Search results for "inclusion bodies"

showing 10 items of 53 documents

Adult polyglucosan body myopathy.

1992

This report describes a sporadic late-onset myopathy in two unrelated adults which was marked by polyglucosan inclusions surrounded by abnormally structured mitochondria, the latter finding a localized, possibly reactive phenomenon. The polyglucosan material was characterized by a battery of histochemical and enzyme histochemical techniques; revealed common antigenicity with Lafora bodies, corpora amylacea and muscle fiber inclusions in types IV and VII glycogenoses; and contained ubiquitin. Additional lectin histochemical and associated digestion preparations disclosed the presence of alpha-glycosyl residues as apparently the sole carbohydrate component in polyglucosan bodies while the abo…

MaleAntigenicityPathologymedicine.medical_specialtyMolecular Sequence DataCarbohydratesPathology and Forensic MedicineCellular and Molecular NeuroscienceUbiquitinMuscular DiseasesPolysaccharidesLectinsmedicineHumansSymptom onsetMuscle fibreMyopathyLafora bodyInclusion BodiesbiologyMusclesLectinGeneral MedicineHypertrophyMiddle AgedMitochondria MuscleMicroscopy ElectronNeurologyBiochemistryCarbohydrate Sequencebiology.proteinFemaleNeurology (clinical)medicine.symptomAtrophyCorpora amylaceaJournal of neuropathology and experimental neurology
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The deletion of six amino acids at the C-terminus of the alpha 1 (II) chain causes overmodification of type II and type XI collagen: further evidence…

1996

We have identified an 18 bp deletion in exon 49 of the type II procollagen gene (COL2A1) in a patient with Kniest dysplasia. The deletion is located at the very C-terminus of the helical domain and removes two of three Gly-Pro-Pro triplets at positions 1007-1012, which are thought to be involved in helix formation and stability. Morphological investigation of an iliac crest biopsy showed large inclusions in the endoplasmic reticulum of chondrocytes, reflecting impaired secretion of type II collagen. Electrophoretic analysis of collagens extracted from cartilage or synthesised by cultured chondrocytes showed that type II and also type XI procollagen molecules containing mutant alpha 1 (II) c…

MaleDNA Mutational AnalysisMolecular Sequence DataMutantType II collagenBiologyOsteochondrodysplasiasChondrocyteIliumExonKniest dysplasiaGeneticsmedicineHumansAmino Acid SequencePeptide sequenceCells CulturedGenetics (clinical)Sequence DeletionInclusion BodiesGeneticsBase SequenceC-terminusExonsmedicine.diseaseMolecular biologyProcollagen peptidaseCartilagemedicine.anatomical_structureGenesChild PreschoolCollagenEndoplasmic Reticulum RoughProcollagenResearch ArticleJournal of Medical Genetics
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Gastric α-synuclein immunoreactive inclusions in Meissner's and Auerbach's plexuses in cases staged for Parkinson's disease-related brain pathology

2005

The progressive degenerative process associated with sporadic Parkinson's disease (sPD) is characterized by formation of alpha-synuclein-containing inclusion bodies in a few types of projection neurons in both the enteric and central nervous systems (ENS and CNS). In the brain, the process apparently begins in the brainstem (dorsal motor nucleus of the vagal nerve) and advances through susceptible regions of the basal mid-and forebrain until it reaches the cerebral cortex. Anatomically, all of the vulnerable brain regions are closely interconnected. Whether the pathological process begins in the brain or elsewhere in the nervous system, however, is still unknown. We therefore used immunocyt…

MaleNervous systemProtein FoldingPathologymedicine.medical_specialtyPrionsModels NeurologicalCentral nervous systemMyenteric PlexusBiologyAxonal TransportCentral nervous system diseaseNeural PathwaysDisease Transmission InfectiousmedicineHumansAgedAged 80 and overInclusion BodiesNeuronsGeneral NeuroscienceBrainParkinson DiseaseVagus NerveSubmucous PlexusMiddle Agedmedicine.diseasemedicine.anatomical_structureDorsal motor nucleusGastric MucosaCerebral cortexForebrainalpha-SynucleinFemaleEnteric nervous systemBrainstemNerve NetNeuroscienceNeuroscience Letters
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Ultrastructural Pathology of Eccrine Sweat Gland Epithelial Cells in Globoid Cell Leukodystrophy

1993

Three of four children were recognized by deficient β-galactocerebrosidase activities as having globoid cell leukodystrophy inclusions in sweat gland epithelial cells, similar in ultrastructure to those seen in Schwann cells. This observation in globoid cell leukodystrophy emphasizes the need to include sweat gland epithelial cells in examinations of skin in globoid cell leukodystrophy, as well as in any neurometabolic disorder. ( J Child Neurol 1993;8:171-174).

MalePathologymedicine.medical_specialtyBiopsyCellEccrine GlandsBiologyEpitheliumInclusion bodiesUltrastructural Pathology03 medical and health sciences0302 clinical medicine030225 pediatricsSweat glandmedicineHumansEccrine sweat glandChildSkinInclusion Bodiesintegumentary systemLeukodystrophyInfantLipid Metabolismmedicine.diseaseEpitheliumLeukodystrophy Globoid CellMicroscopy Electronmedicine.anatomical_structureChild PreschoolVacuolesPediatrics Perinatology and Child HealthUltrastructureFemaleNeurology (clinical)030217 neurology & neurosurgeryJournal of Child Neurology
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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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Ultrastructure of differentiating hemocytes in the embryo of Oncopeltus fasciatus dallas (insecta, heteroptera).

