Search results for " Cytoskeleton"

showing 10 items of 105 documents

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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Actin binding LIM protein 3 (abLIM3).

2005

LIM domain proteins were demonstrated to play key roles in various biological processes such as embryonic development, cell lineage determination, and cancer differentiation. Actin binding LIM protein 1 (abLIM1) was reported to be localized in a genomic region often deleted in human cancers and suggested to be involved in axon guidance. Recently, existence of a second family member was reported, actin binding LIM protein 2. By means of computational biology and comparative genomics, we now characterized an additional, third member of the actin binding LIM protein subgroup, actin binding LIM protein 3 (abLIM3). The human mRNA sequence was previously annotated as differentially regulated in h…

Homeodomain ProteinsMicrofilament ProteinsMolecular Sequence DataSequence alignmentGeneral MedicineGenomicsBiologyActin cytoskeletonMolecular biologyConserved sequenceGeneticsAnimalsHumansABLIM1Tissue DistributionAmino Acid SequenceABLIM3LHX3Databases Nucleic AcidSequence AlignmentActinLIM domainInternational journal of molecular medicine
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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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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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Vezatin, a novel transmembrane protein, bridges myosin VIIA to the cadherin-catenins complex

2000

International audience; Defects in myosin VIIA are responsible for deafness in the human and mouse. The role of this unconventional myosin in the sensory hair cells of the inner ear is not yet understood. Here we show that the C-terminal FERM domain of myosin VIIA binds to a novel transmembrane protein, vezatin, which we identi®ed by a yeast two-hybrid screen. Vezatin is a ubiquitous protein of adherens cell±cell junctions, where it interacts with both myosin VIIA and the cadherin±catenins complex. Its recruitment to adherens junctions implicates the C-terminal region of a-catenin. Taken together, these data suggest that myosin VIIA, anchored by vezatin to the cadherin±catenins complex, cre…

MESH: Cytoskeletal ProteinsMESH: alpha CateninStereocilia (inner ear)[SDV]Life Sciences [q-bio]MESH: Amino Acid SequenceDeafnessMESH: CadherinsMiceMESH: Protein Structure Tertiary0302 clinical medicine[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseasesMyosinMESH: Hair Cells AuditoryMESH: AnimalsCytoskeleton0303 health sciencesFERM domainGeneral NeuroscienceMESH: Alternative SplicingArticlesCadherinsCell biologymedicine.anatomical_structureIntercellular Junctions[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyMyosin VIIaHair cellMESH: Membrane ProteinsMESH: DyneinsProtein BindingMESH: MutationMacromolecular SubstancesMolecular Sequence DataMESH: Deafnessmacromolecular substancesBiologyIn Vitro TechniquesMyosinsGeneral Biochemistry Genetics and Molecular BiologyCell LineAdherens junction03 medical and health sciencesHair Cells Auditorymedicineotorhinolaryngologic diseasesAnimalsHumansMESH: Myosin VIIaMESH: Protein BindingAmino Acid SequenceMolecular BiologyMESH: Mice030304 developmental biologyMESH: In Vitro TechniquesMESH: Molecular Sequence DataMESH: HumansGeneral Immunology and MicrobiologyCadherinDyneinsMembrane ProteinsMESH: Macromolecular SubstancesMESH: MyosinsActin cytoskeleton[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyProtein Structure TertiaryMESH: Cell LineAlternative SplicingCytoskeletal ProteinsMutationsense organs030217 neurology & neurosurgeryalpha Catenin[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyMESH: Intercellular Junctions
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TRPC1 is regulated by caveolin-1 and is involved in oxidized LDL-induced apoptosis of vascular smooth muscle cells.

2009

International audience; Oxidized low-density lipoprotein (oxLDL) induced-apoptosis of vascular cells may participate in plaque instability and rupture. We have previously shown that vascular smooth muscle cells (VSMC) stably expressing caveolin-1 were more susceptible to oxLDL-induced apoptosis than VSMC expressing lower level of caveolin-1, and this was correlated with enhanced Ca(2+) entry and pro-apoptotic events. In this study, we aimed to identify the molecular events involved in oxLDL-induced Ca(2+) influx and their regulation by the structural protein caveolin-1. In VSMC, transient receptor potential canonical-1 (TRPC1) silencing by ARN interference prevents the Ca(2+) influx and red…

MESH: Lipoproteins LDLVascular smooth muscleOxysterolCaveolin 1ApoptosisBiologyMESH: Base SequenceMESH : RNA Small InterferingMuscle Smooth VascularTRPC1Transient receptor potential channelMESH: RNA Small InterferingMESH : Cells CulturedHumansMESH: Caveolin 1RNA Small InterferingMESH: TRPC Cation ChannelsCells CulturedTRPC Cation ChannelsMESH: HumansBase SequenceMESH : Gene Expression RegulationMESH: ApoptosisMESH : HumansMESH : TRPC Cation ChannelsMESH : Muscle Smooth VascularArticlesCell BiologyMESH: Muscle Smooth VascularActin cytoskeletonMESH: Gene Expression RegulationCell biologyLipoproteins LDLGene Expression RegulationApoptosisCaveolin 1MESH : Caveolin 1Molecular Medicinelipids (amino acids peptides and proteins)MESH : Base SequenceMESH : Lipoproteins LDLHomeostasisMESH : ApoptosisMESH: Cells Cultured
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New neurons use Slit-Robo signaling to migrate through the glial meshwork and approach a lesion for functional regeneration

2018

Appropriate positioning of new neurons in the brain promotes post-stroke functional recovery.

