Search results for "Intermediate filaments"

showing 10 items of 29 documents

Structural and regulatory functions of keratins.

2007

The diversity of epithelial functions is reflected by the expression of distinct keratin pairs that are responsible to protect epithelial cells against mechanical stress and to act as signaling platforms. The keratin cytoskeleton integrates these functions by forming a supracellular scaffold that connects at desmosomal cell-cell adhesions. Multiple human diseases and murine knockouts in which the integrity of this system is destroyed testify to its importance as a mechanical stabilizer in certain epithelia. Yet, surprisingly little is known about the precise mechanisms responsible for assembly and disease pathology. In addition to these structural aspects of keratin function, experimental e…

CellIntermediate Filamentsmacromolecular substancesBiologyFocal adhesionEpidermolysis bullosa simplexMicrotubuleOrganelleKeratinmedicineAnimalsHumansCytoskeletonCytoskeletonchemistry.chemical_classificationCell PolarityEpithelial CellsCell BiologyDesmosomesmedicine.diseaseCell biologymedicine.anatomical_structureCell Transformation NeoplasticchemistryKeratinsStress MechanicalFunction (biology)Signal TransductionExperimental cell research
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Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity?

2012

Abstract The cytoskeleton is a highly complex network of three major intracellular filaments, microfilaments (MFs), microtubules (MTs) and intermediate filaments (IFs). This network plays a key role in the control of cell shape, division, functions and interactions in animal organs and tissues. Dysregulation of the network can contribute to numerous human diseases. Although small HSPs (sHSPs) and in particular HSP27 (HSPB1) or αB-crystallin (HSPB5) display a wide range of cellular properties, they are mostly known for their ability to protect cells under stress conditions. Mutations in some sHSPs have been found to affect their ability to interact with cytoskeleton proteins, leading to IF a…

Epithelial-Mesenchymal TransitionIntermediate FilamentsVimentinmacromolecular substancesMicrofilamentBiochemistry03 medical and health sciences0302 clinical medicineHsp27MicrotubuleStress PhysiologicalHeat shock proteinNeoplasmsAnimalsHumansCytoskeletonIntermediate filament030304 developmental biology0303 health sciencesbiologyGenetic Diseases InbornCell BiologyFibrosisCell biologyHeat-Shock Proteins SmallMutationbiology.proteinDesmin030217 neurology & neurosurgeryThe international journal of biochemistrycell biology
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Intermediate Filament Diseases: Desminopathy

2008

Desminopathy is one of the most common intermediate filament human disorders associated with mutations in closely interacting proteins, desmin and alphaB-crystallin. The inheritance pattern in familial desminopathy is characterized as autosomal dominant or autosomal recessive, but many cases have no family history. At least some and likely most sporadic desminopathy cases are associated with de novo DES mutations. The age of disease onset and rate of progression may vary depending on the type of inheritance and location of the causative mutation. Typically, the illness presents with lower and later upper limb muscle weakness slowly spreading to involve truncal, neck-flexor, facial and bulba…

GeneticsPathologymedicine.medical_specialtyPoint mutationMutantCardiomyopathyIntermediate Filamentsalpha-Crystallin B ChainGene mutationBiologymedicine.diseaseSudden deathPolymorphism Single NucleotideArticleUpper limb muscle weaknessDesminMuscular DiseasesmedicineDisease ProgressionAnimalsHumansDesminIntermediate filament
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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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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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Giant axonal neuropathy and leukodystrophy

1991

Abstract An 11-year-old Persian boy, born to consanguineous parents, manifested a progressive gait abnormality beginning at 5 years of age. A severe cerebellar disorder developed with associated dysfunction of the peripheral nervous system, but no sign of mental impairment. The sensory and motor nerve conduction velocities were greatly reduced, especially in the lower extremities. Cerebrospinal fluid protein was normal. Computed tomography and magnetic resonance imaging revealed leukoencephalopathy, especially in the cerebellum, but also in periventricular areas. The diagnosis of giant axonal neuropathy was established by biopsy of the sural nerve. The few previous histologic examinations h…

MaleIntermediate FilamentsMotor nerveGenes RecessiveSural nerveCerebral VentriclesLeukoencephalopathyConsanguinityDevelopmental NeuroscienceCerebellummedicineHumansCerebellar disorderGliosisPeripheral NervesChildMyelin SheathSpinocerebellar DegenerationsGiant axonal neuropathybusiness.industryLeukodystrophyAnatomymedicine.diseaseMagnetic Resonance ImagingAxonsMicroscopy Electronmedicine.anatomical_structurenervous systemNeurologyPeripheral nervous systemPediatrics Perinatology and Child HealthGait abnormalityNeurology (clinical)medicine.symptomHereditary Sensory and Motor NeuropathybusinessPediatric Neurology
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Neuronal markers in the rodent pineal gland ? an immunohistochemical investigation

