Search results for "protein degradation"

showing 10 items of 51 documents

De Novo prion aggregates trigger autophagy in skeletal muscle

2014

ABSTRACT In certain sporadic, familial, and infectious prion diseases, the prion protein misfolds and aggregates in skeletal muscle in addition to the brain and spinal cord. In myocytes, prion aggregates accumulate intracellularly, yet little is known about clearance pathways. Here we investigated the clearance of prion aggregates in muscle of transgenic mice that develop prion disease de novo . In addition to neurodegeneration, aged mice developed a degenerative myopathy, with scattered myocytes containing ubiquitinated, intracellular prion inclusions that were adjacent to myocytes lacking inclusions. Myocytes also showed elevated levels of the endoplasmic reticulum chaperone Grp78/BiP, su…

PrionsAutophagosome maturationanimal diseasesBlotting WesternImmunologyMice TransgenicBiologyProtein degradationPolymerase Chain ReactionMedical and Health SciencesMicrobiologyTransgenicPrion DiseasesMiceVirologyAutophagymedicineAnimalsMyocyteMuscle SkeletalEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsDNA PrimersMuscle CellsAgricultural and Veterinary SciencesBlottingEndoplasmic reticulumNeurodegenerationAutophagySkeletal muscleSkeletalBiological Sciencesmedicine.diseaseImmunohistochemistryMolecular biologynervous system diseasesmedicine.anatomical_structureInsect ScienceChaperone (protein)biology.proteinMuscleWestern
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Quantitative Analysis of Prion-Protein Degradation by Constitutive and Immuno-20S Proteasomes Indicates Differences Correlated with Disease Susceptib…

2004

Abstract The main part of cytosolic protein degradation depends on the ubiquitin-proteasome system. Proteasomes degrade their substrates into small peptide fragments, some of which are translocated into the endoplasmatic reticulum and loaded onto MHC class I molecules, which are then transported to the cell surface for inspection by CTL. A reliable prediction of proteasomal cleavages in a given protein for the identification of CTL epitopes would benefit immensely from additional cleavage data for the training of prediction algorithms. To increase the knowledge about proteasomal specificity and to gain more insight into the relation of proteasomal activity and susceptibility to prion diseas…

Proteasome Endopeptidase ComplexPrionsMolecular Sequence DataImmunologyCellProtein degradationPeptide MappingMultienzyme ComplexesMHC class ImedicineAnimalsHumansImmunology and AllergyAmino Acid SequencePeptide sequenceAllelesCell Line TransformedSheepbiologyHydrolysisMolecular biologyPeptide FragmentsRecombinant ProteinsCell biologyCysteine EndopeptidasesKineticsCytosolCTL*medicine.anatomical_structureProteasomeCell culturebiology.proteinDisease SusceptibilityThe Journal of Immunology
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The Cleavage Product of Amyloid-β Protein Precursor sAβPPα Modulates BAG3-Dependent Aggresome Formation and Enhances Cellular Proteasomal Activity

2015

Alzheimer's disease (AD) is the major age-associated form of dementia characterized by gradual cognitive decline. Aberrant cleavage of the amyloid-β protein precursor (AβPP) is thought to play an important role in the pathology of this disease. Two principal AβPP processing pathways exist: amyloidogenic cleavage of AβPP resulting in production of the soluble N-terminal fragment sAβPPβ, amyloid-β (Aβ), which accumulates in AD brain, and the AβPP intracellular domain (AICD) sAβPPα, p3 and AICD are generated in the non-amyloidogenic pathway. Prevalence of amyloidogenic versus non-amyloidogenic processing leads to depletion of sAβPPα and an increase in Aβ. Although sAβPPα is a well-accepted neu…

Proteasome Endopeptidase ComplexTime FactorsCell SurvivalLeupeptinsGreen Fluorescent ProteinsCysteine Proteinase InhibitorsProtein degradationProtein aggregationBiologyTransfectionBAG3Rats Sprague-DawleyAmyloid beta-Protein PrecursorAnimalsHumansRNA MessengerRNA Small InterferingProtein precursorCells CulturedAdaptor Proteins Signal TransducingNeuronsAmyloid beta-PeptidesDose-Response Relationship DrugGeneral NeuroscienceHEK 293 cellsBrainGeneral MedicineFibroblastsEmbryo MammalianRatsCell biologyPsychiatry and Mental healthClinical PsychologyHEK293 CellsProteostasisAggresomeGene Expression RegulationBiochemistryProteasomeProteolysisAmyloid Precursor Protein SecretasesGeriatrics and GerontologyApoptosis Regulatory ProteinsJournal of Alzheimer's Disease
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Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spa…

2006

Missense mutations in the humanPLP1gene lead to dysmyelinating diseases with a broad range of clinical severity, ranging from severe Pelizaeus–Merzbacher disease (PMD) to milder spastic paraplegia type 2 (SPG-2). The molecular pathology has been generally attributed to endoplasmic reticulum (ER) retention of misfolded proteolipid protein (PLP) (and its splice isoform DM20) and induction of the unfolded protein response. As opposed to previous studies of heterologous expression systems, we have analyzed PLP/DM20 trafficking in oligodendroglial cells, thereby revealing differences between PMD and SPG-2-associated PLP/DM20 isoforms. PLPA242Vand DM20A242V(jimpy-msdin mice), associated with seve…

