRNA (4.5-, 20-, and 50-fold, respectively) b…

Transcriptional ActivationRecombinant Fusion ProteinsGenetic VectorsBiophysicsBiologyHydroxamic AcidsTransfectionBiochemistryGene Expression Regulation EnzymologicAdenoviridaeCytochrome P-450 Enzyme SystemSp3 transcription factorCell Line TumormedicineHumansRNA MessengerEnzyme InhibitorsLuciferasesPromoter Regions GeneticMolecular BiologyTranscription factorBinding SitesNuclear ProteinsPromoterMolecular biologyDNA-Binding ProteinsHistone Deacetylase InhibitorsHepatocyte nuclear factorsTrichostatin AHepatocyte nuclear factor 4Hepatocyte nuclear factor 4 alphaHepatocytesFOXA2Transcription Initiation SiteHepatocyte Nuclear Factor 3-gammaHeLa CellsTranscription Factorsmedicine.drugArchives of Biochemistry and Biophysics
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Increased AICD generation does not result in increased nuclear translocation or activation of target gene transcription.

2008

A sequence of amyloid precursor protein (APP) cleavages culminates in the sequential release of the APP intracellular domain (AICD) and the amyloid beta peptide (Abeta) and/or p3 fragment. One of the environmental factors favouring the accumulation of AICD appears to be a rise in intracellular pH. Here we further identified the metabolism and subcellular localization of artificially expressed constructs under such conditions. We also co-examined the mechanistic lead up to the AICD accumulation and explored possible significances for its increased expression. We found that most of the AICD generated under pH neutralized conditions is likely cleaved from C83. While the AICD surplus was unable…

Transcriptional ActivationTranscription GeneticAmyloid betaActive Transport Cell NucleusCHO CellsModels BiologicalTransactivationAmyloid beta-Protein PrecursorCricetulusTranscription (biology)CricetinaeAmyloid precursor proteinAnimalsHumansLuciferaseCells CulturedRegulation of gene expressionCell NucleusbiologyCell BiologyHydrogen-Ion ConcentrationSubcellular localizationMolecular biologyCell biologyProtein Structure TertiaryCytosolbiology.proteinProtein Processing Post-TranslationalProtein BindingExperimental cell research
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Hypoxia-inducible factor 1Α may regulate the commitment of mesenchymal stromal cells toward angio-osteogenesis by mirna-675-5P

2017

Abstract Background aims During bone formation, angiogenesis and osteogenesis are regulated by hypoxia, which is able to induce blood vessel formation, as well as recruit and differentiate human mesenchymal stromal cells (hMSCs). The molecular mechanisms involved in HIF-1α response and hMSC differentiation during bone formation are still unclear. This study aimed to investigate the synergistic role of hypoxia and hypoxia-mimetic microRNA miR-675-5p in angiogenesis response and osteo-chondroblast commitment of hMSCs. Methods By using a suitable in vitro cell model of hMSCs (maintained in hypoxia or normoxia), the role of HIF-1α and miR-675-5p in angiogenesis and osteogenesis coupling was inv…

Transcriptional ActivationVascular Endothelial Growth Factor A0301 basic medicineCancer ResearchAngiogenesisCellular differentiationImmunologyNeovascularization PhysiologicBiology03 medical and health scienceschemistry.chemical_compoundOsteogenesisMiR-675-5pmedicineHumansImmunology and AllergyHypoxiaCells Culturedbeta CateninGenetics (clinical)TransplantationOsteoblastsMesenchymal stromal cellMesenchymal stem cellWnt signaling pathwayCell DifferentiationMesenchymal Stem CellsOsteoblastCell BiologyHypoxia-Inducible Factor 1 alpha SubunitCell HypoxiaUp-RegulationCell biologyVascular endothelial growth factorMicroRNAsVascular endothelial growth factor A030104 developmental biologymedicine.anatomical_structureGene Expression RegulationOncologyHypoxia-inducible factorschemistryRegenerative medicineImmunologyOsteoblast commitmentCytotherapy
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In vivo manipulation of Vgamma9Vdelta2 T cells with zoledronate and low-dose interleukin-2 for immunotherapy of advanced breast cancer patients.

2010

The potent anti-tumour activities of gamma delta T cells have prompted the development of protocols in which gamma delta-agonists are administered to cancer patients. Encouraging results from small Phase I trials have fuelled efforts to characterize more clearly the application of this approach to unmet clinical needs such as metastatic carcinoma. To examine this approach in breast cancer, a Phase I trial was conducted in which zoledronate, a V gamma 9V delta 2 T cell agonist, plus low-dose interleukin (IL)-2 were administered to 10 therapeutically terminal, advanced metastatic breast cancer patients. Treatment was well tolerated and promoted the effector maturation of V gamma 9V delta 2 T …

Translational Studiesmedicine.medical_treatmentLymphocyte ActivationZoledronic AcidMetastasisTNF-Related Apoptosis-Inducing LigandProstate cancerT-Lymphocyte SubsetsImmunology and AllergyMedicineDiphosphonatesRemission InductionEsterasesImidazolesReceptors Antigen T-Cell gamma-deltaMiddle AgedMetastatic breast cancerTreatment Outcomemedicine.anatomical_structureDisease ProgressionCytokinesFemaleImmunotherapyBreast diseaseChemokinesT cellImmunologyBreast NeoplasmsInterferon-gammaHemiterpenesOrganophosphorus CompoundsBreast cancerAdjuvants ImmunologicVgamma9Vdelta2 T cells Zoledronate interleukin-2advanced breast cancer patientsHumansLymphocyte CountAgedCell ProliferationSalvage Therapybusiness.industryLysineMucin-1CancerImmunotherapymedicine.diseaseTumor Necrosis Factor Receptor Superfamily Member 7ImmunologyInterleukin-2Leukocyte Common Antigensbusiness
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