Search results for "Proteasome Inhibitors"

showing 10 items of 27 documents

The emergence of drug resistance to targeted cancer therapies: Clinical evidence.

2019

For many decades classical anti-tumor therapies included chemotherapy, radiation and surgery; however, in the last two decades, following the identification of the genomic drivers and main hallmarks of cancer, the introduction of therapies that target specific tumor-promoting oncogenic or non-oncogenic pathways, has revolutionized cancer therapeutics. Despite the significant progress in cancer therapy, clinical oncologists are often facing the primary impediment of anticancer drug resistance, as many cancer patients display either intrinsic chemoresistance from the very beginning of the therapy or after initial responses and upon repeated drug treatment cycles, acquired drug resistance deve…

0301 basic medicineDrugCancer Researchmedicine.drug_classmedicine.medical_treatmentmedia_common.quotation_subjectTranslational researchApoptosisDrug resistanceMonoclonal antibodyBioinformatics03 medical and health sciences0302 clinical medicineNeoplasmsmedicineHumansPharmacology (medical)Hedgehog ProteinsEpigeneticsProtein Kinase Inhibitorsmedia_commonPharmacologyChemotherapybusiness.industryCancerImmunotherapyProtein-Tyrosine Kinasesmedicine.disease030104 developmental biologyInfectious DiseasesOncologyDrug Resistance Neoplasm030220 oncology & carcinogenesisbusinessProteasome InhibitorsDrug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy
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Venetoclax or placebo in combination with bortezomib and dexamethasone in patients with relapsed or refractory multiple myeloma (BELLINI): a randomis…

2020

Background Venetoclax is a highly selective, potent, oral BCL-2 inhibitor, which induces apoptosis in multiple myeloma cells. Venetoclax plus bortezomib and dexamethasone has shown encouraging clinical efficacy with acceptable safety and tolerability in a phase 1 trial. The aim of this study was to evaluate venetoclax plus bortezomib and dexamethasone in patients with relapsed or refractory multiple myeloma. Methods In this randomised, double-blind, multicentre, phase 3 trial, patients aged 18 years or older with relapsed or refractory multiple myeloma, an Eastern Cooperative Oncology Group performance status of 2 or less, who had received one to three previous therapies were enrolled from …

0301 basic medicineMalemedicine.medical_specialtyTime FactorsPopulationNeutropeniaPlaceboDexamethasoneBortezomib03 medical and health scienceschemistry.chemical_compound0302 clinical medicineDouble-Blind MethodInternal medicineAntineoplastic Combined Chemotherapy ProtocolsClinical endpointMedicineHumansProgression-free survivaleducationAgededucation.field_of_studySulfonamidesbusiness.industryVenetoclaxBortezomibMiddle Agedmedicine.diseaseBridged Bicyclo Compounds HeterocyclicProgression-Free SurvivalVenetoclax BCL-2 inhibitor multiple myeloma Venetoclax plus bortezomib and dexamethasone030104 developmental biologyOncologychemistryTolerability030220 oncology & carcinogenesisFemalebusinessMultiple MyelomaProteasome Inhibitorsmedicine.drug
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Identification of noncovalent proteasome inhibitors with high selectivity for chymotrypsin-like activity by a multistep structure-based virtual scree…

2016

Noncovalent proteasome inhibitors introduce an alternative mechanism of inhibition to that of covalent inhibitors, e.g. carfilzomib, used in cancer therapy. A multistep hierarchical structure-based virtual screening (SBVS) of the 65,375 NCI lead-like compound library led to the identification of two compounds (9 and 28) which noncovalently inhibited the chymotrypsin-like (ChT-L) activity (Ki = 2.18 and 2.12 μM, respectively) with little or no effects on the other two major proteasome proteolytic activities, trypsin-like (T-L) and post-glutamyl peptide hydrolase (PGPH) activities. A subsequent hierarchical similarity search over the full NCI database with the most active tripeptide-based inh…