1978

The hemocytes of Oncopeltus differentiate rather early during embryogenesis. They are segregated by the mesoderm soon after its formation (about 50h after egg deposition). Newly segregated hemocytes show the “typical” features of “embryonic” cells: many free ribosomes, a few strands of rough ER, the cisternae of which are considerably distended, electron lucent vacuoles around the periphery, and glycogen deposits. A few hours thereafter the hemocytes undergo striking subcellular changes. First, glycogen, electron lucent vacuoles and rough ER disappear and phagocytotic activity can be observed. Golgi complexes become well expressed and give rise to electron dense vesicles which fuse to large…

MesodermHistologyHemocytesInsectaGolgi ApparatusVacuoleBiologyEndoplasmic ReticulumPathology and Forensic Medicinesymbols.namesakePhagocytosismedicineAnimalsInclusion BodiesBlood CellsEndoplasmic reticulumVesicleEmbryogenesisCell DifferentiationCell BiologyAnatomyGolgi apparatusCell biologymedicine.anatomical_structureCytoplasmLarvaVacuolessymbolsUltrastructureRibosomesGlycogenCell and tissue research
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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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Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy

2007

Reducing body myopathy (RBM) is a rare disorder causing progressive muscular weakness characterized by aggresome-like inclusions in the myofibrils. Identification of genes responsible for RBM by traditional genetic approaches has been impossible due to the frequently sporadic occurrence in affected patients and small family sizes. As an alternative approach to gene identification, we used laser microdissection of intracytoplasmic inclusions identified in patient muscle biopsies, followed by nanoflow liquid chromatography-tandem mass spectrometry and proteomic analysis. The most prominent component of the inclusions was the Xq26.3-encoded four and a half LIM domain 1 (FHL1) protein, expresse…

Models MolecularProteomicsMolecular Sequence DataMuscle ProteinsBiologyTransfectionProteomicsInclusion bodiesMuscular DiseasesmedicineAmino Acid SequenceLaser capture microdissectionInclusion BodiesIntracellular Signaling Peptides and ProteinsCardiac muscleSkeletal muscleGenetic Diseases X-LinkedGeneral MedicineLIM Domain Proteinsmedicine.diseaseCongenital myopathyMolecular biologyFHL1medicine.anatomical_structureMutationMyofibrilResearch Article
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A molecular assembly system that renders antigens of choice highly repetitive for induction of protective B cell responses.

2002

Virus like particles (VLPs) are known to induce potent B cell responses in the absence of adjuvants. Moreover, epitope-specific antibody responses may be induced by VLPs that contain peptides inserted in their immunodominant regions. However, due to steric problems, the size of the peptides capable of being incorporated into VLPs while still permitting capsid assembly, is rather limited. While peptides genetically fused to either the N- or C-terminus of VLPs present fewer assembly problems, the immune responses obtained against such epitopes are often limited, most likely because the epitopes are not optimally exposed. In addition, such particles may be less stable in vivo. Here, we show th…

Models MolecularViral Hepatitis VaccinesHepatitis B virusMacromolecular SubstancesProtein ConformationvirusesRecombinant Fusion ProteinsProtozoan ProteinsAntigens ProtozoanBiologyProtein EngineeringEpitopePhospholipases AInclusion Bodies ViralViral Matrix ProteinsMiceImmune systemAntigenVirus-like particlemedicineAnimalsB cellB-LymphocytesMice Inbred BALB CVaccines SyntheticGeneral VeterinaryGeneral Immunology and MicrobiologyImmunodominant EpitopesImmunogenicityVaccinationPublic Health Environmental and Occupational HealthMolecular biologyHepatitis B Core AntigensPeptide FragmentsCell biologyProtein Structure TertiaryHBcAgBee VenomsInfectious Diseasesmedicine.anatomical_structureCross-Linking ReagentsCapsidDrug DesignMolecular MedicineFemaleImmunizationPeptidesOligopeptidesVaccine
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Congenital myopathies at their molecular dawning

2003

The introduction and application of molecular techniques have commenced to influence and alter the nosology of congenital myopathies. Long-known entities such as nemaline myopathies, core diseases, and desmin-related myopathies have now been found to be caused by unequivocal mutations. Several of these mutations and their genes have been identified by analyzing aggregates of proteins within muscle fibers as a morphological hallmark as in desminopathy and actinopathy, the latter a subtype among the nemaline myopathies. Immunohistochemistry has played a crucial role in recognizing this new group of protein aggregate myopathies within the spectrum of congenital myopathies. It is to be expected…

MutationPathologymedicine.medical_specialtyPhysiologyMuscle ProteinsProtein aggregationBiologymedicine.disease_causemedicine.diseaseInclusion bodiesCellular and Molecular NeuroscienceNemaline myopathyMuscular DiseasesPhysiology (medical)Putative genemedicineHumansNeurology (clinical)Congenital diseaseGeneMuscle & Nerve
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