Search results for "Proteasome Endopeptidase Complex"

showing 10 items of 81 documents

The chaperone-like protein Cdc48 regulates ubiquitin-proteasome system in plants.

2021

The degradation of misfolded proteins is mainly mediated by the ubiquitin-proteasome system (UPS). UPS can be assisted by the protein Cdc48 but the relationship between UPS and Cdc48 in plants has been poorly investigated. Here, we analyzed the regulation of UPS by Cdc48 in tobacco thanks to two independent cell lines overexpressing Cdc48 constitutively and plant leaves overexpressing Cdc48 transiently. In the cell lines, the accumulation of ubiquitinated proteins was affected both quantitatively and qualitatively and the amount of proteasomal subunits was modified, while proteolytic activities were unchanged. Similarly, the over-expression of Cdc48 in planta impacted the accumulation of ub…

0106 biological sciences0301 basic medicineHypersensitive responseProgrammed cell deathProteasome Endopeptidase ComplexPhysiologyProtein subunitubiquitinomePlant Science01 natural sciencescryptogeinCdc48Fungal Proteins03 medical and health sciences[CHIM.ANAL]Chemical Sciences/Analytical chemistryValosin Containing ProteinTobacco[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyPlant ImmunityPlant ProteinsbiologyChemistryUbiquitinUbiquitin homeostasisPlants Genetically ModifiedUbiquitinated ProteinsElicitorCell biology030104 developmental biologyproteasomeProteasomeCell cultureChaperone (protein)biology.protein010606 plant biology & botanyPlant, cellenvironmentREFERENCES
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Preferential induction of 20S proteasome subunits during elicitation of plant defense reactions: towards the characterization of "plant defense prote…

2003

Plants have evolved efficient mechanisms to resist pathogens. The earliest defense response is the hypersensitive response (HR) considered as the main step leading to plant systemic acquired resistance (SAR) that protects the whole plant against a large spectrum of pathogens. We showed previously that elicitation of defense reactions in tobacco cells by cryptogein, a proteinaceous elicitor of plant defense reactions, leads to a rapid and differential accumulation of transcripts corresponding to genes encoding defense-induced (din) subunits of 20S proteasome: beta1din, alpha3din and alpha6din.Here, expression of these three subunits was investigated by Northern blotting and by Western blotti…

0106 biological sciencesHypersensitive responseProteasome Endopeptidase Complex[SDV]Life Sciences [q-bio]Protein subunitBlotting WesternGene ExpressionBiology01 natural sciencesBiochemistryMixed Function OxygenasesFungal Proteins03 medical and health sciencesMultienzyme ComplexesTobaccoPlant defense against herbivoryElectrophoresis Gel Two-DimensionalNorthern blotComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesAlgal ProteinsProteinsCell BiologyBlotting NorthernMolecular biologyCell biologyElicitor[SDV] Life Sciences [q-bio]BlotPlant LeavesTobacco Mosaic VirusCysteine EndopeptidasesProteasomeEnzyme InductionREPONSE DE LA PLANTESystemic acquired resistance010606 plant biology & botanyPeptide HydrolasesThe international journal of biochemistrycell biology
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The Role of Osteoprotegerin and Its Ligands in Vascular Function

2019

International audience; The superfamily of tumor necrosis factor (TNF) receptors includes osteoprotegerin (OPG) and its ligands, which are receptor activators of nuclear factor kappa-B ligand (RANKL) and TNF-related apoptosis-inducing ligand (TRAIL). The OPG/RANKL/RANK system plays an active role in pathological angiogenesis and inflammation as well as cell survival. It has been demonstrated that there is crosstalk between endothelial cells and osteoblasts during osteogenesis, thus establishing a connection between angiogenesis and osteogenesis. This OPG/RANKL/RANK/TRAIL system acts on specific cell surface receptors, which are then able to transmit their signals to other intracellular comp…