0301 basic medicineNon-covalentVirtual screeningProteasome Endopeptidase ComplexStereochemistryProtein ConformationProteolysisDrug Evaluation PreclinicalTripeptideSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity RelationshipUser-Computer Interface0302 clinical medicineProtein structureCell Line TumorDrug DiscoverymedicineStructure–activity relationshipChymotrypsinHumansProteasome inhibitorCell ProliferationPharmacologyVirtual screeningmedicine.diagnostic_testOrganic ChemistryGeneral MedicineCarfilzomibPeptide scaffoldMolecular Docking SimulationProteasome inhibitors; Non-covalent; Peptide scaffold; Docking studies; Virtual screening030104 developmental biologyProteasomechemistryBiochemistryDocking (molecular)030220 oncology & carcinogenesisDocking studieProteolysisProteasome InhibitorsEuropean journal of medicinal chemistry
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Characterization of a mutant form of human apolipoprotein B (Thr26_Tyr27del) associated with familial hypobetalipoproteinemia

2016

We have previously identified a deletion mutant of human apoB [apoB (Thr26_Tyr27del)] in a subject with primary hypobetalipoproteinemia. The present study determined the effect of Thr26_Tyr27del mutation on apoB secretion using transfected McA-RH7777 cells. Transient or stable transfection of apoB-48 containing the Thr26_Tyr27del mutation showed drastically reduced secretion of the mutant as compared to wild-type apoB-48. No lipoproteins containing the mutant apoB-48 were secreted into the medium. Incubation of transfected cells in a lipid-rich medium in the presence of cycloheximide showed rapid turnover of cell-associated mutant apoB-48 as compared to that of wild-type apoB-48. Immunofluo…

0301 basic medicineSettore MED/09 - Medicina InternaTime FactorsApolipoprotein B-48 secretionApolipoprotein BMutantDNA Mutational AnalysisApolipoprotein B mutation Apolipoprotein B-48 secretion Hypobetalipoproteinemia Proteasomal degradation030204 cardiovascular system & hematologymedicine.disease_causeEndoplasmic ReticulumHypobetalipoproteinemiaschemistry.chemical_compound0302 clinical medicineProteasomal degradationProteolysiSequence DeletionMutationbiologyMedicine (all)TransfectionProteasome InhibitorPhenotypeBiochemistryApolipoprotein B-100lipids (amino acids peptides and proteins)Proteasome InhibitorsHumanHeterozygoteProteasome Endopeptidase ComplexTime FactorCycloheximideTransfectiondigestive systemCell LineDNA Mutational Analysi03 medical and health sciencesmedicineHumansSecretionGenetic Predisposition to DiseaseMolecular BiologyEndoplasmic reticulumnutritional and metabolic diseasesCell Biologymedicine.diseaseMolecular biology030104 developmental biologychemistryProteolysisbiology.proteinHypobetalipoproteinemiaApolipoprotein B mutationApolipoprotein B-48Hypobetalipoproteinemia
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Identification of a new series of amides as non-covalent proteasome inhibitors

2014

Proteasome inhibition has emerged as an important therapeutic strategy for the treatment of multiple myeloma (MM) and some forms of lymphoma, with potential application in other types of cancers. 20S proteasome consists of three different catalytic activities known as chymotrypsin-like (ChT-L), trypsin-like (T-L), and, post-glutamyl peptide hydrolyzing (PGPH) or caspase-like (C-L), which are located respectively on the β5, β2, and β1 subunits of each heptameric β rings. Currently a wide number of covalent proteasome inhibitors are reported in literature; however, the less widely investigated non-covalent inhibitors might be a promising alternative to employ in therapy, because of the lack o…

AmideMagnetic Resonance SpectroscopyStereochemistryProtein subunitPeptideMolecular Docking SimulationDrug DiscoverymedicineHumansProteasome inhibitorDocking studiesMultiple myelomaPharmacologychemistry.chemical_classificationOrganic ChemistryGeneral Medicinemedicine.diseaseAmidesYeastMolecular Docking SimulationchemistryProteasomeBiochemistryNon-covalent inhibitorDocking (molecular)Covalent bondProteasome Inhibitors
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Proteasome-inhibited dendritic cells demonstrate improved presentation of exogenous synthetic and natural HLA-class I peptide epitopes.

