Search results for "Intermediate filament"

showing 10 items of 103 documents

Vimentin and desmin of a cartilaginous fish, the shark Scyliorhinus stellaris: Sequence, expression patterns and in vitro assembly

2002

In the shark Scyliorhinus stellaris we have biochemically identified and cDNA-cloned orthologs of human vimentin and desmin, SstV and SstD, as deduced from immunoblotting and sequence alignment with teleost, frog and human vimentin and desmin, respectively. This allowed us to further clarify the relationship of previously identified lower vertebrate intermediate filament proteins to mammalian vimentin and desmin. Immunofluorescence microscopy with antibodies H5 and VIM13.2 showed vimentin expression in shark eye and brain and absence in epithelia, which resembles the situation in higher vertebrates. In addition, SstV is expressed in many mesenchymal cell types which corresponds to the case …

HistologyNeurofilamentMolecular Sequence DataIntermediate FilamentsGene ExpressionVimentinmacromolecular substancesDesminPathology and Forensic MedicineEvolution MolecularProtein filamentKeratinAnimalsVimentinIntermediate filamentPhylogenychemistry.chemical_classificationSequence Homology Amino AcidbiologyProtein primary structureCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyMicroscopy ElectronchemistrySharksbiology.proteinDesminScyliorhinus stellarisEuropean Journal of Cell Biology
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Dissection of keratin dynamics: different contributions of the actin and microtubule systems.

2005

It has only recently been recognized that intermediate filaments (IFs) and their assembly intermediates are highly motile cytoskeletal components with cell-type- and isotype-specific characteristics. To elucidate the cell-type-independent contribution of actin filaments and microtubules to these motile properties, fluorescent epithelial IF keratin polypeptides were introduced into non-epithelial, adrenal cortex-derived SW13 cells. Time-lapse fluorescence microscopy of stably transfected SW13 cell lines synthesizing fluorescent human keratin 8 and 18 chimeras HK8-CFP and HK18-YFP revealed extended filament networks that are entirely composed of transgene products and exhibit the same dynamic…

HistologyRecombinant Fusion ProteinsArp2/3 complexAntineoplastic Agentsmacromolecular substancesBiologyMicrotubulesPathology and Forensic MedicineGenes ReporterKeratinHumansIntermediate filamentCytoskeletonchemistry.chemical_classificationKeratin FilamentNocodazoleActin remodelingCell BiologyGeneral MedicineBridged Bicyclo Compounds HeterocyclicActinsCell biologyActin CytoskeletonProtein TransportThiazoleschemistryMicroscopy Fluorescencebiology.proteinKeratin 8KeratinsThiazolidinesLamellipodiumEuropean journal of cell biology
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Zebrafish vimentin: molecular characterization, assembly properties and developmental expression

1998

To provide a basis for the investigation of the intermediate filament (IF) protein vimentin in one of the most promising experimental vertebrate systems, the zebrafish (Danio rerio), we have isolated a cDNA clone of high sequence identity to and with the characteristic features of human vimentin. Using this clone we produced recombinant zebrafish vimentin and studied its assembly behaviour. Unlike other vimentins, zebrafish vimentin formed unusually thick filaments when assembled at temperatures below 21 degrees C. At 37 degrees C few filaments were observed, which often also terminated in aggregated masses, indicating that its assembly was severely disturbed at this temperature. Between 21…

HistologyTroutMolecular Sequence DataCellDanioClone (cell biology)Vimentinmacromolecular substancesPathology and Forensic MedicineMyosinmedicineAnimalsHumansVimentinTissue DistributionAmino Acid SequenceRNA MessengerCloning MolecularIntermediate filamentPeptide sequenceZebrafishZebrafishSequence Homology Amino AcidbiologyTemperatureGene Expression Regulation DevelopmentalCell BiologyGeneral Medicinebiology.organism_classificationImmunohistochemistryMolecular biologyCell biologyMicroscopy Electronmedicine.anatomical_structurebiology.protein
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Expression Profile of Stress Proteins, Intermediate Filaments, and Adhesion Molecules in Experimentally Denervated and Reinnervated Rat Facial Muscle