0301 basic medicineAngiogenesismedicine.medical_treatmentReview030204 cardiovascular system & hematologyLigandslcsh:ChemistryTNF-Related Apoptosis-Inducing Ligand0302 clinical medicineReceptorlcsh:QH301-705.5Cellular SenescenceSpectroscopyReceptor Activator of Nuclear Factor-kappa BbiologyChemistryvascular diseaseGeneral MedicineComputer Science ApplicationsProtein Transportmedicine.anatomical_structureCytokineRANKLTumor necrosis factor alphaDisease Susceptibilitymedicine.symptomProtein BindingSignal Transductionmusculoskeletal diseasesProteasome Endopeptidase ComplexEndotheliumendotheliumNeovascularization PhysiologicInflammationCatalysisInorganic ChemistryStructure-Activity Relationship03 medical and health sciencesOsteoprotegerin[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemmedicineAnimalsHumansPhysical and Theoretical ChemistryMolecular BiologyMyocardiumRANK LigandOrganic ChemistryEndothelial Cells030104 developmental biologylcsh:Biology (General)lcsh:QD1-999osteoprotegerinOPG/RANKL/RANKCancer researchbiology.proteinBlood VesselsBiomarkers
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HDAC1 and HDAC2 integrate the expression of p53 mutants in pancreatic cancer.

2015

Mutation of p53 is a frequent genetic lesion in pancreatic cancer being an unmet clinical challenge. Mutants of p53 have lost the tumour-suppressive functions of wild type p53. In addition, p53 mutants exert tumour-promoting functions, qualifying them as important therapeutic targets. Here, we show that the class I histone deacetylases HDAC1 and HDAC2 contribute to maintain the expression of p53 mutants in human and genetically defined murine pancreatic cancer cells. Our data reveal that the inhibition of these HDACs with small molecule HDAC inhibitors (HDACi), as well as the specific genetic elimination of HDAC1 and HDAC2, reduce the expression of mutant p53 mRNA and protein levels. We fur…

0301 basic medicineCancer ResearchProteasome Endopeptidase ComplexMutantHistone Deacetylase 2Histone Deacetylase 1Biologymedicine.disease_causeMolecular oncologyProto-Oncogene Proteins c-myc03 medical and health sciencesMicePancreatic cancerGeneticsmedicineAnimalsHumansRNA MessengerPromoter Regions GeneticMolecular BiologyRegulation of gene expressionMice KnockoutMutationWild typeCancerProto-Oncogene Proteins c-mdm2medicine.diseaseGenes p53HDAC13. Good healthGene Expression Regulation NeoplasticHistone Deacetylase InhibitorsPancreatic NeoplasmsDisease Models Animal030104 developmental biologyMutationCancer researchOncogene
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Enhanced autophagic-lysosomal activity and increased BAG3-mediated selective macroautophagy as adaptive response of neuronal cells to chronic oxidati…

2019

Oxidative stress and a disturbed cellular protein homeostasis (proteostasis) belong to the most important hallmarks of aging and of neurodegenerative disorders. The proteasomal and autophagic-lysosomal degradation pathways are key measures to maintain proteostasis. Here, we report that hippocampal cells selected for full adaptation and resistance to oxidative stress induced by hydrogen peroxide (oxidative stress-resistant cells, OxSR cells) showed a massive increase in the expression of components of the cellular autophagic-lysosomal network and a significantly higher overall autophagic activity. A comparative expression analysis revealed that distinct key regulators of autophagy are upregu…

