Search results for "microtubule"

showing 10 items of 232 documents

Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein.

2008

AbstractCentrins are Ca2+-binding EF-hand proteins. All four known centrin isoforms are expressed in the ciliary apparatus of photoreceptor cells. Cen1p and Cen2p bind to the visual G-protein transducin in a strictly Ca2+-dependent way, which is thought to regulate light driven movements of transducin between photoreceptor cell compartments. These relatively slow motile processes represent a novel paradigm in light adaptation of photoreceptor cells.Here we validated specific phosphorylation as a novel regulator of centrins in photoreceptors. Centrins were differentially phosphorylated during photoreceptor dark adaptation. Inhibitor treatments revealed protein kinase CK2 as the major protein…

genetic structuresLightG proteinVisionChromosomal Proteins Non-HistoneBlotting WesternDark AdaptationBiologySignal transductionMicrotubulesPhotoreceptor cellMass SpectrometryCa2+-binding proteinsSubstrate SpecificityRats Sprague-DawleyMiceHeterotrimeric G proteinmedicineAnimalsCiliaTransducinPhosphorylationProtein kinase ACasein Kinase IIFluorescent Antibody Technique IndirectMicroscopy ImmunoelectronMolecular BiologyCytoskeletonCiliumCalcium-Binding ProteinsCell BiologyCell biologyRatsMice Inbred C57BLmedicine.anatomical_structureCentrinPhosphorylationHeterotrimeric G-proteinCalciumCattleTransducinsense organsMolecular translocationPhotoreceptor Cells VertebrateProtein BindingBiochimica et biophysica acta
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Apoptotic-like Leishmania exploit the host´s autophagy machinery to reduce T-cell-mediated parasite elimination

2015

Apoptosis is a well-defined cellular process in which a cell dies, characterized by cell shrinkage and DNA fragmentation. In parasites like Leishmania, the process of apoptosis-like cell death has been described. Moreover upon infection, the apoptotic-like population is essential for disease development, in part by silencing host phagocytes. Nevertheless, the exact mechanism of how apoptosis in unicellular organisms may support infectivity remains unclear. Therefore we investigated the fate of apoptotic-like Leishmania parasites in human host macrophages. Our data showed--in contrast to viable parasites--that apoptotic-like parasites enter an LC3(+), autophagy-like compartment. The compartm…

log.ph logarithmic phaseT-LymphocytesApoptosisMACS magnetic-associated cell sortingMacrophageMFI mean fluorescence intensityLeishmaniasisMOI multiplicity of infectionanti-inflammatoryLeishmaniaeducation.field_of_studyPhagocytesCFSE carboxyfluorescein succinimidyl esterTGFB transforming growth factorAcquired immune systemapoptotic-like LeishmaniaPS phosphatidylserinehuman primary macrophagesCell biologyβ; TT tetanus toxoidCorrigendumProgrammed cell deathautophagyPopulationAntigen presentationANXA5 annexin VBasic Science Research PapersBiologyPhagocytosisCM complete mediumMAP1LC3/LC3 microtubule-associated protein 1 light chain 3AnimalsHumansMHC major histocompatibility complexIF immunofluorescenceeducationMolecular Biologyimmune evasionPBMCs peripheral blood mononuclear cellsT-cell proliferationIntracellular parasiteMacrophagesstat.ph stationary phaseAutophagyLm LeishmaniaCell BiologyLeishmaniabiology.organism_classificationIL interleukinLAP LC3-associated phagocytosisLAPhMDM human monocyte derived macrophageAutophagy
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Histamine and spontaneously released mast cell granules affect the cell growth of human hepatocellular carcinoma cells

2007

The role of mast cells in tumor growth is still controversial. In this study we analyzed the effects of both histamine and pre-formed mediators spontaneously released by mast cells on the growth of two human hepatocellular carcinoma cell lines, HA22T/VGH and HuH-6, with different characteristics of differentiation, biological behavior and genetic defects. We showed that total mast cell releasate, exocytosed granules (granule remnants) and histamine reduced cell viability and proliferation in HuH-6 cells. In contrast, in HA22T/VGH cells granule remnants and histamine induced a weak but significant increase in cell growth. We showed that both cell lines expressed histamine receptors H(1) and …

