Search results for "Intermediate filaments"

showing 9 items of 29 documents

Cytokeratin 8 immunostaining pattern and E-cadherin expression distinguish lobular from ductal breast carcinoma.

2000

Immunohistochemistry using antibodies to cytokeratin 8 can serve as a valuable diagnostic tool for the differentiation of lobular from ductal carcinomas of the breast. In contrast with ductal carcinomas, which exhibit a peripheral-predominant immunostaining pattern, adjacent tumor cells “molding” to each other, lobular carcinomas exhibit a ring-like perinuclear immunostaining pattern, creating a “bag of marbles” appearance with neighboring tumor cells. This immunostaining pattern is stable even in the tumors that otherwise do not exhibit characteristic histomorphologic features (ie, solid or pleomorphic type of a lobular carcinoma) and tumors that mimic growth patterns characteristic of the…

Pathologymedicine.medical_specialtyLobular carcinomaIntermediate FilamentsBreast NeoplasmsBiologyDiagnosis DifferentialImmunoenzyme TechniquesCytokeratinBreast cancerCarcinomamedicineHumansskin and connective tissue diseasesCell NucleusCarcinoma Ductal BreastGeneral MedicineDuctal carcinomamedicine.diseaseCadherinsDuctal Breast CarcinomaCarcinoma LobularInvasive lobular carcinomaKeratin 8KeratinsFemaleAmerican journal of clinical pathology
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Neuropathologic and morphometric studies in hereditary motor and sensory neuropathy type II with neurofilament accumulation.

1986

Histological, electron microscopic and morphometric data on sural nerve, muscle, and skin biopsies of three patients affected by autosomal dominant hereditary motor and sensory neuropathy type II with neurofilament accumulation, whose neurological, cardiological and electrophysiological data have been provided in a previous paper disclosed focally enlarged myelinated axons, due to aggregation of neurofilaments in sural nerves of all 3 biopsied patients, as well as densely packed clusters of filaments in occasional non-myelinated axons without axonal enlargement, in several fibroblasts and endothelial cells in muscle and particularly in skin. This accumulation of filaments was less pronounce…

Pathologymedicine.medical_specialtyNeurofilamentNeurologyIntermediate FilamentsSural nerveDermatologyBiologylaw.invention03 medical and health sciences0302 clinical medicineSural NervelawCharcot-Marie-Tooth DiseasemedicineHumansHereditary Sensory and Autonomic NeuropathiesIntermediate filamentCytoskeletonMyelin Sheath030304 developmental biologySkinMotor Neurons0303 health sciencesGeneral NeuroscienceMusclesGeneral MedicineAnatomymedicine.diseaseAxonsPsychiatry and Mental healthElectrophysiologyMicroscopy ElectronMuscular Atrophynervous systemUltrastructureNeurology (clinical)Electron microscopeHereditary motor and sensory neuropathy030217 neurology & neurosurgeryItalian journal of neurological sciences
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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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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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Morphometry and comparative histology of sinus and atrioventricular nodes in humans and pigs and their relevance in the prevention of nodal arrhythmi…

2019

The cardiac conduction system is a network structure that allows the initiation and fast propagation of electrical impulses that trigger the electrical depolarization of the myocardial tissue. The purpose of this work is to study the histological and morphometric characteristics of the different components of the sinus and atrioventricular nodes in humans and pigs and their relationship with supraventricular arrhythmias. In this study, we describe the morphometry of the sinus and atrioventricular nodes of 10 adult humans and 10 pig hearts. A computerized morphometric study has been carried out, where we determined the number of cells that compose the nodes as well as different parameters re…

Swine040301 veterinary sciencesBiology0403 veterinary science03 medical and health sciencesHeart Conduction SystemmedicineAnimalsHumansdiameter [Area]Intermediate filamentsHeart AtriaHistology Comparativecardiovascular diseasesSinus (anatomy)Sinoatrial Node030304 developmental biology0303 health sciencesSupraventricular arrhythmiaGeneral VeterinaryT cellArrhythmias CardiacHistologyDepolarization04 agricultural and veterinary sciencesAnatomyAtrioventricular nodemedicine.anatomical_structureConduction systemAtrioventricular NodeP cellcardiovascular systemDesminElectrical conduction system of the heartNODALResearch in Veterinary Science
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Focal adhesions are hotspots for keratin filament precursor formation

2006

Recent studies showed that keratin filament (KF) formation originates primarily from sites close to the actin-rich cell cortex. To further characterize these sites, we performed multicolor fluorescence imaging of living cells and found drastically increased KF assembly in regions of elevated actin turnover, i.e., in lamellipodia. Abundant KF precursors (KFPs) appeared within these areas at the distal tips of actin stress fibers, moving alongside the stress fibers until their integration into the peripheral KF network. The earliest KFPs were detected next to actin-anchoring focal adhesions (FAs) and were only seen after the establishment of FAs in emerging lamellipodia. Tight spatiotemporal …

