Search results for "Proteasome inhibitors"

showing 10 items of 27 documents

Bortezomib induces in HepG2 cells IkappaBalpha degradation mediated by caspase-8.

2006

The present paper demonstrates that the proteasome inhibitor bortezomib, which behaves as an apoptotic agent in hepatoma HepG2 cells, caused in these cells a decrease in IkappaBalpha level and a consequent increase in NF- kappaB activity. The effect already appeared at 4 h of treatment and preceded the onset of apoptosis which was observed at 24 h. Our results demonstrate that bortezomib-induced IkappaBalpha degradation occurred in conjunction with the activation of caspase-8; moreover, the decrease in IkappaBalpha level was prevented in a dose-dependent manner by the addition of z-IETD, a specific inhibitor of caspase-8. Bortezomib caused the same effects in non-tumor Chang liver cells, wh…

Clinical BiochemistryBiologyCaspase 8Cell LineBortezomibchemistry.chemical_compoundNF-KappaB Inhibitor alphaCell Line Tumormedicinehepatoblastoma proteasome inhibitors NF-kB apoptosisHumansMolecular BiologyCaspase 8BortezomibLiver NeoplasmsNF-kappa BNF-κBCalpainCell BiologyGeneral MedicineMolecular biologyBoronic AcidsIκBαchemistryLiverApoptosisCell culturePyrazinesCancer researchProteasome inhibitorbiology.proteinI-kappa B Proteinsmedicine.drug
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Selected cytotoxic gold compounds cause significant inhibition of 20S proteasome catalytic activities

2014

Abstract Six structurally diverse cytotoxic gold compounds are reported to cause profound and differential inhibition of the three main catalytic activities of purified 20S proteasome whilst auranofin , an established gold(I) drug in clinical use, is nearly ineffective. In particular, the gold(I) complex [( pbiH ) Au ( PPh 3 )] PF 6 , turns out to be the most potent inhibitor of all three enzyme activities with sub-micromolar IC 50 values. The present results further support the view that proteasome inhibition may play a major – yet not exclusive – role in the cytotoxic actions of gold based anticancer agents.

DrugProteasome Endopeptidase ComplexAuranofinmedia_common.quotation_subjectAntineoplastic AgentsPharmacologyBiochemistry20s proteasomeProteasome Gold compounds Anticancer drugs Enzyme inhibitionCatalysisInorganic ChemistryInhibitory Concentration 50Structure-Activity RelationshipGold CompoundsCoordination ComplexesAuranofinmedicineHumansCytotoxic T cellmedia_commonchemistry.chemical_classificationCytotoxinsChemistryEnzymeProteasomeBiochemistryBiocatalysisOrganogold CompoundsProteasome Inhibitorsmedicine.drug
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Targeting apoptosis in solid tumors: the role of bortezomib from preclinical to clinical evidence.

2007

The ubiquitin-proteasome pathway is the main proteolytic system present in the nucleus and cytoplasm of all eukaryotic cells. Apoptosis activation induced by ubiquitin-proteasome pathway inhibition makes the proteasome a new target of anticancer therapy. Bortezomib is the first proteasome inhibitor to be approved by the US FDA; in 2003 as a third line and in 2005 as a second line therapy for the treatment of multiple myeloma only. This review focuses on the use of bortezomib, not only in its therapeutic role but also, more specifically, in its biologic role and discusses the most recent applications of the drug in solid tumors, both at a preclinical and clinical level.

Drugubiquitin-proteasome pathway proteasome inhibitorsSettore MED/06 - Oncologia Medicamedia_common.quotation_subjectClinical BiochemistryDrug Evaluation PreclinicalAntineoplastic AgentsApoptosisPharmacologyBortezomibNeoplasmsDrug DiscoverymedicineAnimalsHumansMultiple myelomamedia_commonPharmacologyClinical Trials as Topicbusiness.industryBortezomibmedicine.diseaseBoronic AcidsProteasomeClinical evidenceCytoplasmApoptosisPyrazinesProteasome inhibitorMolecular Medicinebusinessmedicine.drug
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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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Investigating the Vascular Toxicity Outcomes of the Irreversible Proteasome Inhibitor Carfilzomib

