Search results for "Cytoplasmic inclusion"

showing 7 items of 7 documents

Loss of ISWI Function in Drosophila Nuclear Bodies Drives Cytoplasmic Redistribution of Drosophila TDP-43

2018

Over the past decade, evidence has identified a link between protein aggregation, RNA biology, and a subset of degenerative diseases. An important feature of these disorders is the cytoplasmic or nuclear aggregation of RNA-binding proteins (RBPs). Redistribution of RBPs, such as the human TAR DNA-binding 43 protein (TDP-43) from the nucleus to cytoplasmic inclusions is a pathological feature of several diseases. Indeed, sporadic and familial forms of amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration share as hallmarks ubiquitin-positive inclusions. Recently, the wide spectrum of neurodegenerative diseases characterized by RBPs functions’ alteration and loss was coll…

0301 basic medicineCytoplasmCytoplasmic inclusionFluorescent Antibody TechniqueProtein aggregationHeterogeneous ribonucleoprotein particleHeterogeneous-Nuclear Ribonucleoproteinslcsh:Chemistry0302 clinical medicineDrosophila Proteinsneurodegenerative diseasesnuclear bodylcsh:QH301-705.5SpectroscopyGeneral MedicinehnRNPsComputer Science ApplicationsCell biologyChromatinTransport proteinDNA-Binding ProteinsProtein Transportmedicine.anatomical_structureDrosophilaDrosophila ProteinProtein BindingImitation SWIBiologyCatalysisArticleInorganic Chemistryomega speckles03 medical and health sciencesmedicineAnimalsPhysical and Theoretical ChemistryMolecular BiologyGenetic Association StudiesCell NucleusOrganic Chemistryta1182Chromatin Assembly and DisassemblyCell nucleus030104 developmental biologylcsh:Biology (General)lcsh:QD1-999gene expression<i>Drosophila</i>; nuclear body; omega speckles; dTDP-43; hnRNPs; omega speckles; neurodegenerative diseases; gene expression; gene regulationdTDP-43gene regulation030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
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Myelin changes in Alexander disease

2018

Introduction: Alexander disease (AxD) is a type of leukodystrophy. Its pathological basis, along with myelin loss, is the appearance of Rosenthal bodies, which are cytoplasmic inclusions in astrocytes. Mutations in the gene coding for glial fibrillary acidic protein (GFAP) have been identified as a genetic basis for AxD. However, the mechanism by which these variants produce the disease is not understood. Development: The most widespread hypothesis is that AxD develops when a gain-of-function mutation causes an increase in GFAP. However, this mechanism does not explain myelin loss, given that experimental models in which GFAP expression is normal or mutated do not exhibit myelin disorders. …

0301 basic medicineMutationGlial fibrillary acidic proteinbiologyMechanism (biology)Cytoplasmic inclusionLeukodystrophymedicine.diseasemedicine.disease_causelcsh:RC346-429Alexander diseaseCell biology03 medical and health sciencesMyelin030104 developmental biology0302 clinical medicinemedicine.anatomical_structurenervous systembiology.proteinmedicineEpigeneticslcsh:Neurology. Diseases of the nervous system030217 neurology & neurosurgeryNeurología (English Edition)
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Neuraminidase deficiency presenting as non-immune hydrops fetalis

1984

A newborn infant with oedema, ascites and hepatosplenomegaly is described. In ascites fluid foamy macrophages were found, in a liver biopsy cytoplasmic inclusions and membrane-bound vacuoles were seen. Furthermore the child excreted excessive amounts of sialic acid-rich oligosaccharides in the urine, and therefore a neurovisceral degenerative disorder was assumed. The diagnosis of sialidosis was confirmed by enzymatic assay in cultured fibroblasts, in which a complete deficiency of the lysosomal enzyme neuraminidase could be demonstrated. After recurrent septicaemias the child became dystrophic and died at the age of 6 months. Our case is compared with sialidosis observed by other authors, …