1990

Although some embryological and morphological features speak in favour of a neuronal character of rodent pinealocytes, histochemistry and ultrastructure let this issue appear controversial. Using antibodies to different neurofilaments, the neural adhesion molecule L1, synaptophysin and tubulin as neuronal markers, the pineal glands of rat and guinea-pig were studied by means of immunofluorescence. Neurofilament-immunoreactivity was present in some rat pineal nerve fibers and in the majority of guinea-pig pinealocytes, L1 decorated rat intrapineal nerve fibers, synaptophysin was almost ubiquitously distributed in the pineal of both species, while tubulin-immunofluorescence was seen in nerve …

Malemedicine.medical_specialtyHistologyNeurofilamentL1Cell Adhesion Molecules NeuronalGuinea PigsIntermediate FilamentsSynaptophysinNerve Tissue ProteinsPineal GlandPinealocyteGuinea pigPineal glandTubulinInternal medicinemedicineAnimalsMolecular BiologyCytoskeletonbiologyMembrane ProteinsRats Inbred StrainsCell BiologyGeneral MedicineImmunohistochemistryRatsCell biologyMedical Laboratory TechnologyEndocrinologymedicine.anatomical_structurenervous systemSynaptophysinbiology.proteinUltrastructureImmunohistochemistryAnatomyGeneral Agricultural and Biological SciencesBiomarkersHistochemistry
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Patterns of Expression and Organization of Cytokeratin Intermediate Filaments

1985

Cytokeratins are a large multigene family comprising two polypeptide types, i.e. acidic (type I) and basic (type II) ones, which are distinguished on the basis of immunological, peptide mapping, mRNA hybridization, and primary amino acid sequence data. The acidic (type I) cytokeratins can be subdivided into at least two different subtypes on the basis of their carboxy-terminal sequences. Considerable interspecies conservation of sequences exists, even extending to the 3'-non-coding mRNA regions. Different pairs of type I and II cytokeratins show different resistance to dissociation in urea. Sequence differences of the type I cytokeratins containing functional domains may be an explanation o…

Messenger RNANeurofilamentBase SequenceProtein ConformationChemistryGeneral NeuroscienceIntermediate FilamentsRNAMolecular biologyGeneral Biochemistry Genetics and Molecular BiologyMolecular WeightCytokeratinProtein structureHistory and Philosophy of ScienceTetramerAnimalsHumansKeratinsAmino Acid SequenceRNA MessengerIntermediate filamentPeptide sequenceCytoskeletonAnnals of the New York Academy of Sciences
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Tension Causes Unfolding of Intracellular Vimentin Intermediate Filaments

2020

Intermediate filament (IF) proteins are a class of proteins that constitute different filamentous structures in mammalian cells. As such, IF proteins are part of the load-bearing cytoskeleton and support the nuclear envelope. Molecular dynamics simulations show that IF proteins undergo secondary structural changes to compensate mechanical loads, which is confirmed by experimental in vitro studies on IF hydrogels. However, the structural response of intracellular IF to mechanical load is yet to be elucidated in cellulo. Here, in situ nonlinear Raman imaging combined with multivariate data analysis is used to quantify the intracellular secondary structure of the IF cytoskeletal protein viment…

MicroscopybiologyChemistryIntermediate FilamentsBiomedical EngineeringVimentinSpectrum Analysis RamanMechanotransduction CellularProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular BiologyBiomaterialsMolecular dynamicsSelf-healing hydrogelsBiophysicsbiology.proteinHumansVimentinMechanotransductionIntermediate filamentCytoskeletonProtein secondary structureIntracellularHeLa CellsProtein UnfoldingAdvanced Biosystems
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Neurofilament light chain levels reflect outcome in a patient with glutamic acid decarboxylase 65 antibody–positive autoimmune encephalitis under imm…

2020

Neurological immune-mediated side effects are rare but often severe complications of immune checkpoint inhibitor (ICI) treatment. This report describes a severe case of nivolumab/ipilimumab-associated glutamic acid decarboxylase 65-positive autoimmune encephalitis. It proposes neurofilament light chain levels, a biomarker indicating axonal damage, in the cerebrospinal fluid and serum as a putative novel biomarker for this diagnostically and therapeutically challenging entity with an often unfavorable outcome. Additionally, we provide an overview of previous reports of patients developing autoimmune encephalitis under ICI treatment.

NeurofilamentGlutamate decarboxylaseIntermediate Filaments610 MedizinHashimoto Disease03 medical and health sciences0302 clinical medicineCerebrospinal fluid610 Medical sciencesHumansMedicine030212 general & internal medicineImmune Checkpoint InhibitorsAutoimmune encephalitisbiologyGlutamate Decarboxylasebusiness.industrymedicine.diseaseIpilimumabNivolumabNeurologyImmunologybiology.proteinEncephalitisBiomarker (medicine)Neurology (clinical)AntibodyNivolumabbusiness030217 neurology & neurosurgeryEncephalitisEuropean Journal of Neurology
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