Search results for " inclusion bodies"

showing 8 items of 8 documents

Aerobic growth of Rhodococcus aetherivorans BCP1 using selected naphthenic acids as the sole carbon and energy sources

2018

Naphthenic acids (NAs) are an important group of toxic organic compounds naturally occurring in hydrocarbon deposits. This work shows that Rhodococcus aetherivorans BCP1 cells not only utilize a mixture of eight different NAs (8XNAs) for growth but they are also capable of marked degradation of two model NAs, cyclohexanecarboxylic acid (CHCA) and cyclopentanecarboxylic acid (CPCA) when supplied at concentrations from 50 to 500 mgL−1 . The growth curves of BCP1 on 8XNAs, CHCA, and CPCA showed an initial lag phase not present in growth on glucose, which presumably was related to the toxic effects of NAs on the cell membrane permeability. BCP1 cell adaptation responses that allowed survi…

0301 basic medicineMicrobiology (medical)Inclusion bodie030106 microbiologylcsh:QR1-502Settore BIO/19 - Microbiologia Generale7. Clean energyMicrobiologylcsh:Microbiology03 medical and health scienceschemistry.chemical_compoundBiosynthesisRhodococcus aetherivorans naphthenic acids stress response b-oxidation transmission electron microscopy fatty acids methyl esters inclusion bodiesnaphthenic acidsBeta oxidationchemistry.chemical_classificationbiologyStress responseRhodococcus aetherivoranNaphthenic acidCyclohexanecarboxylic acidbiology.organism_classificationRhodococcus aetherivoranschemistryBiochemistryFatty acids methyl esterβ-oxidationfatty acids methyl estersEnergy sourceRhodococcusBacteriaIntracellularTransmission electron microscopyPolyunsaturated fatty acid
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Nuclear inclusions of pathogenic ataxin-1 induce oxidative stress and perturb the protein synthesis machinery

2020

Spinocerebellar ataxia type-1 (SCA1) is caused by an abnormally expanded polyglutamine (polyQ) tract in ataxin-1. These expansions are responsible for protein misfolding and self-assembly into intranuclear inclusion bodies (IIBs) that are somehow linked to neuronal death. However, owing to lack of a suitable cellular model, the downstream consequences of IIB formation are yet to be resolved. Here, we describe a nuclear protein aggregation model of pathogenic human ataxin-1 and characterize IIB effects. Using an inducible Sleeping Beauty transposon system, we overexpressed the ATXN1(Q82) gene in human mesenchymal stem cells that are resistant to the early cytotoxic effects caused by the expr…

0301 basic medicineSCA1 Spinocerebellar ataxia type-1Intranuclear Inclusion BodiesClinical BiochemistryMSC mesenchymal stem cellProtein aggregationBiochemistry0302 clinical medicineMutant proteinProtein biosynthesisDE differentially expressed genesNuclear proteinlcsh:QH301-705.5FTIR Fourier-transform infrared spectroscopyAtaxin-1lcsh:R5-920biologyChemistryNuclear ProteinspolyQ polyglutamineRibosomeCell biologySB Sleeping BeautyRibosome ; Polyglutamine ; Ataxin-1 ; Oxidative stress ; Transposon ; Sleeping beauty transposon ; Protein networkSpinocerebellar ataxiaProtein foldingCellular modelFunction and Dysfunction of the Nervous Systemlcsh:Medicine (General)Research PaperiPSC induced pluripotent stem cellAtaxin 1Nerve Tissue ProteinsPPI protein-protein interaction03 medical and health sciencesROS reactive oxygen speciesProtein networkSleeping beauty transposonGSEA Gene Set Enrichment AnalysismedicineHumansNPC neural progenitor cellOrganic Chemistrymedicine.diseaseAFM atomic force microscopyOxidative Stress030104 developmental biologylcsh:Biology (General)IIBs intranuclear inclusion bodiesMS mass spectrometryCardiovascular and Metabolic Diseasesbiology.proteinPolyglutamine030217 neurology & neurosurgery
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ALS-linked FUS mutations confer loss and gain of function in the nucleus by promoting excessive formation of dysfunctional paraspeckles