medicine.medical_specialtyCarcinoma HepatocellularCell SurvivalSurvivinClinical BiochemistryHistamine AntagonistsApoptosisHistamine H1 receptorBiologyRanitidineBiochemistryExocytosisInhibitor of Apoptosis ProteinsHistamine receptorchemistry.chemical_compoundInternal medicineCell Line TumormedicineAnimalsHumansHistamine H4 receptorMast CellsEnterochromaffin-like cellRats WistarMolecular BiologyCells Culturedbeta CateninCell ProliferationCell growthCaspase 3Liver NeoplasmsMast cellMolecular biologyNeoplasm ProteinsRatsEnzyme ActivationEndocrinologymedicine.anatomical_structurechemistryCell cultureCyclooxygenase 2Molecular MedicineReceptors HistamineFemaleTerfenadinePoly(ADP-ribose) PolymerasesMicrotubule-Associated ProteinsHistamineHistamine
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Translation of HTT mRNA with expanded CAG repeats is regulated by the MID1-PP2A protein complex.

2012

Expansion of CAG repeats is a common feature of various neurodegenerative disorders, including Huntington's disease. Here we show that expanded CAG repeats bind to a translation regulatory protein complex containing MID1, protein phosphatase 2A and 40S ribosomal S6 kinase. Binding of the MID1-protein phosphatase 2A protein complex increases with CAG repeat size and stimulates translation of the CAG repeat expansion containing messenger RNA in a MID1-, protein phosphatase 2A- and mammalian target of rapamycin-dependent manner. Our data indicate that pathological CAG repeat expansions upregulate protein translation leading to an overproduction of aberrant protein and suggest that the MID1-com…

metabolism [Microtubule Proteins]General Physics and AstronomyHTT protein humanRibosomal s6 kinaseMice0302 clinical medicinemetabolism [Transcription Factors]Protein Phosphatase 2Luciferasesgenetics [Nerve Tissue Proteins]genetics [Protein Biosynthesis]0303 health sciencesHuntingtin ProteinMultidisciplinarybiologyTOR Serine-Threonine KinasesNuclear ProteinsTranslation (biology)3. Good healthmetabolism [Luciferases]Microtubule Proteinsddc:500metabolism [Nuclear Proteins]genetics [Trinucleotide Repeat Expansion]Protein Bindingcongenital hereditary and neonatal diseases and abnormalitiesMTOR protein humanUbiquitin-Protein LigasesBlotting WesternNerve Tissue Proteinsmetabolism [TOR Serine-Threonine Kinases]metabolism [RNA Messenger]General Biochemistry Genetics and Molecular Biology03 medical and health sciencesgenetics [RNA Messenger]mental disordersHuntingtin ProteinAnimalsHumansEukaryotic Small Ribosomal SubunitRNA MessengerNucleotide Motifs030304 developmental biologyMessenger RNAmetabolism [Nerve Tissue Proteins]RNAmetabolism [Protein Phosphatase 2]General ChemistryProtein phosphatase 2Molecular biologynervous system diseasesProtein Biosynthesisbiology.proteinTrinucleotide repeat expansionTrinucleotide Repeat Expansion030217 neurology & neurosurgeryMid1 protein humanHeLa CellsTranscription FactorsNature communications
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The E3 Ubiquitin Ligase MID1 Catalyzes Ubiquitination and Cleavage of Fu

2014

Sonic Hedgehog (SHH)-GLI signalling plays an important role during embryogenesis and in tumorigenesis. The survival and growth of several types of cancer depend on autonomously activated SHH-GLI signalling. A protein complex containing the ubiquitin-ligase MID1 and protein phosphatase 2A (PP2A) regulates the nuclear localization and transcriptional activity of GLI3, a transcriptional effector molecule of SHH, in cancer cell lines with autonomously activated SHH signalling. However, the exact molecular mechanisms that mediate the interaction between MID1 and GLI3 remained unknown. Here, we show that MID1 catalyses the ubiquitination and proteasomal cleavage of the GLI3-regulator Fu. Our data…

