Search results for "MICROTUBULES"

showing 10 items of 71 documents

Papillote and Piopio:DrosophilaZP-domain proteins required for cell adhesion to the apical extracellular matrix and microtubule organization

2005

Adhesion between epithelial cells and extracellular substrates is normally mediated through basal adhesion complexes. However, some cells also possess comparable junctions on their apical surface. Here, we describe two new Drosophila proteins, Piopio and Papillote, that are required for the link between the apical epithelial surface and the overlying apical extracellular matrix (aECM). The two proteins share a zona pellucida (ZP) domain with mammalian aECM components, including the tectorins found in the vertebrate inner ear. Tagged versions of both proteins localized to the apical epithelial surface. Mutations in piopio, papillote and dumpy (another gene encoding a ZP-domain protein) cause…

Molecular Sequence DataBiologyMicrotubulesEpitheliumExtracellular matrixMicrotubuleCell AdhesionmedicineExtracellularAnimalsDrosophila ProteinsWings AnimalAmino Acid SequenceCell adhesionCytoskeletonZona pellucidaMicrotubule nucleationExtracellular Matrix ProteinsSequence Homology Amino AcidMembrane ProteinsEpithelial CellsCell BiologyExtracellular MatrixCell biologyMicroscopy ElectronDrosophila melanogasterPhenotypemedicine.anatomical_structureMicroscopy FluorescenceMutationCarrier ProteinsDrosophila ProteinJournal of Cell Science
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Endocytosis in skeletal muscle fibers.

1999

Defining the organization of endocytic pathway in multinucleated skeletal myofibers is crucial to understand the routing of membrane proteins, such as receptors and glucose transporters, through this system. Here we analyzed the organization of the endocytic trafficking pathways in isolated rat myofibers. We found that sarcolemmal-coated pits and transferrin receptors were concentrated in the I band areas. Fluid phase markers were taken up into vesicles in the same areas along the whole length of the fibers and were then delivered into structures around and between the nuclei. These markers also accumulated beneath the neuromuscular and myotendinous junctions. The recycling compartment, lab…

Monosaccharide Transport ProteinsEndosomeEndocytic cycleMuscle Fibers SkeletalFluorescent Antibody TechniqueGene ExpressionMuscle ProteinsTransferrin receptorEndosomesBiologyEndocytosisMicrotubulesSarcolemmaMicrotubuleReceptors TransferrinMyocyteAnimalsMuscle SkeletalCells Culturedchemistry.chemical_classificationGlucose Transporter Type 4Cell MembraneCoated Pits Cell-MembraneCell BiologyEndocytosisCell biologyCell CompartmentationRatsMicroscopy ElectronMembrane proteinchemistryTransferrinLysosomesExperimental cell research
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Microtubule Dynamics and Neuronal Excitability: Advances on Cytoskeletal Components Implicated in Epileptic Phenomena

2020

AbstractExtensive researches have deepened knowledge on the role of synaptic components in epileptogenesis, but limited attention has been devoted to the potential implication of the cytoskeleton. The study of the development of epilepsy and hyperexcitability states involves molecular, synaptic, and structural alterations of neuronal bioelectric activity. In this paper we aim to explore the neurobiological targets involved in microtubule functioning and cytoskeletal transport, i.e. how dynamic scaffolding of microtubules can influence neuronal morphology and excitability, in order to suggest a potential role for microtubule dynamics in the processes turning a normal neuronal network in a hy…

NeurodevelopmentHyperexcitabilityMicrotubuleBiologyMicrotubulesSettore BIO/09 - FisiologiaEpileptogenesisNeuroprotectionMicrotubule polymerizationCellular and Molecular NeuroscienceNeurotrophic factorsMicrotubulemedicineHumansPremovement neuronal activityCannabinoidCytoskeletonNeuronsEpilepsyNeurodegenerationCell BiologyGeneral Medicinemedicine.diseaseNeuroprotectionMicrotubule-Associated ProteinsNeuroscienceNeural developmentCellular and Molecular Neurobiology
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Analysis of the infectious entry pathway of human papillomavirus type 33 pseudovirions.