2020

Background: Carfilzomib&rsquo

Male0301 basic medicinevasculature030204 cardiovascular system & hematologyPharmacologyDinoprostEndoplasmic Reticulumlcsh:ChemistryMicechemistry.chemical_compound0302 clinical medicineAMP-Activated Protein Kinase Kinasesvascular smooth muscle cellsCytotoxicitylcsh:QH301-705.5endoplasmatic-reticulum stressSpectroscopychemistry.chemical_classificationcarfilzomibCobaltGeneral MedicineMetforminComputer Science ApplicationsRespiratory burstMetforminDrug Therapy CombinationGlycolysisOligopeptidesProteasome Inhibitorsmedicine.drugProteasome Endopeptidase ComplexautophagyCell SurvivalMyocytes Smooth MuscleAntineoplastic AgentsNitric OxideArticleCatalysisInorganic Chemistry03 medical and health sciencesmedicineAnimalsHumansPhysical and Theoretical ChemistryMolecular BiologyReactive oxygen speciesbusiness.industryOrganic ChemistryAutophagyCarfilzomibActinsVasoprotectiveMice Inbred C57BLGlucose030104 developmental biologychemistrylcsh:Biology (General)lcsh:QD1-999Proteasome inhibitorTumor Suppressor Protein p53Reactive Oxygen SpeciesbusinessProtein KinasesInternational Journal of Molecular Sciences
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Morphological Changes within the Rat Lateral Ventricle after the Administration of Proteasome Inhibitors.

2015

The broad variety of substances that inhibit the action of the ubiquitin-proteasome system (UPS)—known as proteasome inhibitors—have been used extensively in previous studies, and they are currently frequently proposed as a novel form of cancer treatment and as a protective factor in intracerebral hemorrhage treatment. The experimental data on the safest route of proteasome inhibitor administration, their associated side effects, and the possible ways of minimizing these effects have recently become a very important topic. The aim of our present study was to determine the effects of administering of MG-132, lactacystin and epoxomicin, compounds belonging to three different classes of protea…

MalePathologymedicine.medical_specialtyProteasome Endopeptidase ComplexEpendymal CellRosette FormationLactacystinlcsh:MedicineBiologyGlial scarchemistry.chemical_compoundLateral ventriclesEpoxomicinEpendymaLateral VentriclesmedicineAnimalsRats Wistarlcsh:ScienceMultidisciplinaryUbiquitinlcsh:RRatsmedicine.anatomical_structureProteasomechemistryGlioma SubependymalProteasome inhibitorlcsh:QAtrophyEpendymaProteasome Inhibitorsmedicine.drugResearch ArticlePloS one
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Post-transplant consolidation based on combination of lenalidomide and proteasome inhibitors in multiple myeloma

2021

Multiple myeloma (MM) is a hematological malignancy due to uncontrolled proliferation of neoplastic plasma cells in the bone marrow, associated to chromosomal instability and cytogenetic abnormalities, which could have an impact on prognosis. Response to treatment and survival of newly diagnosed myeloma patients is heterogeneous, with median overall survival ranging from two to more than ten years, due to clinical and biological factors. To warrant long-term control of disease, several strategies have been proposed in the last years, including short-term high-dose of treatment, named as consolidation, before maintenance. This review will discuss the role of consolidation in the current myel…

Oncologymedicine.medical_specialtyTime FactorsDisease030204 cardiovascular system & hematologyRisk Assessment03 medical and health sciences0302 clinical medicineRisk FactorsInternal medicineChromosome instabilityAntineoplastic Combined Chemotherapy ProtocolsmedicineHumansImmunologic FactorsLenalidomideMultiple myelomaLenalidomide030219 obstetrics & reproductive medicinebusiness.industryGeneral Medicinemedicine.diseaseResponse to treatmentProgression-Free SurvivalPost transplantConsolidation Chemotherapymedicine.anatomical_structureProteasomeBone marrowMultiple MyelomabusinessProteasome InhibitorsStem Cell Transplantationmedicine.drugPanminerva Medica
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MYC and EGR1 synergize to trigger tumor cell death by controlling NOXA and BIM transcription upon treatment with the proteasome inhibitor bortezomib

2014

The c-MYC (MYC afterward) oncogene is well known for driving numerous oncogenic programs. However, MYC can also induce apoptosis and this function of MYC warrants further clarification. We report here that a clinically relevant proteasome inhibitor significantly increases MYC protein levels and that endogenous MYC is necessary for the induction of apoptosis. This kind of MYC-induced cell death is mediated by enhanced expression of the pro-apoptotic BCL2 family members NOXA and BIM. Quantitative promoter-scanning chromatin immunoprecipitations (qChIP) further revealed binding of MYC to the promoters of NOXA and BIM upon proteasome inhibition, correlating with increased transcription. Both pr…