metabolism [Microtubule Proteins]Ubiquitin-conjugating enzymeBiochemistrymetabolism [Protein Serine-Threonine Kinases]Ubiquitinmetabolism [Transcription Factors]Nuclear proteinSonic hedgehogbiologymetabolism [Protein-Serine-Threonine Kinases]Nuclear Proteinsrespiratory systemProtein-Serine-Threonine KinasesUbiquitin ligaseGene Expression Regulation NeoplasticGLI3 protein humanBiochemistryddc:540embryonic structuresMicrotubule Proteinsmetabolism [Hedgehog Proteins]Function and Dysfunction of the Nervous Systemmetabolism [Nuclear Proteins]Signal Transductionmetabolism [Kruppel-Like Transcription Factors]Proteasome Endopeptidase Complexanimal structuresSTK36 protein humanUbiquitin-Protein LigasesKruppel-Like Transcription FactorsNerve Tissue ProteinsProtein Serine-Threonine Kinaseschemistry [Ubiquitin-Protein Ligases]CatalysisZinc Finger Protein Gli3Cell Line TumorGLI3HumansHedgehog Proteinsmetabolism [Proteasome Endopeptidase Complex]metabolism [Cell Nucleus]Molecular Biologychemistry [Lysine]DNA PrimersCell Nucleusmetabolism [Nerve Tissue Proteins]UbiquitinLysineUbiquitinationCell BiologyProtein phosphatase 2chemistry [Ubiquitin]Proteasomebiology.proteinSHH protein humanhuman activitiesMid1 protein humanHeLa CellsTranscription FactorsJournal of Biological Chemistry
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Endoderm development requires centrioles to restrain p53-mediated apoptosis in the absence of ERK activity

2021

Centrioles comprise the heart of centrosomes, microtubule-organizing centers. To study the function of centrioles in lung and gut development, we genetically disrupted centrioles throughout the mouse endoderm. Surprisingly, removing centrioles from the endoderm did not disrupt intestinal growth or development but blocked lung branching. In the lung, acentriolar SOX2-expressing airway epithelial cells apoptosed. Loss of centrioles activated p53, and removing p53 restored survival of SOX2-expressing cells, lung branching, and mouse viability. To investigate how endodermal p53 activation specifically killed acentriolar SOX2-expressing cells, we assessed ERK, a prosurvival cue. ERK was active t…

p53Cell SurvivalApoptosisInbred C57BLMedical and Health SciencesArticleGeneral Biochemistry Genetics and Molecular BiologyMiceMorphogenesis2.1 Biological and endogenous factorsAnimalscentrioleintestine developmentAetiologyExtracellular Signal-Regulated MAP KinasesendodermLungMolecular BiologyCentriolesSOXB1 Transcription FactorsStem CellsEndodermapoptosisEpithelial CellsCell BiologyBiological SciencesIntestinesMice Inbred C57BLlung branchingERKembryonic structuresTumor Suppressor Protein p53Microtubule-Associated ProteinsDevelopmental BiologyDevelopmental Cell
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Molecular Mechanisms of the Blockage of Glioblastoma Motility

2021

Glioblastoma (GBM) is the most common and lethal brain tumor. GBM has a remarkable degree of motility and is able to infiltrate the healthy brain. In order to perform a rationale-based drug-repositioning study, we have used known inhibitors of two small Rho GTPases, Rac1 and Cdc42, which are upregulated in GBM and are involved in the signaling processes underlying the orchestration of the cytoskeleton and cellular motility. The selected inhibitors (R-ketorolac and ML141 for Cdc42 and R-ketorolac and EHT 1864 for Rac1) have been successfully employed to reduce the infiltration propensity of GBM in live cell imaging studies. Complementarily, all-atom simulations have elucidated the molecular …

rac1 GTP-Binding Proteinrho GTP-Binding ProteinsGeneral Chemical EngineeringBrain tumorMotilityRAC1CDC42Library and Information SciencesBiologySettore BIO/09 - FisiologiaMicrotubules01 natural sciencesDownregulation and upregulationLive cell imaging0103 physical sciencesmedicineHumanscdc42 GTP-Binding Protein010304 chemical physicsDrug discoveryCancerGeneral Chemistrymedicine.disease0104 chemical sciencesComputer Science Applications010404 medicinal & biomolecular chemistrySettore CHIM/03 - Chimica Generale E InorganicaCancer researchGlioblastomaJournal of Chemical Information and Modeling
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A novel microtubule de-stabilizing complementarity-determining region C36L1 peptide displays antitumor activity against melanoma in vitro and in vivo

