Search results for "proteolysis"

showing 10 items of 119 documents

Inhibition of ubiquitin-dependent proteolysis by a synthetic glycine-alanine repeat peptide that mimics an inhibitory viral sequence.

2002

AbstractThe glycine–alanine repeat (GAr) of the Epstein–Barr virus nuclear antigen-1 is a cis-acting transferable element that inhibits ubiquitin/proteasome-dependent proteolysis in vitro and in vivo. We have here examined the effect of a synthetic 20-mer GAr oligopeptide on the degradation of iodinated or biotin labeled lysozyme in a rabbit reticulocyte lysates in vitro assay. Micromolar concentrations of the GA-20 peptide inhibited the hydrolysis of lysozyme without significant effect on ubiquitination. Addition of the peptide did not inhibit the hydrolysis of fluorogenic substrate by purified proteasomes and did not affect the ubiquitination of lysozyme. An excess of the peptide failed t…

Herpesvirus 4 HumanProteasome Endopeptidase ComplexGly–Ala repeatPolymersProteolysisMolecular Sequence DataBiophysicsGlycineBiotinPeptideBiochemistryIodine Radioisotopeschemistry.chemical_compoundS5aUbiquitinStructural BiologyMultienzyme ComplexesGeneticsmedicineAnimalsAmino Acid SequenceEnzyme InhibitorsMolecular BiologyPeptide sequenceUbiquitinsEpstein–Barr virus nuclear antigen-1Alaninechemistry.chemical_classificationOligopeptideAlaninebiologymedicine.diagnostic_testProteasomeMolecular MimicryUbiquitinationCell BiologyCysteine EndopeptidasesBiochemistryProteasomechemistryEpstein-Barr Virus Nuclear AntigensIsotope Labelingbiology.proteinMuramidaseRabbitsLysozymeCarrier ProteinsPeptidesOligopeptidesFEBS letters
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Cryptogein affects expression of alpha3, alpha6 and beta1 20S proteasome subunits encoding genes in tobacco.

2001

Twelve a and b 20S proteasome subunits cDNAs showing 70–82% identity with the corresponding genes in Arabidopsis or rice, and features of eukaryotic proteasome subunits were cloned in tobacco. Only b1-tcI 7, a3 and a6, 20S proteasome subunits encoding genes were up-regulated by cryptogein, a proteinaceous elicitor of plant defence reactions. These results led to the hypothesis that the activation of b1-tcI 7, a3 and a6 could induce a specific proteolysis involved in the hypersensitive response and systemic acquired resistance monitored by cryptogein. In eukaryotes, the 26S proteasome is the central multicatalytic proteinase complex comprising two subcomplexes: the 20S core particle that per…

Hypersensitive responseProteasome Endopeptidase ComplexPhysiologyProtein subunitProteolysisMolecular Sequence DataPlant ScienceGenes PlantGene Expression Regulation EnzymologicFungal ProteinsGene Expression Regulation PlantMultienzyme ComplexesArabidopsisGene expressionTobaccomedicineAmino Acid SequenceGenePlant Diseasesbiologymedicine.diagnostic_testAlgal Proteinsbiology.organism_classificationPlants Genetically ModifiedCysteine EndopeptidasesProteasomeBiochemistryProtein foldingJournal of experimental botany
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Rapid inactivation and proteasome-mediated degradation of OGG1 contribute to the synergistic effect of hyperthermia on genotoxic treatments

2013

Inhibition of DNA repair has been proposed as a mechanism underlying heat-induced sensitization of tumour cells to some anticancer treatments. Base excision repair (BER) constitutes the main pathway for the repair of DNA lesions induced by oxidizing or alkylating agents. Here, we report that mild hyperthermia, without toxic consequences per se, affects cellular DNA glycosylase activities, thus impairing BER. Exposure of cells to mild hyperthermia leads to a rapid and selective inactivation of OGG1 (8-oxoguanine DNA glycosylase) associated with the relocalisation of the protein into a detergent-resistant cellular fraction. Following its inactivation, OGG1 is ubiquitinated and directed to pro…

HyperthermiaProteasome Endopeptidase ComplexPyrrolidinesDNA RepairDNA repairUbiquitin-Protein Ligases[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiochemistryDNA Glycosylases03 medical and health scienceschemistry.chemical_compound0302 clinical medicineUbiquitinEnzyme StabilitymedicineHumans[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyComputingMilieux_MISCELLANEOUSCell Proliferation030304 developmental biologyCell Nucleus0303 health sciencesPhotosensitizing AgentsbiologyCell growthUbiquitinationCell BiologyBase excision repairmedicine.diseaseMolecular biology[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]Protein TransportProteasomechemistryDNA glycosylase030220 oncology & carcinogenesisProteolysisCancer researchbiology.proteinHeat-Shock ResponseQuinolizinesDNADNA DamageHeLa Cells
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Salivary protein profiles and sensitivity to the bitter taste of caffeine.

