Search results for "Proteolysi"

showing 10 items of 119 documents

The C-terminal region of human plasma fetuin-B is dispensable for the raised-elephant-trunk mechanism of inhibition of astacin metallopeptidases

2019

© The Author(s) 2019.

0301 basic medicineProteasesProtein Conformationlcsh:MedicineAstacoideaCrystallography X-RayCleavage (embryo)Protein Structure SecondaryArticleMice03 medical and health sciencesScissile bondHydrolaseAnimalsHumansAmino Acid Sequencelcsh:ScienceProtein secondary structureX-ray crystallographyBinding SitesMultidisciplinary030102 biochemistry & molecular biologyChemistrylcsh:RMetalloendopeptidasesProteasesFetuinFetuin-BCell biologyZincFertility030104 developmental biologyProteolysisMetalloproteaseslcsh:QAstacinLinkerScientific Reports
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Host Cell Calpains Can Cleave Structural Proteins from the Enterovirus Polyprotein

2019

Enteroviruses are small RNA viruses that cause diseases with various symptoms ranging from mild to severe. Enterovirus proteins are translated as a single polyprotein, which is cleaved by viral proteases to release capsid and nonstructural proteins. Here, we show that also cellular calpains have a potential role in the processing of the enteroviral polyprotein. Using purified calpains 1 and 2 in an in vitro assay, we show that addition of calpains leads to an increase in the release of VP1 and VP3 capsid proteins from P1 of enterovirus B species, detected by western blotting. This was prevented with a calpain inhibitor and was dependent on optimal calcium concentration, especially for calpa…

0301 basic medicineProteasesentsyymitRNA virusviruksetvirusesPeptideCleavage (embryo)infektiotMass SpectrometryArticle03 medical and health sciencesViral ProteinsCapsidVirologyCleaveEnterovirus InfectionsAnimalsHumansCells CulturedGlycoproteinsPolyproteinschemistry.chemical_classification030102 biochemistry & molecular biologybiologyChemistryCalpainenterovirusvirus diseasesRNA virusCalpainbiochemical phenomena metabolism and nutritionbiology.organism_classificationAmino acidRatspolyproteinenterovirukset030104 developmental biologyInfectious DiseasesBiochemistryCapsidproteolytic processingProteolysisbiology.proteinCapsid ProteinsproteiinitPeptidescalpain
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BAG3 regulates total MAP1LC3B protein levels through a translational but not transcriptional mechanism

2015

Autophagy is mainly regulated by post-translational and lipid modifications of ATG proteins. In some scenarios, the induction of autophagy is accompanied by increased levels of certain ATG mRNAs such as MAP1LC3B/LC3B, ATG5 or ATG12. However, little is known about the regulation of ATG protein synthesis at the translational level. The cochaperone of the HSP70 system BAG3 (BCL2-associated athanogene 3) has been associated to LC3B lipidation through an unknown mechanism. In the present work, we studied how BAG3 controls autophagy in HeLa and HEK293 cells. Our results showed that BAG3 regulates the basal amount of total cellular LC3B protein by controlling its mRNA translation. This effect was …

0301 basic medicineProteasome Endopeptidase ComplexTranscription GeneticATG8ATG5BiologyBAG3ATG1203 medical and health sciences0302 clinical medicineProtein biosynthesisHumansRNA MessengerMolecular BiologyAdaptor Proteins Signal TransducingGeneticsGene knockdownAutophagyCell BiologyLipidsBasic Research PaperCell biologyHEK293 Cells030104 developmental biologyProtein BiosynthesisProteolysisApoptosis Regulatory ProteinsLysosomesMicrotubule-Associated ProteinsMAP1LC3B030217 neurology & neurosurgeryHeLa Cells
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Phosphorylation of meprin β controls its cell surface abundance and subsequently diminishes ectodomain shedding

2021

Meprin β is a zinc-dependent metalloprotease exhibiting a unique cleavage specificity with strong preference for acidic amino acids at the cleavage site. Proteomic studies revealed a diverse substrate pool of meprin β including the interleukin-6 receptor (IL-6R) and the amyloid precursor protein (APP). Dysregulation of meprin β is often associated with pathological conditions such as chronic inflammation, fibrosis, or Alzheimer's disease (AD). The extracellular regulation of meprin β including interactors, sheddases, and activators has been intensively investigated while intracellular regulation has been barely addressed in the literature. This study aimed to analyze C-terminal phosphorylat…

