Search results for "cytoskeleton"

showing 10 items of 272 documents

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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Dystroglycan in Skin and Cutaneous Cells: β-Subunit Is Shed from the Cell Surface

2004

In skin, hemidesmosomal protein complexes attach the epidermis to the dermis and are critical for stable connection of the basal epithelial cell cytoskeleton with the basement membrane (BM). In muscle, a similar supramolecular aggregate, the dystrophin glycoprotein complex links the inside of muscle cells with the BM. A component of the muscle complex, dystroglycan (DG), also occurs in epithelia. In this study, we characterized the expression and biochemical properties of authentic and recombinant DG in human skin and cutaneous cells in vitro. We show that DG is present at the epidermal BM zone, and it is produced by both keratinocytes and fibroblasts in vitro. The biosynthetic precursor is…

KeratinocytesCellHuman skinPerlecanDermatologyTransfectionBiochemistryCell LineDystroglycanmedicineExtracellularMyocyteHumansCytoskeletonDystroglycansMolecular BiologyBasement membraneMembrane GlycoproteinsbiologyMembrane ProteinsDermisCell BiologyCell biologyCulture MediaProtein Structure TertiaryCytoskeletal Proteinsmedicine.anatomical_structureBiochemistrybiology.proteinProtein BindingJournal of Investigative Dermatology
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α-parvin is required for epidermal morphogenesis, hair follicle development and basal keratinocyte polarity

2020

Epidermal morphogenesis and hair follicle (HF) development depend on the ability of keratinocytes to adhere to the basement membrane (BM) and migrate along the extracellular matrix. Integrins are cell-matrix receptors that control keratinocyte adhesion and migration, and are recognized as major regulators of epidermal homeostasis. How integrins regulate the behavior of keratinocytes during epidermal morphogenesis remains insufficiently understood. Here, we show that alpha-parvin (alpha-pv), a focal adhesion protein that couples integrins to actin cytoskeleton, is indispensable for epidermal morphogenesis and HF development. Inactivation of the murine alpha-pv gene in basal keratinocytes res…

KeratinocytesIntegrinsEpitheliumBasement MembraneExtracellular matrixMiceAnimal CellsCell MovementMedicine and Health SciencesMorphogenesisCells CulturedSkinMultidisciplinarybiologyintegumentary systemChemistryQMicrofilament ProteinsMorfogènesiRCell DifferentiationDermisCell biologyExtracellular Matrixmedicine.anatomical_structureMedicineCellular TypesAnatomyCellular Structures and OrganellesIntegumentary SystemKeratinocyteHair FollicleResearch ArticleCèl·lulesCellsScienceIntegrinMorphogenesisMice TransgenicActin cytoskeleton organizationFocal adhesionHair FolliclesmedicineCell AdhesionAnimalsFocal AdhesionsBiology and Life SciencesEpithelial CellsCell BiologyActin cytoskeletonActinsBiological Tissuebiology.proteinEpidermisEpidermal thickeningDevelopmental BiologyHairPLoS ONE
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Epidermolysis Bullosa Simplex-Type Mutations Alter the Dynamics of the Keratin Cytoskeleton and Reveal a Contribution of Actin to the Transport of Ke…

2003

Dominant keratin mutations cause epidermolysis bullosa simplex by transforming keratin (K) filaments into aggregates. As a first step toward understanding the properties of mutant keratins in vivo, we stably transfected epithelial cells with an enhanced yellow fluorescent protein-tagged K14R125C mutant. K14R125C became localized as aggregates in the cell periphery and incorporated into perinuclear keratin filaments. Unexpectedly, keratin aggregates were in dynamic equilibrium with soluble subunits at a half-life time of <15 min, whereas filaments were extremely static. Therefore, this dominant-negative mutation acts by altering cytoskeletal dynamics and solubility. Unlike previously post…

KeratinocytesMutantmacromolecular substancesBiologyEpidermolysis bullosa simplexMicrotubuleKeratinmedicineHumansRNA Small InterferingCytoskeletonMolecular BiologyCells CulturedCytoskeletonActinchemistry.chemical_classificationintegumentary systemBiological TransportArticlesCell BiologyKeratin 6Amedicine.diseaseMolecular biologyActinsRecombinant ProteinsCell biologyKeratin 5chemistryEpidermolysis Bullosa SimplexMutationKeratinsMolecular Biology of the Cell
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Maturation of epidermal Langerhans cells: increased expression of beta- and gamma-actin isoforms as a basis of specialized cell functions.