2002

AbstractHuman papillomavirus type 33 (HPV-33) pseudovirus infection is a slow process dependent on the initial interaction with cell-surface heparan sulfate (T. Giroglou, L. Florin, F. Schafer, R. E. Streeck, and M. Sapp, 2001a, J. Virol. 75, 1565–1570). We have now further dissected the initial steps of pseudovirus uptake using removal of cell-surface proteoglycans and selective inhibition of entry pathways. Treatment of cells with heparinase I, but not with phosphoinositol-specific phospholipase C (PIPLC), prevented binding of papillomavirus-like particles and infection with HPV-33 pseudovirions, indicating that GPI-linked proteoglycans (glypicans) are not required for productive infectio…

NystatinEndosomemedia_common.quotation_subjectvirus entryBiologypapillomavirusMicrotubulesendosomal acidificationchemistry.chemical_compoundViral entryVirologyAnimalsHumansInternalizationPapillomaviridaemedia_commonCytochalasin DCOS cellsPhospholipase CVirionpseudovirionsHeparan sulfateVirologyActinsCell biologyAnti-Bacterial AgentsNocodazolechemistryCOS CellsproteoglycansMacrolidesHeparan Sulfate ProteoglycansHeLa CellsVirology
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Role of Recycling Endosomes and Lysosomes in Dynein-Dependent Entry of Canine Parvovirus

2002

ABSTRACT Canine parvovirus (CPV) is a nonenveloped virus with a 5-kb single-stranded DNA genome. Lysosomotropic agents and low temperature are known to prevent CPV infection, indicating that the virus enters its host cells by endocytosis and requires an acidic intracellular compartment for penetration into the cytoplasm. After escape from the endocytotic vesicles, CPV is transported to the nucleus for replication. In the present study the intracellular entry pathway of the canine parvovirus in NLFK (Nordisk Laboratory feline kidney) cells was studied. After clustering in clathrin-coated pits and being taken up in coated vesicles, CPV colocalized with coendocytosed transferrin in endosomes r…

Parvovirus CanineEndosomeanimal diseasesvirusesImmunologyDyneinCoated vesicleEndosomesBiologyEndocytosisMicrobiologyMicrotubulesCell LineDogsMicrotubuleVirologyAnimalsMicroscopy ImmunoelectronIn Situ Hybridization FluorescenceMicroscopy ConfocalVesicleEndoplasmic reticulumDyneinsEndocytosisCell biologyVirus-Cell InteractionsCytoplasmInsect ScienceLysosomes
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Exploitation of Microtubule Cytoskeleton and Dynein during Parvoviral Traffic toward the Nucleus

2003

ABSTRACT Canine parvovirus (CPV), a model virus for the study of parvoviral entry, enters host cells by receptor-mediated endocytosis, escapes from endosomal vesicles to the cytosol, and then replicates in the nucleus. We examined the role of the microtubule (MT)-mediated cytoplasmic trafficking of viral particles toward the nucleus. Immunofluorescence and immunoelectron microscopy showed that capsids were transported through the cytoplasm into the nucleus after cytoplasmic microinjection but that in the presence of MT-depolymerizing agents, viral capsids were unable to reach the nucleus. The nuclear accumulation of capsids was also reduced by microinjection of an anti-dynein antibody. More…

Parvovirus CaninevirusesImmunoelectron microscopyImmunologyDyneinActive Transport Cell Nucleusmacromolecular substancesMicrotubulesMicrobiologyMotor proteinCapsidCytosolMicrotubuleVirologymedicineAnimalsCytoskeletonCytoskeletonCell NucleusbiologyDyneinsbiochemical phenomena metabolism and nutritionVirus-Cell InteractionsCell biologyMicroscopy ElectronTubulinmedicine.anatomical_structureCytoplasmInsect ScienceCatsbiology.proteinNucleusJournal of Virology
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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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Cell cycle studies on the mode of action of yeast K28 killer toxin.