0301 basic medicineProtein Kinase C-alphaImmunoprecipitationmedia_common.quotation_subjectBiochemistry03 medical and health sciences0302 clinical medicineProtein Kinase C betaTumor Cells CulturedGeneticsAmyloid precursor proteinHumansPhosphorylationInternalizationMolecular BiologyProtein kinase Cmedia_commonbiologyChemistryCell MembraneMetalloendopeptidasesSheddaseCell biology030104 developmental biologyGene Expression RegulationEctodomainColonic NeoplasmsProteolysisbiology.proteinPhosphorylationExtracellular Space030217 neurology & neurosurgeryIntracellularBiotechnologyThe FASEB Journal
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Endogenous β-neurexins on axons and within synapses show regulated dynamic behavior

2021

Summary: Neurexins are key organizer molecules that regulate synaptic function and are implicated in autism and schizophrenia. β-neurexins interact with numerous cell adhesion and receptor molecules, but their neuronal localization remains elusive. Using single-molecule tracking and high-resolution microscopy to detect neurexin1β and neurexin3β in primary hippocampal neurons from knockin mice, we demonstrate that endogenous β-neurexins are present in fewer than half of excitatory and inhibitory synapses. Moreover, we observe a large extrasynaptic pool of β-neurexins on axons and show that axonal β-neurexins diffuse with higher surface mobility than those transiently confined within synapses…

0301 basic medicineQH301-705.5Green Fluorescent ProteinsNerve Tissue ProteinsEndogenyHippocampal formationNeurotransmissionGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineProtein DomainsAnimalsPremovement neuronal activityneurotransmissionBiology (General)synaptic functionCell adhesionelectron microscopyintegumentary systemChemistryCell MembranefungiGlutamate receptorcell adhesionproteaseAxonsCell biologyMice Inbred C57BL030104 developmental biologyEctodomainProteolysisSynapsesExcitatory postsynaptic potentialsingle-particle tracking030217 neurology & neurosurgeryCell Reports
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The RAB GTPase RAB18 modulates macroautophagy and proteostasis

2017

Macroautophagy is a conserved degradative pathway and its deterioration is linked to disturbances in cellular proteostasis and multiple diseases. Here, we show that the RAB GTPase RAB18 modulates autophagy in primary human fibroblasts. The knockdown of RAB18 results in a decreased autophagic activity, while its overexpression enhances the degradative pathway. Importantly, this function of RAB18 is dependent on RAB3GAP1 and RAB3GAP2, which might act as RAB GEFs and stimulate the activity of the RAB GTPase. Moreover, the knockdown of RAB18 deteriorates proteostasis and results in the intracellular accumulation of ubiquitinated degradation-prone proteins. Thus, the RAB GTPase RAB18 is a positi…

0301 basic medicineRecombinant Fusion Proteinsrab3 GTP-Binding ProteinsPrimary Cell CultureBiophysicsGTPaseBiochemistry03 medical and health sciencesUbiquitinGenes ReporterAutophagyHumansRNA Small InterferingMolecular BiologyGene knockdownbiologyProtein StabilityChemistryfungiAutophagyCell BiologyFibroblastsCell biologyLuminescent Proteins030104 developmental biologyProteostasisGene Expression Regulationrab GTP-Binding ProteinsProteolysisbiology.proteinCancer researchRabSignal transductionRAB18Signal TransductionBiochemical and Biophysical Research Communications
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On the origin of BAG(3) and its consequences for an expansion of BAG3's role in protein homeostasis

2021

The B-cell CLL 2-associated athanogene (BAG) protein family in general and BAG3, in particular, are pivotal elements of cellular protein homeostasis, with BAG3 playing a major role in macroautophagy. In particular, in the contexts of senescence and degeneration, BAG3 has exhibited an essential role often related to its capabilities to organize and remove aggregated proteins. Exciting studies in different species ranging from human, murine, zebrafish, and plant samples have delivered vital insights into BAG3s' (and other BAG proteins') functions and their regulations. However, so far no studies have addressed neither BAG3's evolution nor its phylogenetic position in the BAG family.