1997

The immunohistochemical profiles of ubiquitin, heat shock protein 70, alpha-B-crystallin, desmin, vimentin, neural cell adhesion molecule (N-CAM), and tenascin in rat facial muscle were studied after permanent denervation by transection of the facial plexus on one side and compared with findings after immediate reinnervation by hypoglossal-facial nerve anastomosis subsequent to transection on the contralateral side. Levator labii muscle samples were collected sequentially at 2, 6, 7, 10, 20, and 24 weeks after surgery. Normal levator labii muscle fibers showed physiological expression of desmin and alpha-B-crystallin. Denervated rat facial muscle displayed distinct up-regulation of ubiquiti…

Hypoglossal NervePathologymedicine.medical_specialtyTime Factorsanimal structuresMuscle Fibers SkeletalFacial MusclesTenascinDesminIntermediate Filament ProteinsDevelopmental NeurosciencemedicineAnimalsVimentinHSP70 Heat-Shock ProteinsRats WistarIntermediate filamentNeural Cell Adhesion MoleculesUbiquitinsHeat-Shock ProteinsConnective Tissue CellsDenervationMuscle DenervationbiologyAnastomosis SurgicalTenascinmusculoskeletal systemCrystallinsImmunohistochemistryMuscle DenervationRatsSarcoplasmic ReticulumFacial musclesmedicine.anatomical_structureNeurologyConnective Tissuebiology.proteinFemaleNeural cell adhesion moleculeDesminAtrophyReinnervationExperimental Neurology
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Congenital myopathies with inclusion bodies: a brief review

1998

Abstract Based on morphological abnormalities, congenital myopathies can be classified into several categories: (1) enzyme histochemically abnormal appearance without structural pathology, e.g. congenital fibre type disproportion or congenital fibre type uniformity; (2) abnormally placed nuclei, e.g. myotubular and centronuclear myopathies; (3) disruption of normal intrinsic structures, largely sarcomeres, e.g. central cores and minicores; (4) abnormal inclusions within muscle fibres. Several such inclusions are derived from pre-existing structures, most notably rods or nemaline bodies. Other derivatives of Z-band material are cytoplasmic bodies and possibly related inclusions as spheroid b…

Inclusion BodiesCytoplasmPathologymedicine.medical_specialtyMusclesAnatomyBiologymedicine.diseaseSarcomereCongenital myopathyInclusion bodiesDesminIntermediate Filament ProteinsMuscular DiseasesNeurologyPediatrics Perinatology and Child HealthmedicineUltrastructureHumansDesminNeurology (clinical)Nemaline bodiesIntermediate filamentGenetics (clinical)Central core diseaseNeuromuscular Disorders
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Microtubules and intermediate filaments of herpes simplex virus infected cells.

1987

The fate of microtubules and of vimentin or keratin containing intermediate filaments during infection with fusion or rounding producing strains of herpes simplex virus (HSV) was investigated. Microtubules polymerize early after fusion of cells. However, they do not reconstitute 6–7 hours post infection (p.i.) after release of a colcemid block. Keratin and vimentin are maintained around the original nucleus still inside of recruited cells in the polykaryocyte. Cells of fibroblastic and epithelial origin fuse. Inside of polykaryocytes keratin or vimentin containing fibers seem to polymerize. Keratin is to be found in invaginations in the nuclei surrounded by the inner layer of the nuclear me…

Intermediate FilamentsVimentinmacromolecular substancesmedicine.disease_causeMicrofilamentMicrotubulesEpitheliumCell LineCell Fusionchemistry.chemical_compoundCytopathogenic Effect ViralVirologyKeratinmedicineAnimalsSimplexvirusVimentinNuclear membraneIntermediate filamentCytoskeletonchemistry.chemical_classificationintegumentary systembiologyColcemidHerpes SimplexGeneral MedicineFibroblastsVirologyHerpes simplex virusmedicine.anatomical_structurechemistryCytoplasmbiology.proteinKeratinsArchives of virology
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Ectopic expression of desmin in the epidermis of transgenic mice permits development of a normal epidermis.