Male0301 basic medicineanimal structuresNeurogenesisBiologyLesionMice03 medical and health sciences0302 clinical medicineDevelopmental NeuroscienceNeuroblastCell MovementNeuroblast migrationmental disordersmedicineAnimalsRegenerationcardiovascular diseasesReceptors ImmunologicProgenitor cellcdc42 GTP-Binding ProteinResearch Articlesreproductive and urinary physiologyMice KnockoutNeuronsMultidisciplinaryRegeneration (biology)fungiNeurogenesisSciAdv r-articlesBrainActin cytoskeletonSlit-RoboActin Cytoskeleton030104 developmental biologynervous systemCellular NeuroscienceAstrocytesembryonic structuresIntercellular Signaling Peptides and ProteinsProtein Multimerizationmedicine.symptomNeurogliaNeurosciencepsychological phenomena and processes030217 neurology & neurosurgeryResearch ArticleProtein BindingSignal TransductionScience Advances
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On the mechanism of action of phenylephrine in rat atrial heart muscle

1994

Both in rat left atrial heart and in aortic smooth muscle preparations, phenylephrine (PE) caused a concentration-dependent increase in force of contraction (FC) in the presence of atenolol (10 mumol/l), which was antagonized by phentolamine, prazosin and WB 4101 in a competitive manner. The pA2 values of the antagonists in the cardiac tissue were 10-20fold lower than those in the rat thoracic aorta. In the spontaneously beating right atrium, PE exerted a positive chronotropic action, which was not significantly antagonized by phentolamine or prazosin. It is therefore assumed that the effects of phenylephrine in the left atrium and in the aorta are mediated by different subtypes of alpha 1-…

MaleChronotropicmedicine.medical_specialtyPotassium ChannelsSodium-Hydrogen ExchangersAction PotentialsIn Vitro TechniquesRats Sprague-DawleyPhenylephrinePhentolamineHeart RateReceptors Adrenergic alpha-1medicine.arteryInternal medicinemedicinePrazosinAnimalsHeart AtriaPhenylephrineAdrenergic alpha-AntagonistsPharmacologyAortaChemistryCalcium RadioisotopesHeartGeneral MedicineAtenololMyocardial ContractionRatsElectrophysiologyActin CytoskeletonEndocrinologyMechanism of actioncardiovascular systemCalciummedicine.symptomAdrenergic alpha-Agonistsmedicine.drugMuscle contractionNaunyn-Schmiedeberg’s Archives of Pharmacology
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The Cannabinoid Receptor CB1 Interacts with the WAVE1 Complex and Plays a Role in Actin Dynamics and Structural Plasticity in Neurons.

2015

The molecular composition of the cannabinoid type 1 (CB1) receptor complex beyond the classical G-protein signaling components is not known. Using proteomics on mouse cortex in vivo, we pulled down proteins interacting with CB1 in neurons and show that the CB1 receptor assembles with multiple members of the WAVE1 complex and the RhoGTPase Rac1 and modulates their activity. Activation levels of CB1 receptor directly impacted on actin polymerization and stability via WAVE1 in growth cones of developing neurons, leading to their collapse, as well as in synaptic spines of mature neurons, leading to their retraction. In adult mice, CB1 receptor agonists attenuated activity-dependent remodeling o…

MaleReceptor complexCannabinoid receptorDendritic spineQH301-705.5medicine.medical_treatmentDendritic SpinesNeurogenesisRecombinant Fusion ProteinsGrowth ConesWiskott-Aldrich Syndrome Protein NeuronalNerve Tissue ProteinsBiologyCannabinoidergicGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesActin remodeling of neurons0302 clinical medicineReceptor Cannabinoid CB1Parietal LobeChlorocebus aethiopsmedicineAnimalsBiology (General)Cells Cultured030304 developmental biologyMice KnockoutNeurons0303 health sciencesNeuronal PlasticityGeneral Immunology and MicrobiologyCannabinoidsGeneral NeuroscienceNeurogenesisActin cytoskeletonEmbryo MammalianCell biologyFrontal LobeMice Inbred C57BLActin CytoskeletonLuminescent Proteinsnervous systemCOS Cellslipids (amino acids peptides and proteins)CannabinoidGeneral Agricultural and Biological Sciences030217 neurology & neurosurgeryResearch ArticlePLoS Biology
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