TalinKeratin 14Intermediate Filamentsmacromolecular substancesBiologyTransfectionKeratin 18Cell LineFocal adhesionMiceReportStress FibersCell cortexMetalloproteinsAnimalsHumansRNA AntisensePseudopodiaCytoskeletonActinResearch ArticlesCell Line TransformedFocal AdhesionsKeratin FilamentKeratin-18Keratin-14Cell BiologyBridged Bicyclo Compounds HeterocyclicActinsZyxinCell biologyProtein TransportThiazolesBiochemistryEpidermolysis Bullosa SimplexMutationKeratinsThiazolidinesMarine ToxinsLamellipodiumPaxillinThe Journal of Cell Biology
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Induction of rapid and reversible cytokeratin filament network remodeling by inhibition of tyrosine phosphatases

2002

The cytokeratin filament network is intrinsically dynamic, continuously exchanging subunits over its entire surface, while conferring structural stability on epithelial cells. However, it is not known how cytokeratin filaments are remodeled in situations where the network is temporarily and spatially restricted. Using the tyrosine phosphatase inhibitor orthovanadate we observed rapid and reversible restructuring in living cells, which may provide the basis for such dynamics. By examining cells stably expressing fluorescent cytokeratin chimeras, we found that cytokeratin filaments were broken down and then formed into granular aggregates within a few minutes of orthovanadate addition. After …

Tyrosine 3-MonooxygenaseRecombinant Fusion ProteinsGreen Fluorescent ProteinsIntermediate FilamentsFluorescent Antibody Techniquemacromolecular substancesBiologyCytoplasmic GranulesProtein filamentCytokeratinIntermediate Filament ProteinsKeratinTumor Cells CulturedEnzyme InhibitorsPhosphorylationCytoskeletonIntermediate filamentActinchemistry.chemical_classificationCell BiologyPlectinCell biologyLuminescent ProteinsMicroscopy ElectronEukaryotic Cells14-3-3 ProteinschemistryCytoplasmKeratinsPlectinTyrosineProtein Tyrosine PhosphatasesVanadatesJournal of Cell Science
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Light-induced resistance of the keratin network to the filament-disrupting tyrosine phosphatase inhibitor orthovanadate.

2003

Epidermal keratinocytes respond to low-dose light irradiation by inducing signaling cascades that lead to long-term effects on gene transcription thereby protecting cells against damage. In contrast, little is known about immediate light-induced alterations of structural proteins. We have made the intriguing observation that light produces fundamental changes in the properties of the keratin filament system of cultured epidermoid A-431 cells. A short light exposure (1–10 min) causes the keratin cytoskeleton to become immediately resistant to the tyrosine phosphatase inhibitor orthovanadate, which otherwise disrupts the keratin filament network completely in just a few minutes. This protecti…

Ultraviolet Raysultraviolet lightDrug ResistanceIntermediate FilamentsDermatologyProtein tyrosine phosphatasemacromolecular substancesBiologyBiochemistryProtein filamentKeratinUltraviolet lightTumor Cells CulturedHumansVanadatePhosphorylationIntermediate filamentMolecular Biologychemistry.chemical_classificationintermediate filamentKeratin Filamentintegumentary systemVulvar NeoplasmsvanadateCell BiologyMolecular biologyCell biologychemistryEpidermal CellsPhosphorylationKeratinsFemaleProtein Tyrosine PhosphatasesVanadatescytokeratinThe Journal of investigative dermatology
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The identification and localization of two intermediate filament proteins in the tunic of Styela plicata (Tunicata, Styelidae).

2009

The intermediate filament (IF) proteins Styela C and Styela D from the tunicate Styela (Urochordata) are co-expressed in all epidermal cells and they are thought to behave as type I and type II keratins. These two IF proteins, Styela C and Styela D, were identified in immunoblots of proteins isolated from the tunic of Styela plicata. The occurrence and distribution of these proteins within the tunic of this ascidian was examined by means of immunofluorescence and immunoperoxidase techniques, using anti-Styela C and anti-Styela D antibodies. In addition, immuno-electron microscopy of the tunic showed that the two proteins are located in the cuticle layer and in the tunic matrix. These result…

intermediate filamentchemistry.chemical_classificationbiologyIntermediate FilamentsTunicataCell BiologyGeneral MedicineAnatomyStyelabiology.organism_classificationStyelidaeCell biologyTunicateimmunolocalizationStyela plicatachemistryStyela plicataKeratinAnimalsKeratinsUrochordataUrochordataIntermediate filamentDevelopmental BiologyCuticle (hair)Tissuecell
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