Search results for "proteasome"

showing 10 items of 145 documents

Exploring the non-covalent ligand-binding mechanism on immunoproteasome by enhanced Molecular Dynamics

2021

Selective inhibition of immunoproteasome is a valuable strategy to treat autoimmune and inflammatory diseases, and hematologic malignancies. In particular, non-covalent inhibition is strongly desirable because it is free of the drawbacks and side effects associated with covalent inhibition. Recently, a new series of amide derivatives with Ki values in the low/submicromolar ranges toward the β1i subunit have been identified as non-covalent inhibitors 1 . We investigated the binding mechanism of the most potent and selective inhibitor (1) to elucidate the steps from the ligand entrance into the binding pocket to the ligand-induced conformational changes. We carried out a total of 400ns of MD-…

Immunoproteasome non-covalent inhibitors enhanced molecular dynamics
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Role of NF-kappaB in immune and inflammatory responses in the gut.

1998

NF-kappaB is a pleiotropic transcription factor with key functions in the intestinal immune system. NF-kappaB family members control transcriptional activity of various promoters of proinflammatory cytokines, cell surface receptors, transcription factors, and adhesion molecules that are involved in intestinal inflammation. The perpetuated activation of NF-kappaB in patients with active inflammatory bowel disease suggests that regulation of NF-kappaB activity is a very attractive target for therapeutic intervention. Such strategies include antioxidants, proteasome inhibitors, inhibition of NF-kappaB by adenoviral I kappaB alpha expression vectors, and antisense DNA targeting of NF-kappaB. Th…

InflammationMice KnockoutGastroenterologyNF-kappa BInflammationPromoterReviewBiologyNFKB1Proinflammatory cytokineIκBαIntestinal DiseasesMiceImmune systemProteasomeImmunologymedicineAnimalsHumansmedicine.symptomTranscription factorSignal TransductionTranscription FactorsGut
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Bortezomib potentiates the antitumor effect of tributyltin(IV) ferulate in colon cancer cells exacerbating ER stress and promoting apoptosis

2022

Organotin(IV) complexes represent promising drugs in medicinal chemistry for their potential use in cancer therapy. We recently reported synthesis and characterization of a new organotin(IV) complex of ferulic acid (FA), tributyltin(IV) ferulate (TBT-F), showing its antitumor action in colon cancer cells. Here we provide evidence that the efficacy of this compound is strongly potentiated by the proteasome inhibitor bortezomib (BTZ). While low concentrations of tributyltin(IV) ferulate alone promoted autophagy without reducing cell viability, combination of the two compounds markedly affected colon cancer cell viability, cell morphology and exasperated endoplasmic reticulum (ER) stress, as r…

Inorganic ChemistryMaterials ChemistryApoptosisProteasome inhibitorFerulic acidPhysical and Theoretical ChemistryER stressOrganotin(IV) complexes
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Yeast Dun1 Kinase Regulates Ribonucleotide Reductase Inhibitor Sml1 in Response to Iron Deficiency

2014

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox-active cofactor in many biological processes, including DNA replication and repair. Eukaryotic ribonucleotide reductases (RNRs) are Fe-dependent enzymes that catalyze deoxyribonucleoside diphosphate (dNDP) synthesis. We show here that the levels of the Sml1 protein, a yeast RNR large-subunit inhibitor, specifically decrease in response to both nutritional and genetic Fe deficiencies in a Dun1-dependent but Mec1/Rad53- and Aft1-independent manner. The decline of Sml1 protein levels upon Fe starvation depends on Dun1 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar pr…

Iron-Sulfur ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleotideIronDeoxyribonucleotidesGenes FungalSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeRibonucleotide reductase inhibitorProtein Serine-Threonine KinasesBiologyProtein degradationchemistry.chemical_compoundTristetraprolinRibonucleotide ReductasesAspartic Acid EndopeptidasesPhosphorylationMolecular BiologyCheckpoint Kinase 2Binding SitesKinaseIntracellular Signaling Peptides and ProteinsArticlesCell Biologybiology.organism_classificationDNA-Binding ProteinsDeoxyribonucleosideCheckpoint Kinase 2chemistryBiochemistryProteolysisGene DeletionTranscription FactorsMolecular and Cellular Biology
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Novel isatin-derived molecules activate p53 via interference with Mdm2 to promote apoptosis