0301 basic medicineSenescenceProteasome Endopeptidase ComplexProtein family610 MedizinBiologyProtein HomeostasisBAG3BiochemistryEvolution MolecularWW domain03 medical and health sciences0302 clinical medicineProtein Domains610 Medical sciencesAutophagyAnimalsHumansMolecular BiologyZebrafishCellular SenescencePhylogenyAdaptor Proteins Signal TransducingAutophagyFungiCell BiologyPlantsbiology.organism_classificationCell biology030104 developmental biologyProteostasis030220 oncology & carcinogenesisProteolysisProteostasisbiology.proteinApoptosis Regulatory ProteinsSignal TransductionJournal of Cellular Biochemistry
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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 and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family

2017

AbstractWe introduce LytU, a short member of the lysostaphin family of zinc-dependent pentaglycine endopeptidases. It is a potential antimicrobial agent for S. aureus infections and its gene transcription is highly upregulated upon antibiotic treatments along with other genes involved in cell wall synthesis. We found this enzyme to be responsible for the opening of the cell wall peptidoglycan layer during cell divisions in S. aureus. LytU is anchored in the plasma membrane with the active part residing in the periplasmic space. It has a unique Ile/Lys insertion at position 151 that resides in the catalytic site-neighbouring loop and is vital for the enzymatic activity but not affecting the …

0301 basic medicineentsyymitantimicrobial compoundsPROTEINchemistry.chemical_compoundCatalytic DomainCELL-WALLBINDINGMultidisciplinaryACTIVE-SITEQRESISTANT STAPHYLOCOCCUS-AUREUSRHydrogen-Ion ConcentrationAnti-Bacterial AgentsZincBiochemistryMedicineHISTIDINESProtein BindingStaphylococcus aureusScienceenzymesBiologyCleavage (embryo)metalloproteinasesArticleCofactorBACILLUS-SUBTILISCell wallStructure-Activity Relationship03 medical and health sciencesEndopeptidasesProtein Interaction Domains and MotifsAmino Acid Sequencestaphylococciantimikrobiset yhdisteetBinding SitesLysostaphinCell MembraneActive siteIsothermal titration calorimetryPeriplasmic spaceVANCOMYCINstafylokokitmetalloproteinaasitMODEL030104 developmental biologyRESOLUTIONchemistryMutationProteolysisLysostaphinbiology.protein1182 Biochemistry cell and molecular biologyPeptidoglycanScientific Reports
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Proteolytic Enzymes Clustered in Specialized Plasma-Membrane Domains Drive Endothelial Cells’ Migration

2016

In vitro cultured endothelial cells forming a continuous monolayer establish stable cell-cell contacts and acquire a "resting" phenotype; on the other hand, when growing in sparse conditions these cells acquire a migratory phenotype and invade the empty area of the culture. Culturing cells in different conditions, we compared expression and clustering of proteolytic enzymes in cells having migratory versus stationary behavior. In order to observe resting and migrating cells in the same microscopic field, a continuous cell monolayer was wounded. Increased expression of proteolytic enzymes was evident in cell membranes of migrating cells especially at sprouting sites and in shed membrane vesi…

0301 basic medicinekalininsepraseCell Membranesbeta1 integrinCelllcsh:MedicineurokinaseBiochemistryEpitheliumCell membrane0302 clinical medicineAnimal CellsMedicine and Health Sciencesdipeptidyl peptidase IVlcsh:ScienceMultidisciplinarybiologyVesicleProteolytic enzymesCell migrationProteasesEnzymesCell biologyLaboratory EquipmentCell Motilitymedicine.anatomical_structureBiochemistry030220 oncology & carcinogenesisEngineering and TechnologyBiological Culturesmatrix metalloproteinase 14Cellular Structures and OrganellesCellular TypesAnatomyResearch ArticleEquipmentCell MigrationResearch and Analysis MethodsGelatin MediaCell Linegelatinase B03 medical and health sciencescollagen type 4fibronectinmedicineHumansVesiclescollagen type 1gelatinase Alcsh:RCell MembraneBiology and Life SciencesEndothelial CellsProteinsMembrane ProteinsEpithelial CellsCell BiologyCulture MediaFibronectinBiological Tissue030104 developmental biologyMembrane proteinCell cultureProteolysisMicroscopy Electron ScanningEnzymologybiology.proteinlcsh:QCollagensDevelopmental BiologyPLOS ONE
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