Proteolipid protein 1Time FactorsLeupeptinsBlotting WesternGene Expressionchemical and pharmacologic phenomenaNerve Tissue ProteinsBiologyProtein degradationCysteine Proteinase InhibitorsTransfectionMiceMice Neurologic MutantsCricetulusMembrane MicrodomainsMutant proteinimmune system diseasesCricetinaeAnimalsImmunoprecipitationMyelin Proteolipid ProteinLipid raftCells CulturedGeneral NeuroscienceEndoplasmic reticulumCholesterol bindingER retentionArticlesImmunohistochemistryCell biologynervous system diseasesOligodendrogliaProtein TransportCholesterolBiochemistryUnfolded protein responselipids (amino acids peptides and proteins)Mutant ProteinsSubcellular FractionsThe Journal of neuroscience : the official journal of the Society for Neuroscience
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Protein modulation in mouse heart under acute and chronic hypoxia

2011

Exploring cellular mechanisms underlying beneficial and detrimental responses to hypoxia represents the object of the present study. Signaling molecules controlling adaptation to hypoxia (HIF-1α), energy balance (AMPK), mitochondrial biogenesis (PGC-1α), autophagic/apoptotic processes regulation and proteomic dysregulation were assessed. Responses to acute hypoxia (AH) and chronic hypoxia (CH) in mouse heart proteome were detected by 2-D DIGE, mass spectrometry and antigen-antibody reactions. Both in AH and CH, the results indicated a deregulation of proteins related to sarcomere stabilization and muscle contraction. Neither in AH nor in CH the HIF-1α stabilization was observed. In AH, the …

ProteomicsCell signalingProteomeImmunoblottingApoptosisBiologyProtein degradationBiochemistryTwo-Dimensional Difference Gel ElectrophoresisMiceContractile ProteinsHeat shock proteinmedicineAnimalsHypoxiaMolecular BiologyHeat-Shock ProteinsAnimalMyocardiumAutophagyAMPK / Animal proteomics / Apoptosis / Autophagy / Heart / HypoxiaApoptosiProteomicAMPKHeat-Shock ProteinHypoxia (medical)Hypoxia-Inducible Factor 1 alpha SubunitCell biologyGene Expression RegulationMitochondrial biogenesisBiochemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationAdenosylhomocysteinaseContractile Proteinmedicine.symptomEnergy MetabolismPROTEOMICS
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Karyopherin Msn5 is involved in a novel mechanism controlling the cellular level of cell cycle regulators Cln2 and Swi5

2019

ABSTRACT The yeast β-karyopherin Msn5 controls the SBF cell-cycle transcription factor, responsible for the periodic expression of CLN2 cyclin gene at G1/S, and the nuclear export of Cln2 protein. Here we show that Msn5 regulates Cln2 by an additional mechanism. Inactivation of Msn5 causes a severe reduction in the cellular content of Cln2. This occurs by a post-transcriptional mechanism, since CLN2 mRNA level is not importantly affected in asynchronous cultures. Cln2 stability is not significantly altered in msn5 cells and inactivation of Msn5 causes a reduction in protein level even when Cln2 is stabilized. Therefore, the reduced amount of Cln2 in msn5 cells is mainly due not to a higher …

Swi50301 basic medicineSaccharomyces cerevisiae ProteinsS. cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeKaryopherinsCell cycleBiologyProtein degradationCyclin Gene03 medical and health sciences0302 clinical medicineCyclinsGene Expression Regulation FungalPolysomeProtein biosynthesisNuclear export signalMolecular BiologyTranscription factorCyclinMsn5 karyopherinCell BiologyCell cycleActinsCell biologyCln2 cyclin030104 developmental biologyMutagenesisPolyribosomesProtein Biosynthesis030220 oncology & carcinogenesisTranscription FactorsResearch PaperDevelopmental BiologyCell Cycle
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Regulation of cell cycle transcription factor Swi5 by karyopherin Msn5

2012

AbstractInactivation of S. cerevisiae β-karyopherin Msn5 causes hypersensitivity to the overexpression of mitotic cyclin Clb2 and aggravates growth defects of many mutant strains in mitotic exit, suggesting a connection between Msn5 and mitotic exit. We determined that Msn5 controlled subcellular localization of the mitotic exit transcription factor Swi5, since it was required for Swi5 nuclear export. Msn5 physically interacted with the N-terminal end of Swi5. Inactivation of Msn5 caused a severe reduction in cellular levels of Swi5 protein. This effect occurred by a post-transcriptional mechanism, since SWI5 mRNA levels were not affected. The reduced amount of Swi5 in msn5 mutant cells was…