Programmed cell deathTranscription GeneticEGR1ApoptosisBiologyBortezomibProto-Oncogene Proteins c-mycMicehemic and lymphatic diseasesCell Line TumorProto-Oncogene ProteinsGeneticsmedicineAnimalsPromoter Regions GeneticTranscription factorCells CulturedEarly Growth Response Protein 1Zinc finger transcription factorBinding SitesOncogeneBcl-2-Like Protein 11Genes p16Gene regulation Chromatin and EpigeneticsMembrane ProteinsPromoterGenes p53Boronic AcidsChromatinddc:Gene Expression Regulation NeoplasticProto-Oncogene Proteins c-bcl-2PyrazinesCancer researchProteasome inhibitorApoptosis Regulatory ProteinsProteasome Inhibitorsmedicine.drug
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Features of TAP-independent MHC class I ligands revealed by quantitative mass spectrometry.

2008

TAP is responsible for transferring cytosolic peptides into the ER, where they can be loaded onto MHC molecules. Deletion of TAP results in a drastic reduction of MHC class I surface expression and alters the presented peptide pattern. This key molecule in antigen processing is tackled by several viruses and lost in some tumors, rendering the altered cells less vulnerable to T cell-based immune surveillance. Using the TAP-deficient cell line LCL721.174 and its TAP-expressing progenitor cell line LCL721.45, we identified and quantified more than 160 HLA ligands, 50 of which were presented TAP-independently. Peptides which were predominantly presented on the TAP-deficient LCL721.174 cell line…

Proteasome Endopeptidase ComplexImmunologyAntigen presentationEpitopes T-LymphocyteGene ExpressionHuman leukocyte antigenCysteine Proteinase InhibitorsProtein Sorting SignalsMajor histocompatibility complexCell LineAntigenATP Binding Cassette Transporter Subfamily B Member 3HLA AntigensTandem Mass SpectrometryMHC class IHLA-A2 AntigenImmunology and AllergyHumansAmino Acid SequenceATP Binding Cassette Transporter Subfamily B Member 2Antigen PresentationbiologyHLA-A AntigensAntigen processingHistocompatibility Antigens Class IProteinsTransporter associated with antigen processingMHC restrictionMolecular biologyPeptide FragmentsCell biologyHLA-B AntigensIsotope Labelingbiology.proteinATP-Binding Cassette TransportersProteasome InhibitorsGene DeletionProtein BindingEuropean journal of immunology
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Development of Novel Selective Peptidomimetics Containing a Boronic Acid Moiety, Targeting the 20S Proteasome as Anticancer Agents

2014

This paper describes the design, synthesis, and biological evaluation of peptidomimetic boronates as inhibitors of the 20S proteasome, a validated target in the treatment of multiple myeloma. The synthesized compounds showed a good inhibitory profile against the ChT-L activity of 20S proteasome. Compounds bearing a β-alanine residue at the P2 position were the most active, that is, 3-ethylphenylamino and 4-methoxyphenylamino (R)-1-{3-[4-(substituted)-2-oxopyridin-1(2H)-yl]propanamido}-3-methylbutylboronic acids (3 c and 3 d, respectively), and these derivatives showed inhibition constants (Ki ) of 17 and 20 nM, respectively. In addition, they co-inhibited post glutamyl peptide hydrolase act…

Proteasome Endopeptidase ComplexPeptidomimeticStereochemistryCell Survivalanticancer agents; boronates; bortemib; Docking studies; Peptidomimetics; inhibitor; proteasomesAntineoplastic AgentsSaccharomyces cerevisiaedocking studieBiochemistrySubstrate Specificitychemistry.chemical_compoundCell Line TumorDrug DiscoverymedicineMoietyHumansGeneral Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationBinding SitesproteasomesBortezomibOrganic ChemistrybortezomibboronateBoronic AcidspeptidomimeticProtein Structure Tertiaryanticancer agentMolecular Docking SimulationinhibitorEnzymechemistryProteasomeBiochemistryDocking (molecular)Molecular MedicinePeptidomimeticsGrowth inhibitionDrug Screening Assays AntitumorProteasome InhibitorsBoronic acidmedicine.drug
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