2018

International audience; The p53 protein is a key tumor suppressor in mammals. In response to various forms of genotoxic stress p53 stimulates expression of genes whose products induce cell cycle arrest and/or apoptosis. An E3-ubiquitin ligase, Mdm2 (mouse-double-minute 2) and its human ortholog Hdm2, physically interact with the amino-terminus of p53 to mediate its ubiquitin-mediated degradation via the proteasome. Thus, pharmacological inhibition of the p53-Mdm2 interaction leads to overall stabilization of p53 and stimulation of its anti-tumorigenic activity. In this study we characterize the biological effects of a novel class of non-genotoxic isatin Schiff and Mannich base derivatives (…

Isatin0301 basic medicineProgrammed cell deathCell cycle checkpointAntineoplastic AgentsApoptosis[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyPiperazinesHistonesMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicineNutlinCell Line TumorProto-Oncogene ProteinsAnimalsHumansMolecular Biologychemistry.chemical_classificationDNA ligaseIsatinImidazolesISMBDsProto-Oncogene Proteins c-mdm2Cell BiologyNutlinp53-activating moleculesCell biology030104 developmental biologychemistryProteasomeApoptosis030220 oncology & carcinogenesisbiology.proteinMdm2PumaTumor Suppressor Protein p53Apoptosis Regulatory Proteinsautomated microscopy system OperettaResearch PaperDevelopmental BiologyCell Cycle
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Identification of HSP90 as a new GABARAPL1 (GEC1)-interacting protein

2011

GABARAPL1 belongs to the small family of GABARAP proteins (including GABARAP, GABARAPL1 and GABARAPL2/GATE-16), one of the two subfamilies of the yeast Atg8 orthologue. GABARAPL1 is involved in the intracellular transport of receptors, via an interaction with tubulin and GABA(A) or kappa opioid receptors, and also participates in autophagy and cell proliferation. In the present study, we identify the HSP90 protein as a novel interaction partner for GABARAPL1 using GST pull-down, mass spectrometry and coimmunoprecipitation experiments. GABARAPL1 and HSP90 partially colocalize in MCF-7 breast cancer cells overexpressed Dsred-GABARAPL1 and in rat brain. Moreover, treatment of MCF-7 cells overe…

LeupeptinsLactams MacrocyclicGABARAPATG8Blotting WesternLactacystinCysteine Proteinase InhibitorsBiologyBiochemistryMass SpectrometryCell Linechemistry.chemical_compoundCell Line TumorMG132BenzoquinonesAnimalsHumansImmunoprecipitationHSP90 Heat-Shock ProteinsReceptorAdaptor Proteins Signal TransducingMicroscopy ConfocalHEK 293 cellsGeneral MedicineHsp90RatsBiochemistrychemistryProteasomebiology.proteinMicrotubule-Associated ProteinsBiochimie
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HSP27 controls GATA-1 protein level during erythroid cell differentiation.

2010

AbstractHeat shock protein 27 (HSP27) is a chaperone whose cellular expression increases in response to various stresses and protects the cell either by inhibiting apoptotic cell death or by promoting the ubiquitination and proteasomal degradation of specific proteins. Here, we show that globin transcription factor 1 (GATA-1) is a client protein of HSP27. In 2 models of erythroid differentiation; that is, in the human erythroleukemia cell line, K562 induced to differentiate into erythroid cells on hemin exposure and CD34+ human cells ex vivo driven to erythroid differentiation in liquid culture, depletion of HSP27 provokes an accumulation of GATA-1 and impairs terminal maturation. More spec…

LeupeptinsPyridines[SDV]Life Sciences [q-bio]Cellular differentiationCellHSP27 Heat-Shock ProteinsAntigens CD34Biochemistryp38 Mitogen-Activated Protein Kinases0302 clinical medicineTransforming Growth Factor betahemic and lymphatic diseasesChlorocebus aethiopsGATA1 Transcription FactorPhosphorylationComputingMilieux_MISCELLANEOUSCells CulturedHeat-Shock Proteins0303 health sciencesbiologyImidazolesCell DifferentiationHematology[SDV] Life Sciences [q-bio]medicine.anatomical_structure030220 oncology & carcinogenesisembryonic structuresCOS CellsRNA InterferenceSignal transductionProteasome InhibitorsProtein BindingProteasome Endopeptidase ComplexImmunologyImmunoblotting03 medical and health sciencesHsp27Erythroid CellsHeat shock proteinmedicineAnimalsHumansTranscription factor030304 developmental biologyCell NucleusInterleukin-6UbiquitinationCell BiologyTransforming growth factor betaMolecular biologyChaperone (protein)biology.proteinK562 CellsHeLa CellsMolecular ChaperonesBlood
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Neuronal activity triggers uptake of hematopoietic extracellular vesicles in vivo