1999

Epidermal Langerhans cells (LC) represent immature dendritic cells. During in vitro culture in the presence of keratinocytes they mature into potent immunostimulatory cells for naive T cells. This process is thought to simulate in vivo maturation of LC following activation by antigen contact. Maturation of LC is accompanied by morphological alterations. Applying a differential screening procedure we isolated differentially expressed cDNAs involved in the maturation events including cDNAs of the cytoskeletal actin isoforms beta- and gamma-actin. Stronger signals with hybridization probes derived from cultured LC compared with probes derived from freshly isolated LC indicate upregulation of a…

Langerhans cellDNA ComplementaryPhalloidinmacromolecular substancesDermatologyBiologyIn Vitro TechniquesBiochemistrychemistry.chemical_compoundMiceWestern blotmedicineAnimalsProtein IsoformsNorthern blotRNA MessengerCytoskeletonMolecular BiologyActinDNA PrimersMice Inbred BALB Cmedicine.diagnostic_testEpidermis (botany)Base SequenceReverse Transcriptase Polymerase Chain ReactionCell DifferentiationDendritic cellDendritic CellsActinsCell biologyUp-Regulationmedicine.anatomical_structurechemistryLangerhans CellsExperimental dermatology
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eNOS S-nitrosylates β-actin on Cys374 and regulates PKC-θ at the immune synapse by impairing actin binding to profilin-1.

2017

The actin cytoskeleton coordinates the organization of signaling microclusters at the immune synapse (IS); however, the mechanisms involved remain poorly understood. We show here that nitric oxide (NO) generated by endothelial nitric oxide synthase (eNOS) controls the coalescence of protein kinase C-¿ (PKC-¿) at the central supramolecular activation cluster (c-SMAC) of the IS. eNOS translocated with the Golgi to the IS and partially colocalized with F-actin around the c-SMAC. This resulted in reduced actin polymerization and centripetal retrograde flow of ß-actin and PKC-¿ from the lamellipodium-like distal (d)-SMAC, promoting PKC-¿ activation. Furthermore, eNOS-derived NO S-nitrosylated ß-…

Life Sciences & Biomedicine - Other Topics0301 basic medicinePOLARIZATIONIMMUNOLOGICAL SYNAPSEImmunological SynapsesT-LymphocytesPROTEINGolgi ApparatusCYTOSKELETONRetrograde FlowBiochemistryARP2/3 COMPLEXT-CELL-ACTIVATIONProfilinsWhite Blood CellsContractile ProteinsFluorescence MicroscopyAnimal CellsMedicine and Health SciencesPseudopodiaBiology (General)Post-Translational ModificationCells CulturedProtein Kinase CMicroscopyT CellsGeneral NeuroscienceLight MicroscopyNeurochemistryRecombinant Proteins3. Good healthIsoenzymesPOLYMERIZATIONProtein TransportCell ProcessesRNA InterferenceCellular TypesNeurochemicalsGeneral Agricultural and Biological SciencesLife Sciences & BiomedicineResearch ArticleBiochemistry & Molecular BiologyNitric Oxide Synthase Type IIIQH301-705.5Imaging TechniquesRecombinant Fusion ProteinsImmune CellsImmunologyLibrary scienceAntigen-Presenting Cellsmacromolecular substancesBiologyNitric OxideResearch and Analysis MethodsGeneral Biochemistry Genetics and Molecular BiologyCell Line03 medical and health sciencesFluorescence ImagingHumansCysteineNITRIC-OXIDE SYNTHASEBiologyScience & TechnologyBlood CellsRECEPTORGeneral Immunology and MicrobiologyBiology and Life SciencesProteinsCell BiologyActinsS-NitrosylationEnzyme ActivationLuminescent ProteinsCytoskeletal Proteins030104 developmental biologyAmino Acid SubstitutionRETROGRADE FLOWProtein Kinase C-thetaMutationProtein Processing Post-TranslationalNeuroscienceActin PolymerizationPLoS biology
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Interactions of liposomes and hydrophobically-modified poly-(N-isopropylacrylamides): an attempt to model the cytoskeleton

