Search results for "Inclusion bodie"

showing 10 items of 53 documents

De novo expression of nonhepatocellular cytokeratins in Mallory body formation.

1998

Mallory bodies (MBs) are eosinophilic cytoplasmic inclusions observed predominantly in alcoholic liver disease. Although linked to disease activity, their pathogenesis is still unclear. Since intermediate filaments (cytokeratins) are major components of MBs, their cytokeratin polypeptide composition was analysed with monospecific antibodies for cytokeratins 7, 8, 14, 18, 19, and 20 by immunohistology. MBs were identified by light microscopy and ubiquitin immunostaining. All MBs were positive for cytokeratins 8 and 18. A significant percentage of the MBs was strongly positive for cytokeratins 19 and/or 20, which are not detectable in hepatocytes of normal liver and, in the case of cytokerati…

Liver CirrhosisPathologymedicine.medical_specialtyanimal structuresCarcinoma HepatocellularCytoplasmic inclusionmacromolecular substancesBiologyPathology and Forensic MedicineCytokeratinHepatolenticular DegenerationmedicineMallory bodyHumansIntermediate filamentChildMolecular BiologyLiver Diseases AlcoholicInclusion BodiesLiver DiseasesLiver NeoplasmsAntibodies MonoclonalCell BiologyGeneral Medicinemedicine.diseaseImmunohistochemistryStainingLiverImmunohistochemistryKeratinsEctopic expressionImmunostainingVirchows Archiv : an international journal of pathology
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Neonatal form of nemaline myopathy, muscle immaturity, and a microvascular injury.

1990

An infant with a neonatal form of nemaline myopathy showed ultrastructural features of muscle immaturity. Immaturity was characterized by an abnormal presence of myotubes, as well as cells in clusters within a common basement membrane and a great number of satellite cells adhering to very small muscle fibers. In addition, degenerative changes and a severe microvascular lesion were observed. The pathologic findings in the muscle of this patient were those of neonatal nemaline myopathy complicating severe microvascular injury, possibly induced by an unknown toxic agent. ( J Child Neurol 1990;5:122-126).

Pathologymedicine.medical_specialtyMuscle HypotoniaBiopsyIschemiaBiologyMuscle Smooth VascularLesion03 medical and health sciences0302 clinical medicineNemaline myopathyMyofibrilsIschemia030225 pediatricsBiopsymedicineHumansBasement membraneInclusion BodiesAsphyxia NeonatorumRespiratory Distress Syndrome Newbornmedicine.diagnostic_testMyogenesisMicrocirculationMusclesInfant NewbornDisseminated Intravascular Coagulationmedicine.diseaseMicroscopy ElectronMuscular Atrophymedicine.anatomical_structurePediatrics Perinatology and Child HealthMuscle HypotoniaFemaleNeurology (clinical)medicine.symptomMyofibril030217 neurology & neurosurgeryJournal of child neurology
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Desmin-related neuromuscular disorders

1995

Desmin, the intermediate filament protein of skeletal muscle fibers, cardiac myocytes, and certain smooth muscle cells, is a member of the cytoskeleton linking Z-bands with the plasmalemma and the nucleus. The pathology of desmin in human neuromuscular disorders is always marked by increased amounts, diffusely or focally. Desmin is highly expressed in immature muscle fibers, both during fetal life and regeneration as well as in certain congenital myopathies, together with vimentin. Desmin is also enriched in neonatal myotonic dystrophy and small fibers in infantile spinal muscular atrophy. Focal accretion of desmin may be twofold, in conjunction with certain inclusion bodies, cytoplasmic an…

Pathologymedicine.medical_specialtyPhysiologyIntermediate FilamentsMuscle ProteinsVimentinmacromolecular substancesDesminCellular and Molecular NeuroscienceMuscular DiseasesPhysiology (medical)medicineHumansMyocyteIntermediate Filament ProteinMuscle SkeletalMyopathyIntermediate filamentActinInclusion BodiesbiologyNeuromuscular Diseasesbiology.proteinDesminNeurology (clinical)medicine.symptomDystrophinMuscle & 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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Primary desminopathies.

2007

•  Introduction •  Desmin is an essential component of the extrasarcomeric cytoskeleton in striated muscle cells •  Distal myopathy,cardiac arrhythmias,cardiomyopathy:classical criteria of primary desminopathies •  Sub-sarcolemmal and cytoplasmic desmin-positive protein aggregates:the morphological hallmark of primary and secondary desminopathies •  The spectrum of pathogenic desmin gene mutations •  The molecular pathogenesis of primary desminopathies: some answers gained,but even more questions raised •  Diagnostic work-up to distinguish primary from secondary desminopathies •  Treatment and clinical management of primary desminopathy patients Abstract Mutations of the human desmin gene o…

Pathologymedicine.medical_specialtyintermediate filamentsCardiomyopathyReviewsgranulofilamentous materialdesmininclusion bodiesmacromolecular substancesBiologymyofibrillar myopathyprotein aggregationdesmin-related myopathySarcolemmaMuscular DiseasesmedicineMyocyteAnimalsHumansIntermediate filamentMyopathyMuscle SkeletalCytoskeletonGenetic heterogeneityCardiac muscleCell Biologymedicine.diseasemusculoskeletal systemmutationsmedicine.anatomical_structuredesminopathyMutationMolecular MedicineDesminmedicine.symptomMyofibrilJournal of cellular and molecular medicine
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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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Ergastoplasmic paracrystalline inclusion bodies in the adipose gonadal envelope and fat body of the glow worm, Lampyris noctiluca (Insecta, Coleopter…