2011

WOS: 000298381900008; International audience; The interindividual variation in the sensitivity to bitterness is attributed in part to genetic polymorphism at the taste receptor level, but other factors, such as saliva composition, might be involved. In order to investigate this, 2 groups of subjects (hyposensitive, hypersensitive) were selected from 29 healthy male volunteers based on their detection thresholds for caffeine, and their salivary proteome composition was compared. Abundance of 26 of the 255 spots detected on saliva electrophoretic patterns was significantly different between hypo- and hypersensitive subjects. Saliva of hypersensitive subjects contained higher levels of amylase…

Immunoglobulin AMaleSalivaPhysiologymedicine.medical_treatment[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritionperceptionbitternessin-vivoBehavioral Neurosciencechemistry.chemical_compound0302 clinical medicineTaste receptorphenolic astringent stimuliAmylase0303 health scienceswhole salivabiologyperiodontitis patientsMiddle AgedSensory Systemsmucosal pellicleTasteTaste ThresholdCystatinCaffeineimmunoglobulin-acystatinsAdultmedicine.medical_specialtyproteolysisproteomeSerum albumin03 medical and health sciencesstomatognathic systemPhysiology (medical)Internal medicineCaffeinemedicineHumansSalivary Proteins and Peptidescystatin030304 developmental biologysalivaProteasealpha-amylase030206 dentistryEndocrinologychemistrytwo-dimensionalelectrophoresisbiology.protein[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionhealthy-subjects
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Proteolytic processing of Bacillus thuringiensis Vip3A proteins by two Spodoptera species

2014

Abstract Vip3 proteins have been described to be secreted by Bacillus thuringiensis during the vegetative growth phase and to display a broad insecticidal spectrum against lepidopteran larvae. Vip3Aa protoxin has been reported to be significantly more toxic to Spodoptera frugiperda than to Spodoptera exigua and differences in the midgut processing have been proposed to be responsible. In contrast, we have found that Vip3Ae is essentially equally toxic against these two species. Proteolysis experiments were performed to study the stability of Vip3A proteins to peptidase digestion and to see whether the differences found could explain differences in toxicity against these two Spodoptera speci…

InsecticidesPhysiologyProteolysisBacterial ProteinSpodopteraSpodopteraMicrobiologyVegetative insecticidal proteinBacterial ProteinsSpecies SpecificitySpodoptera exiguaBacillus thuringiensisExiguamedicineAnimalsPest Control BiologicalMidgut peptidaseInsecticideChymotrypsinbiologymedicine.diagnostic_testAnimalMedicine (all)Serine EndopeptidasesfungiSpodoptera frugiperdaMidgutbiology.organism_classificationTrypsinSerine EndopeptidaseSerine peptidaseBiochemistryMode of actionLarvaInsect Sciencebiology.proteinDigestionDigestive Systemmedicine.drugJournal of Insect Physiology
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Combining Hexanoic Acid Plant Priming with Bacillus thuringiensis Insecticidal Activity against Colorado Potato Beetle

2013

Interaction between insect herbivores and host plants can be modulated by endogenous and exogenous compounds present in the source of food and might be successfully exploited in Colorado potato beetle (CPB) pest management. Feeding tests with CPB larvae reared on three solanaceous plants (potato, eggplant and tomato) resulted in variable larval growth rates and differential susceptibility to Bacillus thuringiensis Cry3Aa toxin as a function of the host plant. An inverse correlation with toxicity was observed in Cry3Aa proteolytic patterns generated by CPB midgut brush-border membrane vesicles (BBMV) from Solanaceae-fed larvae, being the toxin most extensively proteolyzed on potato, followed…