2019

Mutations in the FUS gene cause amyotrophic lateral sclerosis (ALS-FUS). Mutant FUS is known to confer cytoplasmic gain of function but its effects in the nucleus are less understood. FUS is an essential component of paraspeckles, subnuclear bodies assembled on a lncRNA NEAT1. Paraspeckles may play a protective role specifically in degenerating spinal motor neurons. However it is still unknown how endogenous levels of mutant FUS would affect NEAT1/paraspeckles. Using novel cell lines with the FUS gene modified by CRISPR/Cas9 and human patient fibroblasts, we found that endogenous levels of mutant FUS cause accumulation of NEAT1 isoforms and paraspeckles. However, despite only mild cytoplasm…

Cell NucleusResearchAmyotrophic Lateral SclerosisIntranuclear Inclusion BodiesNEAT1lcsh:RC346-429Cell LineLoss of Function MutationCell Line TumorFused in sarcoma (FUS)ParaspeckleHumansProtein IsoformsRNA-Binding Protein FUSRNA Long NoncodingAmyotrophic lateral sclerosis (ALS)CRISPR-Cas Systemslcsh:Neurology. Diseases of the nervous systemActa Neuropathologica Communications
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Intranuclear nemaline rod myopathy

2006

The clinical, pathologic, and genetic findings of a boy with intranuclear nemaline rod myopathy are described. Serial muscle biopsies revealed myocyte nuclei containing inclusions that were immunoreactive for α-actinin and increased with age. Genetic analysis revealed a Val163Leu ACTA1 mutation previously associated with nemaline rod myopathy. Although initially delayed, he has reached all milestones and remains stable. These findings suggest intranuclear rods may increase with time and do not necessarily imply a poor prognosis. Muscle Nerve, 2006

MalePoor prognosisPathologymedicine.medical_specialtyPhysiologyBiopsyIntranuclear Inclusion BodiesMyopathies Nemalinemedicine.disease_causeCellular and Molecular NeuroscienceNemaline myopathyPhysiology (medical)BiopsymedicineHumansMyocyteIntranuclear Nemaline Rod MyopathyChildMuscle SkeletalMyopathyActinCell NucleusMutationmedicine.diagnostic_testbusiness.industrymedicine.diseaseNeurology (clinical)medicine.symptombusinessMuscle & Nerve
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The Tempered Polymerization of Human Neuroserpin

2012

Neuroserpin, a member of the serpin protein superfamily, is an inhibitor of proteolytic activity that is involved in pathologies such as ischemia, Alzheimer's disease, and Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB). The latter belongs to a class of conformational diseases, known as serpinopathies, which are related to the aberrant polymerization of serpin mutants. Neuroserpin is known to polymerize, even in its wild type form, under thermal stress. Here, we study the mechanism of neuroserpin polymerization over a wide range of temperatures by different techniques. Our experiments show how the onset of polymerization is dependent on the formation of an intermediate mon…

Models MolecularProtein FoldingAmyloidScienceNeuroserpinBiophysicsSerpinBiochemistryAggregationchemistry.chemical_compoundNeuroserpinmedicineHumansPolumerization; Aggregation; Neuroserpin; FENIB; Light scatteringFamilial encephalopathy with neuroserpin inclusion bodiesBiologySerpinschemistry.chemical_classificationMultidisciplinaryPolumerizationPhysicsNeuropeptidesQTemperatureRLight scatteringProteinsPolymermedicine.diseaseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)EnzymesKineticsMonomerchemistryPolymerizationBiochemistryFENIBBiophysicsMedicineProtein foldingProtein MultimerizationResearch ArticlePLoS ONE
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Nuclear actin aggregation is a hallmark of anti-synthetase syndrome-induced dysimmune myopathy

2015

Objective: To analyze antisynthetase syndrome–associated myositis by modern myopathologic methods and to define its place in the spectrum of idiopathic inflammatory myopathies (IIMs). Methods: Skeletal muscle biopsies from antisynthetase syndrome–associated myositis and other IIMs from different institutions worldwide were analyzed by histopathology, quantitative PCR, and electron microscopy. Results: Myonuclear actin filament inclusions were identified as a unique morphologic hallmark of antisynthetase syndrome–associated myositis. Nuclear actin inclusions were never found in dermatomyositis, polymyositis, sporadic inclusion body myositis, autoimmune necrotizing myopathy associated with si…

