Search results for "Actin cytoskeleton"

showing 10 items of 98 documents

Identification and relevance of the CD95-binding domain in the N-terminal region of ezrin.

2003

The CD95 (Fas/APO-1) linkage to the actin cytoskeleton through ezrin is an essential requirement for susceptibility to the CD95-mediated apoptosis in CD4+ T cells. We have previously shown that moesin was not involved in the binding to CD95. Here we further support the specificity of the ezrin/CD95 binding, showing that radixin did not bind CD95. The ezrin region specifically and directly involved in the binding to CD95 was located in the middle lobe of the ezrin FERM domain, between amino acids 149 and 168. In this region, ezrin, radixin, and moesin show 60-65% identity, as compared with the 86% identity in the whole FERM domain. Transfection of two different human cell lines with a green …

Moesinchemical and pharmacologic phenomenaApoptosismacromolecular substancesBiologyBiochemistryEzrinRadixinhemic and lymphatic diseasesHumansfas ReceptorMolecular BiologyActinBinding SitesFERM domainhemic and immune systemsCell BiologyTransfectionActin cytoskeletonPhosphoproteinsActinsCell biologyProtein Structure TertiaryCytoskeletal ProteinsMutationbiological phenomena cell phenomena and immunityBinding domainHeLa CellsProtein BindingSignal TransductionThe Journal of biological chemistry
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MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal melanosomes

2002

Defects of the myosin VIIa motor protein cause deafness and retinal anomalies in humans and mice. We report on the identification of a novel myosin-VIIa-interacting protein that we have named MyRIP (myosin-VIIa- and Rab-interacting protein), since it also binds to Rab27A in a GTP-dependent manner. In the retinal pigment epithelium cells, MyRIP, myosin VIIa and Rab27A are associated with melanosomes. In transfected PC12 cells, overexpression of MyRIP was shown to interfere with the myosin VIIa tail localization. We propose that a molecular complex composed of Rab27A, MyRIP and myosin VIIa bridges retinal melanosomes to the actin cytoskeleton and thereby mediates the local trafficking of thes…

Molecular Sequence Datamacromolecular substancesMyosinsBiologyBiochemistryRetinarab27 GTP-Binding ProteinsMotor proteinMicechemistry.chemical_compoundTwo-Hybrid System Techniquesotorhinolaryngologic diseasesGeneticsmedicineAnimalsHumansAmino Acid SequenceRAB27Molecular BiologyGene LibraryMelanosomesRetinal pigment epitheliumScientific ReportsDyneinsRetinalActin cytoskeletonCell biologymedicine.anatomical_structurechemistryOrgan Specificityrab GTP-Binding ProteinsMelanosome transportMyosin VIIaMelanophilinsense organsRabSequence Alignmentcirculatory and respiratory physiologyEMBO reports
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Influence of cadmium on the morphology and functionality of haemocytes in the compound ascidian Botryllus schlosseri

2013

In order to get insights into the effects of cadmium (Cd) on cell morphology and functions, we exposed haemocytes of the colonial ascidian Botryllus schlosseri to sub-lethal concentrations of CdCl(2). Results indicate that Cd hampers haemocyte spreading and phagocytosis in a dose-dependent way, through the alteration of the actin cytoskeleton. In addition, the metal decreases the stability of the internal membranes, as revealed by the Neutral Red assay. The fraction of cells showing positivity for the lysosomal enzyme acid phosphatase is also reduced in the presence of Cd, whereas the number of cells responsive to the Annexin-V assay and showing chromatin condensation increases, suggesting …

Neutral redHemocytesAscidiansPhysiologyCell SurvivalHealth Toxicology and MutagenesisPhagocytosisApoptosisBotryllus schlosseriToxicologyCell morphologyBiochemistrychemistry.chemical_compoundPhagocytosisSuperoxidesCell AdhesionAnimalsUrochordataBotryllus sp.; Ascidians; Haemocytes; Toxicity; CadmiumHaemocytesbiologyCell DeathToxicitySuperoxideCell MembraneAcid phosphataseCell BiologyGeneral MedicineAnatomyActin cytoskeletonbiology.organism_classificationChromatinPhosphoric Monoester HydrolasesCell biologyActin CytoskeletonOxidative StresschemistryBotryllus spApoptosisbiology.proteinMetallothioneinLysosomesOxidation-ReductionCadmium
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Htid-1, the human homolog of the Drosophila melanogaster l(2)tid tumor suppressor, defines a novel physiological role of APC.