2004

The design and successful clinical implementation of cancer vaccines targeting the induction of T-cell mediated immunity is a rapidly evolving field that is hampered by an empirical selection of antigen and adjuvant. In particular, vaccines using defined tumor-associated peptide epitopes elicit only a restricted T-cell repertoire in a minority of patients. In this regard, vaccines comprising the whole spectrum of antigens presented by individual autologous tumors would be advantageous. In an in vitro model, we evaluated the capacity of naturally processed Epstein-Barr virus-transformed B-lymphoblastoid-cell line (LCL)-derived peptides to activate virus-specific CD8+ T cells of seropositive …

AntigenicityHerpesvirus 4 HumanT cellImmunologyHuman leukocyte antigenBiologyCD8-Positive T-LymphocytesIn Vitro TechniquesLymphocyte ActivationCancer VaccinesEpitopeMonocytesEpitopesAntigenHLA AntigensmedicineImmunology and AllergyHumansProtease InhibitorsAntigen PresentationImmunogenicityHistocompatibility Antigens Class IDendritic cellDendritic CellsCell Transformation ViralMolecular biologyCell biologyClone Cellsmedicine.anatomical_structureProteasome inhibitorLymphocyte Culture Test MixedProteasome Inhibitorsmedicine.drugJournal of immunological methods
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Preclinical evaluation of antitumor activity of the proteasome inhibitor MLN2238 (ixazomib) in hepatocellular carcinoma cells

2017

AbstractHepatocellular carcinoma (HCC) is one of the common malignancies and is an increasingly important cause of cancer death worldwide. Surgery, chemotherapy, and radiation therapy extend the 5-year survival limit in HCC patients by only 6%. Therefore, there is a need to develop new therapeutic approaches for the treatment of this disease. The orally bioavailable proteasome inhibitor MLN2238 (ixazomib) has been demonstrated to have anticancer activity. In the present study, we investigated the preclinical therapeutic efficacy of MLN2238 in HCC cells through in vitro and in vivo models, and examined its molecular mechanisms of action. MLN2238 inhibited cell viability in human HCC cells He…

Boron Compounds0301 basic medicineCancer ResearchCarcinoma HepatocellularMyeloidCell cycle checkpointImmunologyCellGlycineAntineoplastic AgentsArticleIxazomibAntineoplastic AgentMice03 medical and health sciencesCellular and Molecular Neurosciencechemistry.chemical_compound0302 clinical medicinemedicineAnimalsHumansViability assaylcsh:QH573-671Boron CompoundAnimallcsh:Cytologybusiness.industryLiver NeoplasmsCell Biologydigestive system diseases3. Good health030104 developmental biologymedicine.anatomical_structurechemistryLiver NeoplasmCell cultureApoptosis030220 oncology & carcinogenesisProteasome inhibitorCancer researchbusinessProteasome InhibitorsHumanmedicine.drugCell Death & Disease
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Development of peptidomimetic boronates as proteasome inhibitors.

2013

Abstract Proteasome inhibition has emerged over the past decade as an effective therapeutic approach for the treatment of hematologic malignancies. It is a multicatalytic complex, whose proteolytic activity relies in three types of subunits: chymotrypsin-like (β5), trypsin-like (β2) and caspase-like (β1). Most important for the development of effective antitumor agents is the inhibition of the β5 subunits. In this context, the dipeptide boronate bortezomib (Velcade ® ) represents the first proteasome inhibitor approved by the FDA and the lead compound in drug discovery. This paper describes the synthesis and biological evaluation of a series of conformationally constrained pseudopeptide bor…