Pathologymedicine.medical_specialtyBiopsyIntranuclear Inclusion Bodies10208 Institute of Neuropathology610 Medicine & healthAntisynthetase syndromeBiologyPolymyositisSensitivity and SpecificityNecrosisPerimysialmedicineHumansMyopathyMuscle SkeletalMyositisMyositisDermatomyositisActin cytoskeletonmedicine.diseaseAutoimmune necrotizing myopathyActins10040 Clinic for NeurologyActin Cytoskeleton2728 Neurology (clinical)Immunology570 Life sciences; biologyNeurology (clinical)medicine.symptom
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Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics

2015

Neuroserpin (NS) is a serine protease inhibitor (SERPIN) involved in different neurological pathologies, including the Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB), related to the aberrant polymerization of NS mutants. Here we present an in vitro and in silico characterization of native neuroserpin and its dysfunctional conformation isoforms: the proteolytically cleaved conformer, the inactive latent conformer, and the polymeric species. Based on circular dichroism and fluorescence spectroscopy, we present an experimental validation of the latent model and highlight the main structural features of the different conformers. In particular, emission spectra of aromatic res…

Protein FoldingCircular dichroismSerine Proteinase InhibitorsProtein ConformationStereochemistryNeuroserpinBiophysicsEpilepsies MyoclonicMolecular Dynamics SimulationSerpinMolecular DynamicsBiochemistryProtein Structure SecondaryArticleFluorescenceAnalytical ChemistryMolecular dynamicsProtein structureNeuroserpinmedicineHumansProtein IsoformsFluorescence emission spectra; circular dichroism; neuroserpin latent conformationneuroserpin latent conformationFamilial encephalopathy with neuroserpin inclusion bodiesMolecular BiologyConformational isomerismSerpinsFluorescence emission spectraSerpinChemistryCircular DichroismConformational diseaseNeuropeptidesHydrogen Bondingmedicine.diseaseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Heredodegenerative Disorders Nervous SystemProtein foldingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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PML nuclear body-residing proteins sequentially associate with HPV genome after infectious nuclear delivery.

2019

Subnuclear promyelocytic leukemia (PML) nuclear bodies (NBs) are targeted by many DNA viruses after nuclear delivery. PML protein is essential for formation of PML NBs. Sp100 and Small Ubiquitin-Like Modifier (SUMO) are also permanently residing within PML NBs. Often, large DNA viruses disassemble and reorganize PML NBs to counteract their intrinsic antiviral activity and support establishment of infection. However, human papillomavirus (HPV) requires PML protein to retain incoming viral DNA in the nucleus for subsequent efficient transcription. In contrast, Sp100 was identified as a restriction factor for HPV. These findings suggested that PML NBs are important regulators of early stages o…

Viral DiseasesPhysiologyvirusesIntranuclear Inclusion BodiesPromyelocytic Leukemia ProteinVirus ReplicationBiochemistryAutoantigensImmune PhysiologyMedicine and Health SciencesCell Cycle and Cell DivisionNuclear proteinBiology (General)PapillomaviridaeStaining0303 health sciencesViral GenomicsImmune System ProteinsChromosome Biology030302 biochemistry & molecular biologyCell StainingTotal Cell CountingNuclear Proteinsvirus diseasesAntigens NuclearGenomicsCell biologymedicine.anatomical_structureInfectious DiseasesCapsidCell ProcessesViral GenomeCellular Structures and OrganellesIntranuclear SpaceResearch ArticleHuman Papillomavirus InfectionQH301-705.5UrologyImmunologyCell Enumeration TechniquesSUMO-1 ProteinSexually Transmitted DiseasesMitosisMicrobial GenomicsGenome ViralBiologyResearch and Analysis MethodsMicrobiologyVirusAntibodies03 medical and health sciencesPromyelocytic leukemia proteinVirologyNuclear BodiesmedicineGeneticsHumansVesiclesMolecular BiologyMitosisTranscription factor030304 developmental biologyCell NucleusGenitourinary InfectionsTumor Suppressor ProteinsBiology and Life SciencesProteinsCell BiologyRC581-607Cell nucleusViral replicationSpecimen Preparation and Treatmentbiology.proteinParasitologyCapsid ProteinsImmunologic diseases. AllergyTranscription FactorsPLoS Pathogens
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