Insecticidesmedicine.disease_causeMass Spectrometrylcsh:Chemistrychemistry.chemical_compoundHemolysin ProteinsPlant Growth RegulatorsCysteine ProteasesBacillus thuringiensisPlant defense against herbivoryColorado potato beetleElectrophoresis Gel Two-Dimensionallcsh:QH301-705.5SpectroscopySolanaceaeHexanoic acidbiologyfood and beveragesGeneral MedicineComputer Science ApplicationsColeopterasurgical procedures operativeBiochemistryLarvaHost-Pathogen Interactionsplant hormonesInsect ProteinsSolanaceaeproteolysisColoradoMolecular Sequence DataBacillus thuringiensisCatalysisArticleMicrobiologyCry3Aa toxinInorganic Chemistryintestain proteasesBacterial Proteinsplant defensemedicineAnimalsAmino Acid SequencePhysical and Theoretical ChemistryprimingMolecular BiologyCaproatesSolanum tuberosumBacillus thuringiensis ToxinsToxinOrganic ChemistryColorado potato beetlefungiBody WeightMidgutColorado potato beetle;<i> Bacillus thuringiensis</i>; Cry3Aa toxin; intestain proteases; proteolysis; Solanaceae; hexanoic acid; priming; plant defense; plant hormonesFeeding Behaviorbiology.organism_classificationDietEndotoxinsPapainchemistrylcsh:Biology (General)lcsh:QD1-999hexanoic acidPeptidesDigestive SystemSequence AlignmentInternational Journal of Molecular Sciences
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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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Proteomic Analyses Reveal an Acidic Prime Side Specificity for the Astacin Metalloprotease Family Reflected by Physiological Substrates

2011

Astacins are secreted and membrane-bound metalloproteases with clear associations to many important pathological and physiological processes. Yet with only a few substrates described their biological roles are enigmatic. Moreover, the lack of knowledge of astacin cleavage site specificities hampers assay and drug development. Using PICS (proteomic identification of protease cleavage site specificity) and TAILS (terminal amine isotopic labeling of substrates) degradomics approaches >3000 cleavage sites were proteomically identified for five different astacins. Such broad coverage enables family-wide determination of specificities N- and C-terminal to the scissile peptide bond. Remarkably, me…

KeratinocytesModels MolecularProteomicsVascular Endothelial Growth Factor AProteasesmedicine.medical_treatmentProteolysisMolecular Sequence DataBiologyCleavage (embryo)BiochemistryCell LineSubstrate SpecificityAnalytical Chemistry03 medical and health sciencesTandem Mass SpectrometrymedicineHumansAmino Acid SequenceMolecular BiologyPeptide sequencePhylogeny030304 developmental biologyEnzyme Precursors0303 health sciencesProteaseStaining and LabelingEdman degradationmedicine.diagnostic_testResearch030302 biochemistry & molecular biologyTioproninMetalloendopeptidasesTerminal amine isotopic labeling of substratesRecombinant ProteinsKineticsBiochemistryProteolysisKallikreinsAstacinPeptidesSequence AlignmentChromatography LiquidMolecular &amp; Cellular Proteomics
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The degradation of intracrystalline mollusc shell proteins: a proteomics study of Spondylus gaederopus.

2021

Mollusc shells represent excellent systems for the preservation and retrieval of genuine biomolecules from archaeological or palaeontological samples. As a consequence, the post-mortem breakdown of intracrystalline mollusc shell proteins has been extensively investigated, particularly with regard to its potential use as a "molecular clock" for geochronological applications. But despite seventy years of ancient protein research, the fundamental aspects of diagenesis-induced changes to protein structures and sequences remain elusive. In this study we investigate the degradation of intracrystalline proteins by performing artificial degradation experiments on the shell of the thorny oyster, Spo…

Liquid chromatography-tandem mass spectrometry; Peptide bond hydrolysis; Protein degradation; TMT proteomics; Animal Shells; Animals; Bivalvia; Proteolysis; ProteomeProteomeQuantitative proteomicsBiophysicsPeptideProtein degradationProtein degradationProteomicsTandem mass tagBiochemistryAnalytical Chemistry03 medical and health sciences0302 clinical medicineProtein structurePeptide bond hydrolysisAnimal Shells[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]Mollusc shellPeptide bondAnimals[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesChemistryBivalviaTMT proteomicsLiquid chromatography-tandem mass spectrometryProteolysisBiophysics030217 neurology & neurosurgery
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Biodegradable Protein Nanocontainers

2015

The application of synthetic polymers for drug delivery often requires tremendous efforts to ensure biocompatibility and -degradation. To use the body's own substances can help to overcome these problems. Herein, we present the first synthesis of nanocontainers entirely composed of albumin proteins. These protein nanocontainers (PNCs) were loaded with hydrophilic compounds and release of the payload is triggered through natural lysis in vitro in human monocyte-derived dendritic cells (moDCs). No aggregation of PNCs in human blood plasma was observed, indicating stability for blood circulation. As the PNCs were readily taken up by moDCs, they are considered as a promising delivery platform f…

LysisPolymers and PlasticsBiocompatibilityHuman bloodProtein StabilityChemistryAlbuminBioengineeringNanotechnologyDendritic CellsBiomaterialsNanocapsulesAlbuminsDelayed-Action PreparationsBlood circulationProteolysisDrug deliveryMaterials ChemistryHumansHydrophobic and Hydrophilic InteractionsCells CulturedFluorescent DyesBiomacromolecules
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