Search results for "keratin"

showing 10 items of 303 documents

Evolution of tissue-specific keratins as deduced from novel cDNA sequences of the lungfish Protopterus aethiopicus.

2005

Lungfishes are possibly the closest extant relatives of the land vertebrates (tetrapods). We report here the cDNA and predicted amino acid sequences of 13 different keratins (ten type I and three type II) of the lungfish Protopterus aethiopicus. These keratins include the orthologs of human K8 and K18. The lungfish keratins were also identified in tissue extracts using two-dimensional polyacrylamide gel electrophoresis, keratin blot binding assays and immunoblotting. The identified keratin spots were analyzed by peptide mass fingerprinting which assigned seven sequences (inclusively Protopterus K8 and K18) to their respective protein spot. The peptide mass fingerprints also revealed the fac…

HistologyDNA ComplementaryMolecular Sequence DataFluorescent Antibody Techniquemacromolecular substancesPeptide MappingPathology and Forensic MedicineEvolution MolecularPeptide mass fingerprintingComplementary DNAKeratinAnimalsElectrophoresis Gel Two-DimensionalAmino Acid SequencePolyacrylamide gel electrophoresisLungfishchemistry.chemical_classificationProtopterusintegumentary systembiologyPhylogenetic treeLampreyFishesCell BiologyGeneral MedicineAnatomybiology.organism_classificationchemistryEvolutionary biologySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationKeratinsEuropean journal of cell biology
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Tracing keratin evolution: catalog, expression patterns and primary structure of shark (Scyliorhinus stellaris) keratins.

1998

We have studied individual keratins of an elasmobranch, the shark Scyliorhinus stellaris (the lesser-spotted dogfish). From various shark tissues, notably skin and stomach, cytoskeletal proteins were isolated and then separated by two-dimensional polyacrylamide gel electrophoresis. Using complementary keratin blot-binding assays and immunoblotting, among these proteins we identified a variety of type I and type II keratins. According to their tissue-specific expression, we distinguished Is and IIs keratins from IE and IIE keratins ("S" and "E" from "simple epithelial" and "epidermal", respectively). Guinea pig antibodies which in immunoblots specifically labeled the entire range of identifi…

HistologyDNA ComplementaryMolecular Sequence Datamacromolecular substancesPathology and Forensic MedicineKeratinAnimalsHumansAmino Acid SequenceIntermediate filamentPolyacrylamide gel electrophoresisPeptide sequencechemistry.chemical_classificationintegumentary systemPhylogenetic treebiologyBase SequenceProtein primary structureCell BiologyGeneral MedicineKeratin 6Abiology.organism_classificationMolecular biologyBiological EvolutionchemistryMicroscopy FluorescenceSharksKeratinshuman activitiesScyliorhinus stellarisEuropean journal of cell biology
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Sequence, evolution and tissue expression patterns of an epidermal type I keratin from the shark Scyliorhinus stellaris.

2004

From the shark Scyliorhinus stellaris we cloned and sequenced a cDNA encoding a novel type I keratin, termed SstK10. By MALDI-MS peptide mass fingerprinting of cytoskeletal proteins separated on polyacrylamide gels, we assigned SstK10 to a 46-kDa protein which is the major epidermal type I (“IE”) keratin in this fish and is specifically expressed in stratified epithelia. In a phylogenetic tree based on type I keratin sequences and with lamprey keratins applied as outgroup, SstK10 branches off in a rather basal position. This tree strongly supports the concept that teleost keratins and tetrapod keratins resulted from two independent gene radiation processes. The only exception is human K18 b…

HistologyDNA ComplementaryType I keratinMolecular Sequence Datamacromolecular substancesMass SpectrometryPathology and Forensic MedicineSequence Analysis Proteinbiology.animalKeratinAnimalsAmino Acid SequenceCloning MolecularPhylogenychemistry.chemical_classificationintegumentary systemPhylogenetic treebiologyLampreyVertebrateCell BiologyGeneral MedicineGnathostomataKeratin 6AAnatomybiology.organism_classificationImmunohistochemistryCell biologychemistryEpidermal CellsGene Expression RegulationOrgan SpecificitySharksKeratinsElectrophoresis Polyacrylamide GelEpidermisScyliorhinus stellarisEuropean journal of cell biology
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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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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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In vivo detection of cytokeratin filament network breakdown in cells treated with the phosphatase inhibitor okadaic acid.