0301 basic medicineClinical BiochemistryLFQ Label-free quantificationLETM Leucine zipper and EF-hand containing transmembrane proteinmedicine.disease_causeBiochemistryCHX Cycloheximide0302 clinical medicineBNIP3 Bcl-2 interacting protein 3RAPA RapamycinPIK3C3 Class III PI3‐kinasePhosphorylationlcsh:QH301-705.5Neuronslcsh:R5-920PolyUB PolyubiquitinChemistryBAG3OPA1 Optic atrophy 1TOR Serine-Threonine KinasesWIPI1 WD repeat domain phosphoinositide-interacting protein 1ATG Autophagy relatedTFEB Transcription factor EBCell biologyMitochondriasiRNA Small interfering RNADLP1 Dynamin-like protein 1LAMP1 Lysosomal‐associated membrane protein 1PURO Puromycinlcsh:Medicine (General)Protein homeostasisResearch PaperBafA1 Bafilomycin A1LAMP2 Lysosomal‐associated membrane protein 2Proteasome Endopeptidase ComplexRAB18 Member RAS oncogeneTUB TubulinLC3 Light chain 3 proteinOxidative phosphorylationBAG3CTSD Cathepsin DModels BiologicalCell Line03 medical and health sciencesDownregulation and upregulationMacroautophagymedicineAutophagyHumansAdaptationBAG1 Bcl-2-associated athanogene 1BECN1 Beclin1PI3K/AKT/mTOR pathwayAdaptor Proteins Signal TransducingTEM Transmission electron microscopyHsp70 Heat shock protein 70Organic ChemistryAutophagyAutophagosomesmTOR Mammalian target of rapamycinHsp70Oxidative Stress030104 developmental biologyProteostasislcsh:Biology (General)CV CanavanineBAG3 Bcl-2-associated athanogene 3MTT (3-(45-Dimethylthiazol-2-yl)-25-Diphenyltetrazolium Bromide)Apoptosis Regulatory ProteinsLysosomes030217 neurology & neurosurgeryOxidative stressRedox Biology
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Ticagrelor, but not clopidogrel, reduces arterial thrombosis via endothelial tissue factor suppression

2017

The P2Y12 antagonist ticagrelor reduces mortality in patients with acute coronary syndrome (ACS), compared with clopidogrel, and the mechanisms underlying this effect are not clearly understood. Arterial thrombosis is the key event in ACS; however, direct vascular effects of either ticagrelor or clopidogrel with focus on arterial thrombosis and its key trigger tissue factor have not been previously investigated.Methods and results: Human aortic endothelial cells were treated with ticagrelor or clopidogrel active metabolite (CAM) and stimulated with tumour necrosis factor-alpha (TNF-α); effects on procoagulant tissue factor (TF) expression and activity, its counter-player TF pathway inhibito…

0301 basic medicineMaleTicagrelorAdenosineTime FactorsPhysiology030204 cardiovascular system & hematology2737 Physiology (medical)0302 clinical medicineP2Y12AntithromboticCells CulturedClopidogrelReceptors Purinergic P2Y123. Good healthClopidogrelmedicine.anatomical_structureCoagulation10209 Clinic for CardiologyCardiologyCardiology and Cardiovascular MedicineTicagrelormedicine.drugBlood PlateletsAcute coronary syndromemedicine.medical_specialtyProteasome Endopeptidase ComplexTiclopidineEndotheliumDown-Regulation610 Medicine & health2705 Cardiology and Cardiovascular MedicineThromboplastinEquilibrative Nucleoside Transporter 103 medical and health sciencesTissue factorFibrinolytic AgentsPhysiology (medical)Internal medicinemedicineAnimalsHumanscardiovascular diseasesBlood Coagulationbusiness.industryTumor Necrosis Factor-alphaEndothelial CellsThrombosis1314 Physiologymedicine.diseaseMice Inbred C57BLDisease Models Animal030104 developmental biologyProteolysisPurinergic P2Y Receptor AntagonistsbusinessCarotid Artery InjuriesPlatelet Aggregation Inhibitors
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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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Pro- and Antitumorigenic Capacity of Immunoproteasomes in Shaping the Tumor Microenvironment

2021

Abstract Apart from the constitutive proteasome, the immunoproteasome that comprises the three proteolytic subunits LMP2, MECL-1, and LMP7 is expressed in most immune cells. In this study, we describe opposing roles for immunoproteasomes in regulating the tumor microenvironment (TME). During chronic inflammation, immunoproteasomes modulated the expression of protumorigenic cytokines and chemokines and enhanced infiltration of innate immune cells, thus triggering the onset of colitis-associated carcinogenesis (CAC) in wild-type mice. Consequently, immunoproteasome-deficient animals (LMP2/MECL-1/LMP7–null mice) were almost completely resistant to CAC development. In patients with ulcerative c…