2015

AbstractShort peptide sequences from complementarity-determining regions (CDRs) of different immunoglobulins may exert anti-infective, immunomodulatory and antitumor activities regardless of the specificity of the original monoclonal antibody (mAb). In this sense, they resemble early molecules of innate immunity. C36L1 was identified as a bioactive light-chain CDR1 peptide by screening 19 conserved CDR sequences targeting murine B16F10-Nex2 melanoma. The 17-amino acid peptide is readily taken up by melanoma cells and acts on microtubules causing depolymerization, stress of the endoplasmic reticulum and intrinsic apoptosis. At low concentrations, C36L1 inhibited migration, invasion and proli…

rho GTP-Binding ProteinsMelanoma ExperimentalAntineoplastic AgentsApoptosisPeptideComplementarity determining regionBiologyEndoplasmic ReticulumMicrotubulesArticleMicePhosphatidylinositol 3-KinasesCell MovementTubulinCell Line TumormedicineAnimalsNeoplasm MetastasisMelanomaPI3K/AKT/mTOR pathwayCell Proliferationchemistry.chemical_classificationMultidisciplinaryInnate immune systemCell growthMelanomaIntrinsic apoptosisPTEN Phosphohydrolasemedicine.diseaseComplementarity Determining RegionsMolecular biologyMitochondriaDisease Models AnimalchemistryCell cultureCancer researchProtein MultimerizationPeptidesProto-Oncogene Proteins c-aktSignal TransductionScientific Reports
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Chronic ethanol exposure alters the levels, assembly, and cellular organization of the actin cytoskeleton and microtubules in hippocampal neurons in …

2010

The organization and dynamics of microtubules (MTs) and the actin cytoskeleton are critical for the correct development and functions of neurons, including intracellular traffic and signaling. In vitro ethanol exposure impairs endocytosis, exocytosis, and nucleocytoplasmic traffic in astrocytes and alters endocytosis in cultured neurons. In astrocytes, these effects relate to changes in the organization and/or function of MTs and the actin cytoskeleton. To evaluate this possibility in hippocampal cultured neurons, we analyzed if chronic ethanol exposure affects the levels, assembly, and cellular organization of both cytoskeleton elements and the possible underlying mechanisms of these effec…

rho GTP-Binding ProteinsRHOAArp2/3 complexmacromolecular substancesToxicologyFilamentous actinHippocampusMicrotubulesActin cytoskeleton organizationActin remodeling of neuronsAnimalsCytoskeletonCells CulturedCytoskeletonNeuronsbiologyEthanolCentral Nervous System DepressantsActin cytoskeletonActinsCell biologyRatsSomatodendritic compartmentbiology.proteinFemaleSignal TransductionToxicological sciences : an official journal of the Society of Toxicology
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Design, synthesis and structure-activity relationship of 2-(3',4',5'-trimethoxybenzoyl)-benzo[b]furan derivatives as a novel class of inhibitors of t…

2009

The biological importance of microtubules in mitosis and cell division makes them an interesting target for the development of anticancer agents. Small molecules such as benzo[b]furans are attractive as inhibitors of tubulin polymerization. Thus, a new class of inhibitors of tubulin polymerization based on the 2-(3′,4′,5′-trimethoxybenzoyl)-benzo[b]furan molecular skeleton, with electron-donating (Me, OMe or OH) or electron-withdrawing (F, Cl and Br) substituents on the benzene ring, was synthesized and evaluated for antiproliferative activity, inhibition of tubulin polymerization and cell cycle effects. Adding a methyl group at the C-3 position resulted in increased activity. The most prom…

structure-activityStereochemistryClinical BiochemistryPharmaceutical ScienceAntineoplastic Agentsmacromolecular substancesBiochemistryChemical synthesisArticleStructure-Activity Relationshipchemistry.chemical_compoundbenzo[b]furansMicrotubuleCell Line TumorFuranDrug DiscoveryHumansStructure–activity relationshipMolecular BiologyBenzofuransCell ProliferationBinding SitesDose-Response Relationship DrugbiologyChemistryTubulin ModulatorsCell growthCell CycleOrganic ChemistrySmall moleculeTubulin Modulatorstubulin polymerizationTubulinDrug Designbiology.proteinMolecular MedicineProtein MultimerizationColchicine
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