2007

Htid-1, the human counterpart of the Drosophila tumor suppressor gene lethal(2)tumorous imaginal discs (l(2)tid) encodes three splice forms translated into three cytosolic - Tid50, Tid48 and Tid46 - and three mitochondrial - Tid43, Tid40 and Tid38 - proteins. Here we provide evidence for the association of the endogenous Tid50/Tid48 proteins with the adenomatous polyposis coli (APC) tumor suppressor in normal colon epithelium, colorectal cancer cells and mouse NIH3T3 fibroblasts. Using the Glutathione S-transferase binding assay we show that the N-terminal region including the Armadillo domain (ARM) of APC is sufficient to bind the Tid molecules. Using immunoprecipitation and confocal micro…

Patched ReceptorsBeta-cateninTumor suppressor geneAdenomatous polyposis coliAdenomatous Polyposis Coli ProteinReceptors Cell SurfacePlasma protein bindingLigandsMitochondrial ProteinsMiceCytosolCell Line TumorAnimalsDrosophila ProteinsGuanine Nucleotide Exchange FactorsHumansIntestinal MucosaActinHeat-Shock Proteinsbeta CateninPatched ReceptorsbiologySequence Homology Amino AcidGene Expression ProfilingTumor Suppressor ProteinsWnt signaling pathwayGene Expression Regulation DevelopmentalCell BiologyHSP40 Heat-Shock ProteinsActin cytoskeletonMolecular biologyCell biologyMitochondriaDrosophila melanogasterras GTPase-Activating ProteinsMultiprotein Complexesbiology.proteinNIH 3T3 CellsRho Guanine Nucleotide Exchange FactorsProtein BindingCellular signalling
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Protein surplus myopathies and other rare congenital myopathies.

2002

The protein surplus myopathies have emerged as a newly recognized subgroup of morphologically defined myopathies within the spectrum of congenital myopathies because of the accumulation of protein aggregates, some of them mutant proteins. Currently, nosologic, including molecular criteria include desmin-related myopathies, actinopathies, and hereditary inclusion body myopathies, whereas hyaline body myopathy is still a putative form of protein surplus myopathy because of lack of any molecular data. The congenital myopathies (CM), foremost including nemaline and myotubular myopathies, have given evidence that, despite their epidemiologic rarity, the molecular age has dawned in CM and has eve…

Pathologymedicine.medical_specialtyAdolescentInfantHyaline bodyBiologyDesminActin CytoskeletonChild PreschoolPediatrics Perinatology and Child HealthmedicineHumansPoint MutationNeurology (clinical)medicine.symptomMyopathyChildCytoskeletonMyopathies Structural CongenitalSeminars in pediatric neurology
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Nuclear actin aggregation is a hallmark of anti-synthetase syndrome-induced dysimmune myopathy

2015

Objective: To analyze antisynthetase syndrome–associated myositis by modern myopathologic methods and to define its place in the spectrum of idiopathic inflammatory myopathies (IIMs). Methods: Skeletal muscle biopsies from antisynthetase syndrome–associated myositis and other IIMs from different institutions worldwide were analyzed by histopathology, quantitative PCR, and electron microscopy. Results: Myonuclear actin filament inclusions were identified as a unique morphologic hallmark of antisynthetase syndrome–associated myositis. Nuclear actin inclusions were never found in dermatomyositis, polymyositis, sporadic inclusion body myositis, autoimmune necrotizing myopathy associated with si…

Pathologymedicine.medical_specialtyBiopsyIntranuclear Inclusion Bodies10208 Institute of Neuropathology610 Medicine & healthAntisynthetase syndromeBiologyPolymyositisSensitivity and SpecificityNecrosisPerimysialmedicineHumansMyopathyMuscle SkeletalMyositisMyositisDermatomyositisActin cytoskeletonmedicine.diseaseAutoimmune necrotizing myopathyActins10040 Clinic for NeurologyActin Cytoskeleton2728 Neurology (clinical)Immunology570 Life sciences; biologyNeurology (clinical)medicine.symptom
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Endothelial nitric oxide synthase upregulation in the guinea pig organ of Corti after acute noise trauma.