Cytoplasmic inclusionHepatosplenomegalyNeuraminidaseOligosaccharidesMucolipidosesalpha-MannosidaseHydrops fetalisMannosidasesAscitesLeukocytesmedicineLysosomal storage diseaseEdemaHumansSialidosisalpha-L-Fucosidasemedicine.diagnostic_testbiologybusiness.industryInfant NewbornFibroblastsbeta-Galactosidasemedicine.diseasebeta-N-AcetylhexosaminidasesHexosaminidasesLiverLiver biopsyPediatrics Perinatology and Child HealthImmunologybiology.proteinFemalemedicine.symptomLysosomesbusinessNeuraminidaseEuropean Journal of Pediatrics
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Strange vesicles with a homogeneous content in spermatocytes and spermatids of a click beetle, Adelocera murina (Elateridae). A fine structure study

1996

Abstract The restructuring of primary spermatocytes of Adelocera murina, a click beetle, is described using electron microscopy of ultrathin sections. Emphasis is on spherical or rod-shaped cytoplasmic inclusions, invested by a unit membrane. The content of the inclusions is slightly more electron-dense than that of the surrounding cytoplasm and homogeneously textured in most cases. The inclusions are missing in spermatogonia but are abundant in prophase I through anaphase I spermatocytes. Their number declines in telophase I. Very similar elements are associated with the distal ends of the outgrowing flagella in metaphase I through telophase I spermatocytes and form the so-called flagellar…

GeneticsSpermiogenesisCytoplasmic inclusionVesicleGeneral Physics and AstronomyCell BiologyBiologyCell biologyMeiosisStructural BiologyCytoplasmBasal bodyGeneral Materials ScienceTelophaseAnaphaseMicron
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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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Crystal inclusions in subepithelial fibroblasts of the brood pouch of sea horses (hippocampus kuda)

1968

In the subepithelial connective tissue of the inactive broodpouch of sea horses (Hippocampus kuda), fibroblasts with striking crystal inclusions are described light microscopically and electron microscopically in the tunica adventitia of capillaries. These very electron dense crystals turn out to be hexagonal prisms of heterogeneous structures. Results of the X-ray microanalysis and comparison with other crystalline cell inclusions so far described allow the conclusion that they contain an iron protein stored as crystals. The structure and genesis of these crystals as well as the possible importance of the iron protein for the biology of these animals are discussed.

MaleCytoplasmPathologymedicine.medical_specialtybiologyHexagonal crystal systemCytoplasmic inclusionTunica AdventitiaFishesConnective tissueHippocampus kudaFibroblastsbiology.organism_classificationEpitheliumCrystalMicroscopy Electronmedicine.anatomical_structuremedicineAnimalsMicroscopy Phase-ContrastAnatomyCrystallizationBrood pouchMolecular BiologyJournal of Ultrastructure Research
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A Deletion of the Nuclear Localization Signal Domain in the Fus Protein Induces Stable Post-stress Cytoplasmic Inclusions in SH-SY5Y Cells

2021

Mutations in Fused-in-Sarcoma (FUS) gene involving the nuclear localization signal (NLS) domain lead to juvenile-onset Amyotrophic Lateral Sclerosis (ALS). The mutant protein mislocalizes to the cytoplasm, incorporating it into Stress Granules (SG). Whether SGs are the first step to the formation of stable FUS-containing aggregates is still unclear. In this work, we used acute and chronic stress paradigms to study the SG dynamics in a human SH-SY5Y neuroblastoma cell line carrying a deletion of the NLS domain of the FUS protein (homozygous: ΔNLS–/–; heterozygous: ΔNLS+/–). Wild-type (WT) cells served as controls. We evaluated the subcellular localization of the mutant protein through immuno…

amyotrophic lateral sclerosisstomatognathic systemGeneral Neurosciencecytoplasmic inclusionsNeurosciences. Biological psychiatry. NeuropsychiatrySettore MED/26 - Neurologianuclear localization signal (NLS)stress granules (SG)Fused-in-Sarcoma proteinRC321-571NeuroscienceOriginal Research
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