2001

We have previously described vulva carcinoma-derived A-431 subclone AK13-1, which stably expresses fluorescently labeled cytokeratin filaments (CKFs). Time-lapse fluorescence microscopy of these cells permits the continuous monitoring of the dynamics of the CKF cytoskeleton in vivo. To study mechanisms and principles of CKF disassembly as it occurs, e.g., during mitosis and liver disease, we have treated cells with the phosphatase inhibitor okadaic acid (OA), which induces complete CKF network breakdown within 3–5 h without significantly affecting the organization of the actin- and tubulin-based cytofilaments. In time-lapse movies, we find that the network breakdown starts at the cell perip…

HistologyTime FactorsRecombinant Fusion ProteinsGreen Fluorescent ProteinsPathology and Forensic Medicinechemistry.chemical_compoundCytokeratinAdenosine TriphosphateStress FibersOkadaic AcidFluorescence microscopeTumor Cells CulturedHumansEnzyme InhibitorsPhosphorylationCytoskeletonMitosisActinCytoskeletonbiologyVulvar NeoplasmsEpithelial CellsCell BiologyOkadaic acidCell biologyCytoskeletal ProteinsLuminescent ProteinsTubulinchemistryDesmoplakinsMicroscopy FluorescenceCytoplasmbiology.proteinKeratinsFemaleIndicators and ReagentsCell and tissue research
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Immunohistochemical expression of apoptotic factors, cytokeratins, and metalloproteinase-9 in periapical and epithelialized gingival lesions

2012

Bellmann K, 2010, CELL STRESS CHAPERON, V15, P101, DOI 10.1007-s12192-009-0126-9; Cappello Francesco, 2011, Front Biosci (Schol Ed), V3, P341, DOI 10.2741-s155; Cappello F, 2006, CANCER, V107, P2417, DOI 10.1002-cncr.22265; Cappello F, 2002, EUR J HISTOCHEM, V46, P199; Carneiro E, 2009, ORAL SURG ORAL MED O, V107, P127, DOI 10.1016-j.tripleo.2008.07.030; Chandra D, 2007, J BIOL CHEM, V282, P31289, DOI 10.1074-jbc.M702777200; Fujita Y, 2011, ODONTOLOGY, V100, P215; Garcia Celia Carrillo, 2007, Med Oral Patol Oral Cir Bucal, V12, pE585; Garcia CC, 2009, ORAL SURG ORAL MED O, V107, pE43, DOI 10.1016-j.tripleo.2008.12.002; Gregory CD, 2011, J PATHOL, V223, P177, DOI 10.1002-path.2792; Gupta S, …

Histologybusiness.industryCaspase 3GingivaApoptosisGeneral MedicineMolecular biologyImmunohistochemistryCaspase 9EpitheliumPathology and Forensic MedicineCell stressMatrix Metalloproteinase 9cytokeratins MMP-9 caspase-3 caspase-9 perapical lesions epithelial gingival lesions apoptosisIHC PCNA TUNELProliferating Cell Nuclear AntigenMedicineHumansKeratinsbusinessApoptosis Regulatory ProteinsPeriapical Granuloma
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Polyethylenimine is a strong inhibitor of human papillomavirus and cytomegalovirus infection.

2012

ABSTRACT Polyethylenimines are cationic polymers with potential as delivery vectors in gene therapy and with proven antimicrobial activity. However, the antiviral activity of polyethylenimines has not been addressed in detail thus far. We have studied the inhibitory effects of a linear 25-kDa polyethylenimine on infections with human papillomaviruses and human cytomegaloviruses. Preincubation of cells with polyethylenimine blocked primary attachment of both viruses to cells, resulting in a significant reduction of infection. In addition, the dissemination of human cytomegalovirus in culture cells was efficiently reduced by recurrent administration of polyethylenimine. Polyethylenimine conce…

Human cytomegalovirusKeratinocytesGenetic enhancementCongenital cytomegalovirus infectionCytomegalovirusVirus AttachmentBiologyAntiviral Agentschemistry.chemical_compoundCationsChlorocebus aethiopsmedicineCytotoxic T cellAnimalsHumansPolyethyleneiminePharmacology (medical)Human papillomavirusPapillomaviridaePharmacologyPolyethyleniminePapillomavirus InfectionsFibroblastsAntimicrobialmedicine.diseaseVirologyMicrobicides for sexually transmitted diseasesInfectious DiseasesHEK293 CellschemistryMicroscopy FluorescenceOrgan SpecificityCOS CellsCytomegalovirus InfectionsHeLa CellsAntimicrobial agents and chemotherapy
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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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Keratin 7 expression as an early marker of reflux-related columnar mucosa without intestinal metaplasia in the esophagus

2009

BACKGROUND: The role of Barrett esophagus in carcinogenesis is widely accepted, but the significance of esophageal columnar mucosa without histological intestinal metaplasia, known as columnar-lined esophagus, is debated. MATERIAL/METHODS: We studied 128 patients free of Helicobacter pylori with reflux-related symptoms and columnar mucosa in the esophagus at endoscopy, 106 patients with Barrett esophagus (referred to as the Barrett group) and 22 patients without intestinal metaplasia (columnar group). Samples from 20 subjects free of H. pylori were used as controls. Immunostaining for keratin 7 (KRT7), keratin 20 (KRT20), caudal type homeobox 2 (CDX2), mucin 2, oligomeric mucus/gel-forming …

IntestinesBarrett EsophagusMetaplasiaSettore MED/18 - Chirurgia GeneraleHelicobacter pyloriCase-Control StudiesKeratin-7HumansEsophagogastric JunctionBarrett esophagus reflux columnar mucosaSettore MED/08 - Anatomia PatologicaBiomarkers
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