2004

Endothelial nitric oxide synthase (eNOS) upregulation was identified 60 h after acute noise trauma in morphologically intact cells of the reticular lamina in the organ of Corti of the guinea pig in the second turn of the cochlea. Using gold-coupled anti-eNOS antibodies and electron microscopy, it was shown that eNOS expression was upregulated in all cell areas and cell types except inner hair cells. Furthermore, eNOS was found in the organelle-free cytoplasm and in mitochondria of various cell types. The density of eNOS in mitochondria was considerably higher compared with the surrounding cytoplasm. Since eNOS activity is regulated by calcium, the eNOS detection was combined with calcium pr…

Pathologymedicine.medical_specialtyCytoplasmNitric Oxide Synthase Type IIIGuinea Pigschemistry.chemical_elementCalciumMicrotubulesDownregulation and upregulationMicroscopy Electron TransmissionEnosStress PhysiologicalHair Cells AuditorymedicineAnimalsCalcium SignalingMolecular BiologyOrgan of CortiCytoskeletonbiologyGeneral NeuroscienceNitric Oxide Synthase Type IIIbiology.organism_classificationImmunohistochemistryCell biologyMitochondriaUp-RegulationNitric oxide synthaseActin CytoskeletonDisease Models Animalmedicine.anatomical_structureDrosophila melanogasterchemistryAcoustic StimulationHearing Loss Noise-InducedCytoplasmOrgan of Cortibiology.proteinCalciumNeurology (clinical)Nitric Oxide SynthaseNoiseIntracellularDevelopmental BiologyBrain research
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2015

The pathogenesis of glaucoma, a common neurodegenerative disease, involves an immunologic component. Changes in the natural autoantibody profile of glaucoma patients were detected, showing not only up-regulated but also down-regulated immunoreactivities. In recent studies we were able to demonstrate that the antibody changes have a large influence on protein profiles of neuroretinal cells. Furthermore we could demonstrate neuroprotective potential of one of the down-regulated antibodies (γ-synuclein antibody). Anti-GFAP antibody is another antibody found down-regulated in glaucoma patients. Since GFAP expression is intensified in glaucomatous retina, the aim of this study was to detect the …

PharmacologyRetinaGlial fibrillary acidic proteinbiologymedicine.diagnostic_testAutoantibodyActin cytoskeletonGFAP stainMolecular biologyNeuroprotectionmedicine.anatomical_structureWestern blotbiology.proteinmedicineMolecular Medicinesense organsAntibodyJournal of Pharmacological Sciences
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Inhibition of Receptor Signaling to Phospholipase D by Clostridium difficile Toxin B

1996

Rho proteins have been reported to activate phospholipase D (PLD) in in vitro preparations. To examine the role of Rho proteins in receptor signaling to PLD, we studied the effect of Clostridium difficile toxin B, which glucosylates Rho proteins, on the regulation of PLD activity in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor (mAChR). Toxin B treatment of HEK cells potently and efficiently blocked mAChR-stimulated PLD. In contrast, basal and phorbol ester-stimulated PLD activities were not or only slightly reduced. Cytochalasin B and Clostridium botulinum C2 toxin, mimicking the effect of toxin B on the actin cytoskeleton but without involvi…

Phospholipase DG proteinClostridium difficile toxin AClostridium difficile toxin BCell BiologyBiologymedicine.disease_causeActin cytoskeletonBiochemistryMolecular biologyenzymes and coenzymes (carbohydrates)chemistry.chemical_compoundchemistrymedicineClostridium botulinumlipids (amino acids peptides and proteins)Signal transductionMolecular BiologyCytochalasin BJournal of Biological Chemistry
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Clustering induces a lateral redistribution of α2β1 integrin from membrane rafts to caveolae and subsequent protein kinase C-dependent internalization

2004

Integrin alpha 2 beta 1 mediates the binding of several epithelial and mesenchymal cell types to collagen. The composition of the surrounding plasma membrane, especially caveolin-1- and cholesterol-containing membrane structures called caveolae, may be important to integrin signaling. On cell surface alpha 2 beta 1 integrin was located in the raft like membrane domain, rich in GPI-anchored proteins, rather than in caveolae. However, when antibodies were used to generate clusters of alpha 2 beta 1 integrin, they started to move laterally on cell surface along actin filaments. During the lateral movement small clusters fused together. Finally alpha 2 beta 1 integrin was found inside caveolae …

Protein Kinase C-alphaEndosomeintegrinkinasemedia_common.quotation_subjectCaveolin 1IntegrinCoated VesiclesEndosomesCaveolaeCaveolinsCell Membrane StructuresCD49cCollagen receptorCell membraneCaveolaemedicineHumansantibodiesMicroscopy ImmunoelectronInternalizationMolecular BiologyCells CulturedProtein Kinase Cmedia_commonbiologyCell MembraneArticlesCell BiologyIntegrin alphaVproteinsEnterovirus B HumanCell biologyActin Cytoskeletonmedicine.anatomical_structureIntegrin alphaVcaveolaebiology.proteinIntegrin alpha2beta1
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