Swi5Saccharomyces cerevisiae ProteinsGenes FungalActive Transport Cell NucleusMitosisCell Cycle ProteinsSaccharomyces cerevisiaeKaryopherinsProtein degradationBiologyNuclear export signalMolecular BiologyMitosisTranscription factorKaryopherinMsn5Cell Nucleuschemistry.chemical_classificationProtein StabilityCell CycleCell BiologyCell cycleβ-karyopherinMolecular biologyCell biologyProtein TransportchemistryMitotic exitMutationNuclear transportProtein BindingSubcellular FractionsTranscription FactorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Protective effect of paraoxonase-2 against endoplasmic reticulum stress-induced apoptosis is lost upon disturbance of calcium homoeostasis

2008

PON2 (paraoxonase-2) is a ubiquitously expressed antioxidative protein which is largely found in the ER (endoplasmic reticulum). Addressing the cytoprotective functions of PON2, we observed that PON2 overexpression provided significant resistance to ER-stress-induced caspase 3 activation when the ER stress was induced by interference with protein modification (by tunicamycin or dithiothreitol), but not when ER stress was induced by disturbance of Ca2+ homoeostasis (by thapsigargin or A23187). When analysing the underlying molecular events, we found an activation of the PON2 promoter in response to all tested ER-stress-inducing stimuli. However, only tunicamycin and dithiothreitol resulted i…

ThapsigarginRNA StabilityApoptosisCaspase 3Protein degradationEndoplasmic ReticulumBiochemistryGene Expression Regulation EnzymologicCell Linechemistry.chemical_compoundStress PhysiologicalHomeostasisHumansEnzyme InhibitorsPromoter Regions Genetic3' Untranslated RegionsMolecular BiologyCalcimycinIonophoresbiologyAryldialkylphosphataseCalpainTunicamycinEndoplasmic reticulumCalpainCell BiologyTunicamycinCell biologyDithiothreitolchemistryApoptosisbiology.proteinUnfolded protein responseThapsigarginCalcium5' Untranslated RegionsBiochemical Journal
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Caspase-3 contributes to ZO-1 and Cl-5 tight-junction disruption in rapid anoxic neurovascular unit damage.

2011

BACKGROUND: Tight-junction (TJ) protein degradation is a decisive step in hypoxic blood-brain barrier (BBB) breakdown in stroke. In this study we elucidated the impact of acute cerebral ischemia on TJ protein arrangement and the role of the apoptotic effector protease caspase-3 in this context. METHODOLOGY/PRINCIPAL FINDINGS: We used an in vitro model of the neurovascular unit and the guinea pig whole brain preparation to analyze with immunohistochemical methods the BBB properties and neurovascular integrity. In both methodological approaches we observed rapid TJ protein disruptions after 30 min of oxygen and glucose deprivation or middle cerebral artery occlusion, which were accompanied by…

Time FactorsAnatomy and Physiologylcsh:MedicineMiceMolecular Cell BiologyPathologySignaling in Cellular ProcessesHypoxia Brainlcsh:ScienceCells CulturedNeuropathologyApoptotic SignalingMultidisciplinaryTight junctionCaspase 3ChemistryAnimal ModelsCell biologyTransport proteinProtein Transportmedicine.anatomical_structureNeurologyBlood-Brain BarrierMedicineResearch ArticleSignal TransductionClinical Research DesignCerebrovascular DiseasesGuinea PigsIschemiaContext (language use)Caspase 3Protein degradationBlood–brain barrierNeurological SystemTight JunctionsCapillary PermeabilityModel OrganismsDiagnostic MedicinemedicineAnimalsTransient Ischemic AttacksAnimal Models of DiseaseClaudinBiologyIschemic Strokelcsh:REndothelial CellsMembrane ProteinsPhosphoproteinsmedicine.diseaseAnatomical PathologyClaudinsImmunologyZonula Occludens-1 ProteinNervous System Componentslcsh:QPLoS ONE
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Synthetic retinoids dissociate coactivator binding from corepressor release.

2002

The ligand-activated retinoid receptors RXR and RAR control development, homeostasis and disease by regulating transcription of retinoic acid (RA) responsive target genes or crosstalk with other signalling pathways. According to the current model ligand-binding triggers an exchange between corepressor- and coactivator-complexes that inhibit or potentiate transcription by deacetylating and acetylating nucleosomal histones, respectively. Additional cofactors may modify the transcriptional regulatory process by linking liganded retinoid receptors to structural components of chromatin or protein degradation. The desire to specifically influence defined events in RA-signalling, while others are …

Transcriptional Activationmedicine.drug_classReceptors Retinoic AcidAmino Acid MotifsProtein degradationRetinoid X receptorBiologyLigandsBiochemistryRetinoidsCoactivatorChlorocebus aethiopsmedicineAnimalsHumansNuclear Receptor Co-Repressor 1Protein IsoformsNuclear Receptor Co-Repressor 2RetinoidMolecular BiologyNuclear receptor co-repressor 2PELP-1Binding SitesRetinoid X receptor alphaRetinoic Acid Receptor alphaNuclear ProteinsCell BiologyCell biologyDNA-Binding ProteinsRepressor ProteinsBiochemistryGene Expression RegulationCOS CellsMutagenesis Site-DirectedCorepressorHeLa CellsJournal of receptor and signal transduction research
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