2001

Abstract The gonads of glow worm larvae are enveloped by adipose tissue which represents a specialized fat body. The adipose gonadal envelope, and also to a lesser extent the fat body cells, contain tubular paracrystalline inclusion bodies (PIBs). Cells of other tissues are devoid of such inclusions. The PIBs form in the cisternae of rough ER. In young larvae PIB formation is sparse, but at advanced larval stages PIBs often occur as bundles in stacks of ergastoplasm. Typically, a PIB within a cisterna consists of four to seven parallel tubules. The outer diameter of a tubule is ca 28.8 nm and the width of the tubule lumen ca 12.2 nm. The “wall” of a tubule contains globular protein subunits…

Inclusion BodiesEndoplasmic reticulumFat BodyGeneral Physics and AstronomyAdipose tissueCell BiologyAnatomyBiologyParacrystallineCisternabiology.organism_classificationInclusion bodieslaw.inventionCell biologyColeopteraTubuleAdipose TissueStructural BiologylawLampyris noctilucaAnimalsGeneral Materials ScienceElectron microscopeGonadsMicron (Oxford, England : 1993)
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Crystalloid lysozyme inclusions in Paneth cells of vitamin A-deficient rats.

1990

The effect of vitamin A-deficiency on jejunal Paneth cells in rats was investigated. Crystalloid particles were observed in secretion granules of Paneth cells from 6 out of 8 rats with vitamin A-deficiency. The particles were similar to those found in Paneth cells under other experimental conditions. Using an immuno-electron-microscopic technique we demonstrated a clear lysozyme immunoreactivity of these particles. In 2 vitamin A-deficient rats tubular structures have been detected in addition to the crystalloid particles. Crystalloid particles or tubular structures were not detectable in a control group of 8 vitamin A-supplemented rats. The morphological alterations of Paneth cells may be …

VitaminMalemedicine.medical_specialtyHistologyBiologydigestive systemPathology and Forensic Medicinechemistry.chemical_compoundImmunityInternal medicinemedicineAnimalsSecretionInclusion BodiesVitamin A DeficiencyRetinolRats Inbred StrainsCell BiologyMolecular medicineImmunohistochemistryRatsmedicine.anatomical_structureEndocrinologyJejunumchemistryBiochemistryPaneth cellUltrastructureLysozymeLysosomesCell and tissue research
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Phasor-FLIM analysis of Thioflavin T self-quenching in Concanavalin amyloid fibrils

2020

The formation of amyloid structures has traditionally been related to human neurodegenerative pathologies and, in recent years, the interest in these highly stable nanostructures was extended to biomaterial sciences. A common method to monitor amyloid growth is the analysis of Thioflavin T fluorescence. The use of this highly selective dye, diffused worldwide, allows mechanistic studies of supramolecular assemblies also giving back important insight on the structure of these aggregates. Here we present experimental evidence of self-quenching effect of Thioflavin T in presence of amyloid fibrils. A significant reduction of fluorescence lifetime of this dye which is not related to the propert…

Fluorescence-lifetime imaging microscopyAmyloidFLIMHistologyAmyloid02 engineering and technologyProtein aggregationprotein aggregation03 medical and health scienceschemistry.chemical_compound0302 clinical medicineself-quenchingmental disordersamyloid fibrilConcanavalin Afluorescence lifetimeHumansBenzothiazolesInstrumentationFluorescent DyesInclusion BodiesQuenching (fluorescence)biologyStaining and LabelingChemistryOptical ImagingPhasorNeurodegenerative Diseases030206 dentistry021001 nanoscience & nanotechnologyFluorescenceSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Medical Laboratory TechnologyMicroscopy FluorescenceConcanavalin APhasorbiology.proteinBiophysicsThioflavin TThioflavinamyloid fibrils Concanavalin A FLIM fluorescence lifetime Phasor protein aggregation self-quenching Thioflavin TAnatomy0210 nano-technology
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Assembly of fluorescent chimeric virus-like particles of canine parvovirus in insect cells

2004

Canine parvovirus (CPV) is a small non-enveloped ssDNA virus composed of the viral proteins VP1, VP2, and VP3 with a T=1 icosahedral symmetry. VP2 is nested in VP1 and the two proteins are produced by differential splicing of a primary transcript of the right ORF of the viral genome. The VP2 protein can be further proteolytically cleaved to form VP3. Previous studies have shown that VP1 and VP3 are unnecessary for capsid formation and consequently, that VP2 alone is sufficient for assembly. We have hypothesized that insertion of the enhanced green fluorescent protein (EGFP) at the N-terminus of VP2 could be carried out without altering assembly. To investigate the possibility to develop flu…

Parvovirus CanineRecombinant Fusion ProteinsvirusesGreen Fluorescent ProteinsBiophysicsHeterologousFluorescence correlation spectroscopySpodopteraBiochemistryVirusCell LineInclusion Bodies ViralGreen fluorescent proteinAnimalsAmino Acid SequenceMolecular BiologyMicroscopy ConfocalBase SequencebiologyChimeraVirus AssemblyCanine parvovirusvirus diseasesCell Biologybiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyFusion proteinLuminescent ProteinsMicroscopy ElectronCapsidRNA splicingCapsid ProteinsPlasmidsBiochemical and Biophysical Research Communications
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