2002

Cell architecture is largely based on the interaction of cytoskeletal proteins, which include intermediate filaments (IF), microfilaments, microtubules, as well as their type-specific membrane-attachment structures and associated proteins. In order to further our understanding of IF proteins and to address the fundamental issue whether different IF perform unique functions in different tissues, we expressed a desmin transgene in the basal epidermis of mice. Ectopic expression of desmin led to the formation of an additional, keratin-independent IF cytoskeleton and did not interfere with the keratin-desmosome interaction. We show that ectopic expression of a type III IF protein in basal kerat…

KeratinocytesCancer ResearchCellular differentiationMice Transgenicmacromolecular substancesBiologyDesminMiceKeratinmedicineAnimalsHumansIntermediate filamentCytoskeletonMolecular Biologychemistry.chemical_classificationEpidermis (botany)Keratin-14Cell BiologyImmunohistochemistryCell biologyDisease Models Animalmedicine.anatomical_structurePhenotypechemistryEpidermolysis Bullosa SimplexImmunologyKeratinsEctopic expressionDesminEpidermisKeratinocyteDevelopmental BiologyDifferentiation; research in biological diversity
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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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p38 MAPK-dependent shaping of the keratin cytoskeleton in cultured cells

2007

Plasticity of the resilient keratin intermediate filament cytoskeleton is an important prerequisite for epithelial tissue homeostasis. Here, the contribution of stress-activated p38 MAPK to keratin network organization was examined in cultured cells. It was observed that phosphorylated p38 colocalized with keratin granules that were rapidly formed in response to orthovanadate. The same p38p recruitment was noted during mitosis, in various stress situations and in cells producing mutant keratins. In all these situations keratin 8 became phosphorylated on S73, a well-known p38 target site. To demonstrate that p38-dependent keratin phosphorylation determines keratin organization, p38 activity …

MAP Kinase Signaling SystemIntermediate filament cytoskeletonmacromolecular substancesBiologyp38 Mitogen-Activated Protein KinasesArticleKeratinHumansPhosphorylationCytoskeletonProtein Kinase InhibitorsMitosisResearch ArticlesCells CulturedCytoskeletonchemistry.chemical_classificationKeratin Filamentintegumentary systemCell BiologyCell biologyKeratin 5chemistryKeratin 8KeratinsPhosphorylationVanadatesJournal of Cell Biology
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Genes coding for intermediate filament proteins closely related to the hagfish "thread keratins (TK)" alpha and gamma also exist in lamprey, teleosts…

2005

The "thread keratins (TK)" alpha and gamma so far have been considered highly specialized intermediate filament (IF) proteins restricted to hagfish. From lamprey, we now have sequenced five novel IF proteins closely related to TKalpha and TKgamma, respectively. Moreover, we have detected corresponding sequences in EST and genomic databases of teleosts and amphibians. The structure of the TKalpha genes and the positions of their deduced amino acid sequences in a phylogenetic tree clearly support their classification as type II keratins. The genes encoding TKgamma show a structure typical for type III IF proteins, whereas their positions in phylogenetic trees favor a close relationship to the…

MaleBranchiostomaDNA ComplementaryLanceletXenopusMolecular Sequence DataAmphibiansIntermediate Filament Proteinsbiology.animalKeratinAnimalsProtein IsoformsElectrophoresis Gel Two-DimensionalAmino Acid SequenceIntermediate filamentGenePhylogenyZebrafishchemistry.chemical_classificationintegumentary systembiologyPhylogenetic treeSequence Homology Amino AcidEcologyLampreyGene Expression ProfilingFishesGene Expression Regulation DevelopmentalLampreysCell BiologyExonsSequence Analysis DNAbiology.organism_classificationIntronschemistryEvolutionary biologyKeratinsFemaleHagfishesHagfishExperimental cell research
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