0301 basic medicineProteasome Endopeptidase ComplexCancer ResearchChemokineImmunologyMelanoma ExperimentalAntineoplastic AgentsInflammationmedicine.disease_causeArticleMice03 medical and health sciences0302 clinical medicineImmune systemCell Line TumorTumor MicroenvironmentmedicineAnimalsHumansMice KnockoutTumor microenvironmentInnate immune systembiologyChemistryMelanomaHistocompatibility Antigens Class IColitismedicine.diseaseMice Inbred C57BLCysteine Endopeptidases030104 developmental biology030220 oncology & carcinogenesisCancer researchbiology.proteinCytokinesFemalemedicine.symptomCarcinogenesisCD8T-Lymphocytes CytotoxicCancer Immunology Research
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Aβ Induces Excitotoxicity Mediated by APC/C-Cdh1 Depletion That Can Be Prevented by Glutaminase Inhibition Promoting Neuronal Survival

2016

AbstractThe E3 ubiquitin ligase anaphase-promoting complex/cyclosome (APC/C) is activated by the fizzy-related protein homolog/CDC20-like protein 1 (cdh1) in post-mitotic neurons. Growing evidence suggests that dysregulation of APC/C-Cdh1 is involved in neurodegenerative diseases. Here we show in neurons that oligomers of amyloid beta (Aβ), a peptide related to Alzheimer’s disease, cause proteasome-dependent degradation of cdh1. This leads to a subsequent increase in glutaminase (a degradation target of APC/C-Cdh1), which causes an elevation of glutamate levels and further intraneuronal Ca2+ dysregulation, resulting in neuronal apoptosis. Glutaminase inhibition prevents glutamate excitotoxi…

0301 basic medicineProteasome Endopeptidase ComplexCell SurvivalAmyloid betaBlotting WesternExcitotoxicityHippocampusmedicine.disease_causeHippocampusArticleAnaphase-Promoting Complex-CyclosomeCdh1 ProteinsAnimals Genetically ModifiedMice03 medical and health sciences0302 clinical medicineGlutaminasemedicineAnimalsRats WistarNeuronsAmyloid beta-PeptidesMultidisciplinarybiologyGlutaminaseCyclin-dependent kinase 5Glutamate receptorCyclin-Dependent Kinase 5Molecular biologyRatsUbiquitin ligase030104 developmental biologyApoptosisbiology.protein030217 neurology & neurosurgeryScientific Reports
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Phosphorylation and proteasome recognition of the mRNA- binding protein Cth2 facilitates yeast adaptation to iron deficiency

2018

Iron is an indispensable micronutrient for all eukaryotic organisms due to its participation as a redox cofactor in many metabolic pathways. Iron imbalance leads to the most frequent human nutritional deficiency in the world. Adaptation to iron limitation requires a global reorganization of the cellular metabolism directed to prioritize iron utilization for essential processes. In response to iron scarcity, the conserved Saccharomyces cerevisiae mRNA-binding protein Cth2, which belongs to the tristetraprolin family of tandem zinc finger proteins, coordinates a global remodeling of the cellular metabolism by promoting the degradation of multiple mRNAs encoding highly iron-consuming proteins.…

0301 basic medicineProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsIronPosttranslational regulationSaccharomyces cerevisiaeMrna bindingMicrobiology03 medical and health sciencesProtein stabilityTristetraprolinGene Expression Regulation FungalVirologyPolitical scienceProtein stabilitySerineRNA MessengerPhosphorylationIron deficiencyAdaptation PhysiologicalQR1-502Yeast030104 developmental biologyMutagenesisChristian ministryProtein Processing Post-TranslationalHumanities
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