1993

The interactions of small unilamellar vesicles (SUV) and water-soluble copolymers were studied by fluorescence spectroscopy, differential scanning calorimetry (DSC) and quasi-elastic light scattering (QELS). The anchoring onto liposomal bilayer membranes of copolymers of N-isopropylacrylamide, N-(2-(1-naphthyl)ethyl)-N-n-octadecylacrylamide and or N-[4-(1-pyrenyl)butyl]-N-n-octadecylacrylamide (0.5 mol% of the octadecylacrylamide comonomer) was monitored by non-radiative energy transfer between excited naphthalene and pyrene. The anchoring process occurred on zwitterionic lecithin liposomes and on negatively charged phosphatidic acid liposomes, whether the bilayer was in the crystalline or …

Lipid BilayersAcrylic ResinsBiophysicsSynthetic membranePhosphatidic AcidsModels BiologicalBiochemistryLower critical solution temperatureStructure-Activity Relationshipchemistry.chemical_compoundDifferential scanning calorimetryCopolymerOrganic chemistryCytoskeletonchemistry.chemical_classificationLiposomeBilayerComonomerCell BiologyPolymerchemistryChemical engineeringLiposomesPhosphatidylcholinesThermodynamicsDimyristoylphosphatidylcholineBiochimica et Biophysica Acta (BBA) - Biomembranes
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Exposure to cigarette smoke extract and lipopolysaccharide modifies cytoskeleton organization in bronchial epithelial cells

2017

The integrity of the respiratory epithelium is crucial for airway homeostasis. Tobacco smoke exposure and recurrent infections of the airways play a crucial role in the progression and in the decline of the respiratory function in chronic obstructive pulmonary disease (COPD). The aim of this study was to detect differentially expressed proteins in a bronchial epithelial cell line (16-HBE) stimulated with cigarette smoke extract (CSE) and lipopolysaccharide (LPS), a constituent of gram-negative bacteria, alone and/or in combination, by using two-dimensional electrophoresis (2DE) analysis coupled with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Western blot a…

Lipopolysaccharides0301 basic medicinePulmonary and Respiratory Medicinebronchial epithelial cells; cigarette smoke; cytoskeleton; Molecular Biology; Pulmonary and Respiratory Medicine; Clinical BiochemistryProteomeLipopolysaccharideCytoskeleton organizationClinical BiochemistryRespiratory MucosaCell Line03 medical and health scienceschemistry.chemical_compound0302 clinical medicineSmokebronchial epithelial cellHumansCigarette smokeMedicineCytoskeletonMolecular Biologybronchial epithelial cellsCytoskeletonbusiness.industrycigarette smokeTobacco smoke exposureEpithelial CellsTobacco Productsrespiratory systemrespiratory tract diseases030104 developmental biologyGene Expression Regulationchemistry030220 oncology & carcinogenesisImmunologyRespiratory epitheliumAirwaybusinessHomeostasisExperimental Lung Research
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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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Requirement of caveolae microdomains in extracellular signal-regulated kinase and focal adhesion kinase activation induced by endothelin-1 in primary…

1999

Endothelin-1 (ET-1) mitogenic activity in astrocytes is mediated by the activation of the extracellular signal-regulated kinase (ERK) pathway together with the Rho-dependent activation of the focal adhesion kinase (FAK) pathway. To clarify the mechanisms responsible for the coordinate activation of both pathways in the ET-1 signal propagation, the involvement of caveolae microdomains, suggested to play a role in signal transduction, was evaluated. In this study, it is reported that caveolae of primary astrocytes are enriched in endothelin receptor (ETB-R). Furthermore, signaling molecules such as the adaptor proteins Shc and Grb2, and the small G protein Rho, also reside within these microd…

MAPK/ERK pathwayCaveolin 1BiologyBiochemistryCaveolinsFocal adhesionCellular and Molecular Neurosciencechemistry.chemical_compoundCaveolaeCell AdhesionAnimalsFilipinPhosphorylationCells CulturedCytoskeletonMitogen-Activated Protein Kinase 1Endothelin-1Signal transducing adaptor proteinMembrane ProteinsTyrosine phosphorylationProtein-Tyrosine KinasesActinsCell biologyAnti-Bacterial AgentsCell CompartmentationRatsEnzyme ActivationchemistryAstrocytesFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesCaveolin 1Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinTyrosineGRB2Signal transductionExtracellular SpaceCell Adhesion MoleculesSignal TransductionJournal of neurochemistry
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