2019

Communication with the hematopoietic system is a vital component of regulating brain function in health and disease. Traditionally, the major routes considered for this neuroimmune communication are by individual molecules such as cytokines carried by blood, by neural transmission, or, in more severe pathologies, by the entry of peripheral immune cells into the brain. In addition, functional mRNA from peripheral blood can be directly transferred to neurons via extracellular vesicles (EVs), but the parameters that determine their uptake are unknown. Using varied animal models that stimulate neuronal activity by peripheral inflammation, optogenetics, and selective proteasome inhibition of dop…

LipopolysaccharidesMaleGene ExpressionStimulationHippocampusBiochemistryStereotaxic Techniques0302 clinical medicineShort ReportsAnimal CellsMedicine and Health SciencesPremovement neuronal activityBiology (General)Routes of AdministrationNeurons0303 health sciencesBrain MappingKainic AcidBrainAnimal ModelsPeripheralCell biologyHaematopoiesisBioassays and Physiological AnalysisExperimental Organism SystemsHippocampus ; Yellow flourescent protein ; Intravenous injections ; Marker genes ; Gene expression ; Neurons ; Microglial cells ; OptogeneticsFemaleCellular TypesSignal TransductionProteasome Endopeptidase ComplexQH301-705.5Yellow Fluorescent ProteinMice TransgenicGlial CellsMouse ModelsStimulus (physiology)BiologyResearch and Analysis Methods03 medical and health sciencesExtracellular VesiclesImmune systemModel OrganismsIn vivoIntravenous InjectionsGeneticsAnimalsddc:610Molecular Biology TechniquesMolecular BiologyMicroglial Cells030304 developmental biologyInflammationPharmacologyMessenger RNABlood CellsUbiquitinDopaminergic NeuronsBiology and Life SciencesProteinsMarker GenesCell BiologyNeurophysiological AnalysisOptogeneticsLuminescent ProteinsCellular NeuroscienceAnimal Studies030217 neurology & neurosurgeryNeuroscience
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Novel combination of celecoxib and proteasome inhibitor MG132 provides synergistic antiproliferative and proapoptotic effects in human liver tumor ce…

2010

Molecular targeted therapy has shown promise as a treatment for advanced hepatocellular carcinoma (HCC). Celecoxib (Celebrex®) exhibits antitumor effects in human HCC cells, and its mechanism of action is mediated either by its ability to inhibit cyclooxygenase 2 (COX-2) or by a number of various other COX-2 independent effects. Proteasome inhibitors (PIs) can exert cell growth inhibitory and apoptotic effects in different tumor cell types, including HCC cells. The present study examined the interaction between celecoxib and the PI MG132 in two human liver tumor cell lines HepG2 and HA22T/VGH. Our data showed that each inhibitor reduced proliferation and induced apoptosis in a dose-dependen…

MG132TRB3Programmed cell deathLeupeptinsBlotting WesternApoptosisUPRPharmacologyCysteine Proteinase Inhibitorschemistry.chemical_compoundMG132medicineHumansViability assayHCCMolecular BiologyCell ProliferationSettore MED/12 - GastroenterologiaGene knockdownSulfonamidesbiologyCyclooxygenase 2 InhibitorsCell growthReverse Transcriptase Polymerase Chain ReactionDrug SynergismCell BiologyHep G2 CellsCOX-2ER stress responseFlow CytometryapoptosiproteasomechemistryApoptosisCelecoxibSettore BIO/14 - Farmacologiabiology.proteinProteasome inhibitorPyrazolesCyclooxygenaseDevelopmental Biologymedicine.drug
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Antigen-processing machinery breakdown and tumor growth.

2000

Defects in the major histocompatibility complex (MHC) class I antigen-processing machinery (APM) have been described in tumors of different histology. Murine data suggest that defects in the MHC class II APM might also be associated with malignant transformation of human cells. This article describes the pathophysiology of the MHC class I and II APM, reviews APM abnormalities in tumor cells and discusses their role in the escape of tumor cells from in vitro recognition by T cells.

MHC class IIAntigen PresentationProteasome Endopeptidase ComplexbiologyAntigen processingImmunologyAntigen presentationHistocompatibility Antigens Class IHistocompatibility Antigens Class IIATP-binding cassette transporterMajor histocompatibility complexIn vitroMalignant transformationCysteine EndopeptidasesATP Binding Cassette Transporter Subfamily B Member 3Multienzyme ComplexesNeoplasmsMHC class IImmunologybiology.proteinCancer researchAnimalsHumansATP-Binding Cassette TransportersImmunology today
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