Boron CompoundsModels MolecularProteasome Endopeptidase ComplexPeptidomimeticStructure-activity relationshipsPeptidomimetic boronates; Proteasome inhibitors; Docking studiesPharmacologyPeptidomimetic boronateDockingchemistry.chemical_compoundStructure-Activity RelationshipDrug DiscoverymedicineHumansProteasome inhibitorPharmacologyDipeptideDose-Response Relationship DrugMolecular StructureDrug discoveryBortezomibOrganic ChemistryGeneral MedicineBiochemistrychemistryProteasomeDocking (molecular)Proteasome inhibitorPeptidomimeticsLead compoundProteasome Inhibitorsmedicine.drugEuropean journal of medicinal chemistry
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SAHA induces apoptosis in hepatoma cells and synergistically interacts with the proteasome inhibitor Bortezomib.

2007

Histone deacetylase (HDAC) inhibitors represent a promising group of anticancer agents. This paper shows that the HDAC inhibitor suberoylanilide hydroxamic acid (SAHA) stimulated at 5-10 microM apoptosis in human hepatoma HepG2 and Huh6 cells, but was ineffective in primary human hepatocytes (PHH). In HepG2 cells SAHA induced the extrinsic apoptotic pathway, increasing the expression of both FasL and FasL receptor and causing the activation of caspase-8. Moreover, SAHA enhanced the level of Bim proteins, stimulated alternative splicing of the Bcl-X transcript with the expression of the proapoptotic Bcl-Xs isoform, induced degradation of Bid into the apoptotic factor t-Bid and dephosphorylat…

Cancer ResearchCarcinoma HepatocellularFas Ligand ProteinClinical BiochemistryPharmaceutical ScienceApoptosisHydroxamic AcidsFas ligandHistone DeacetylasesBortezomibCell Line TumormedicineHumansProtease InhibitorsProtein kinase BVorinostatHDAC inhibitors . HepG2 cells . PHH . Extrinsic and intrinsic apoptotic pathwaysbcl-2-Associated X ProteinPharmacologyMembrane Potential MitochondrialCaspase 8VorinostatbiologyChemistryBortezomibCytochrome cBiochemistry (medical)Cell BiologyBoronic AcidsHistone Deacetylase InhibitorsProteasomeApoptosisPyrazinesProteasome inhibitorbiology.proteinCancer researchApoptosis Regulatory ProteinsProteasome Inhibitorsmedicine.drug
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Bortezomib: a new pro-apoptotic agent in cancer treatment.

2010

Bortezomib is a proteasome inhibitor. It targets the ubiquitin-proteasome pathway with subsequent inhibition of the degradation of proteins involved in cell cycle regulation and cancer cell survival. The best known molecular mechanism concerns the inhibition of IkappaB breakdown and the related stabilization of NFkappaB, thus preventing its translocation to the nucleus for the activation of downstream pathways. Bortezomib is the only drug in this class which has been approved for clinical use. It has shown an efficient antitumor effect in a phase III clinical trial (APEX) involving relapsed multiple myeloma patients. Response rate, time to progression and overall survival have been improved…

Cancer ResearchCell cycle checkpointSettore MED/06 - Oncologia MedicaAntineoplastic AgentsApoptosisPharmacologyDexamethasoneBortezomibMiceNeoplasmshemic and lymphatic diseasesAntineoplastic Combined Chemotherapy ProtocolsDrug DiscoverymedicineAnimalsHumansDexamethasoneMultiple myelomaPharmacologyproteasome inhibitionClinical Trials as TopicNeovascularization Pathologicbusiness.industryBortezomibCell CycleNF-kappa Bsolid tumorsmedicine.diseaseBoronic AcidsClinical trialBortezomib; solid tumors; proteasome inhibition.OncologyApoptosisPyrazinesCancer cellProteasome inhibitorCancer researchMultiple MyelomabusinessProteasome InhibitorsBortezomib solid tumors proteasome inhibitionmedicine.drug
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