1996

The virally encoded K28 killer toxin of Saccharomyces cerevisiae kills sensitive cells by a receptor-mediated process. DNA synthesis is rapidly inhibited, cell viability is lost more slowly and cells eventually arrest, apparently in the S phase of the cell cycle with a medium-sized bud, a single nucleus in the mother cell and a pre-replicated (1n) DNA content. Cytoplasmic microtubules appear normal, and no spindle is detectable. Arrest of a sensitive haploid yeast strain by alpha-factor at START gave complete protection for at least 4 h against a toxin concentration that killed non-arrested cells at the rate of one log each 2.5 h. Cells released from alpha-factor arrest were killed by toxin…

Saccharomyces cerevisiae ProteinsCellSaccharomyces cerevisiaeSaccharomyces cerevisiaeBiologyMicrobiologyMicrotubulesS Phase4-ButyrolactonemedicineViability assayS phaseGeneticsDNA synthesisCell DeathCell CycleDNACell cycleMycotoxinsbiology.organism_classificationFlow CytometryKiller Factors YeastCell biologySpindle poisonmedicine.anatomical_structureCytoplasmFluorescent Antibody Technique Directmedicine.drugMicrobiology (Reading, England)
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Design and synthesis of pironetin analogue/colchicine hybrids and study of their cytotoxic activity and mechanisms of interaction with tubulin

2014

We here report the synthesis of a series of 12 hybrid molecules composed of a colchicine moiety and a pironetin analogue fragment. The two fragments are connected through an ester-amide spacer of variable length. The cytotoxic activities of these compounds and their interactions with tubulin have been investigated. Relations between the structure and activity are discussed. Since the spacer is not long enough to permit a simultaneous binding of the hybrid molecules to the colchicine and pironetin sites on tubulin, a further feature investigated was whether these molecules would interact with the latter through the pironetin end (irreversible covalent binding) or through the colchicine end (…

StereochemistryChemical structureCellsFluorescent Antibody TechniqueAntineoplastic AgentsLigandsMicrotubulespironetinStructure-Activity Relationshipchemistry.chemical_compoundChemical structureTubulinNeoplasmsDrug DiscoveryTumor Cells CulturedHumansColchicineMoietyMoleculeStructure–activity relationshipBinding siteCell ProliferationPharmacologyBinding SitesDrug effectsMolecular StructurebiologyToxicityCell growthMoleculesTubulinchemistryPyronesDrug Designbiology.proteinMolecular MedicineColchicineJournal of Medicinal Chemistry
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Water-soluble isoindolo[2,1-a]quinoxalin-6-imines: In vitro antiproliferative activity and molecular mechanism(s) of action

2015

Abstract Water-soluble isoindoloquinoxalin (IIQ) imines and the corresponding acetates were conveniently prepared from the key intermediates 2-(2′-aminophenyl)-2H-isoindole-1-carbonitriles obtained by a Strecker reaction between substituted 1,2-dicarbaldehydes and 1,2-phenylenediamines. Both series were screened by the National Cancer Institute (Bethesda, MD) and showed potent antiproliferative activity against a panel of 60 human tumor cell lines. Several of the novel compounds showed GI50 values at a nanomolar level on the majority of the tested cell lines. Among IIQ derivatives, methoxy substituents at positions 3 and 8 or/and 9 were especially effective in impairing cell cycle progressi…

StereochemistryStrecker amino acid synthesisAntineoplastic AgentsApoptosisIsoindolo[21-a]quinoxalin-6-imineTopoisomerase I inhibitorsTopoisomerase-I InhibitorMicrotubulesTubulinCell Line TumorQuinoxalinesDrug DiscoveryHumansCytotoxic T cellCell ProliferationPharmacologyTopoisomerase I inhibitorChemistryAntitubulin agents; G-quadruplex interaction; Isoindolo[2; 1-a]quinoxalin-6-imines; Topoisomerase I inhibitors; Drug Discovery3003 Pharmaceutical Science; Organic Chemistry; PharmacologyAntitubulin agentsDrug Discovery3003 Pharmaceutical ScienceCell CycleOrganic ChemistryWaterGeneral MedicineSettore CHIM/08 - Chimica FarmaceuticaIn vitroTelomereAntitubulin agentAntitubulin agents; G-quadruplex interaction; Isoindolo[21-a]quinoxalin-6-imines; Topoisomerase I inhibitors; Drug Discovery3003 Pharmaceutical Science; Organic Chemistry; Pharmacology1-a]quinoxalin-6-iminesDNA Topoisomerases Type ISolubilityBiochemistryCell cultureApoptosisIsoindolo[2Cancer cellIminesG-quadruplex interactionDrug Screening Assays Antitumor
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