Search results for "binding proteins"

showing 10 items of 911 documents

Function of odorant-binding proteins in the Drosophila melanogaster chemoreception

2017

National audience; Function of odorant-binding proteins in the Drosophila [i]melanogaster[/i] chemoreception. 18. rencontre du Club de neurobiologie des invertébrés

pichia pastorisanimal structures[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritioneducationodorant-binding proteinsdrosophila melanogasterhumanitiestestingCAFÉ assay[SDV.AEN] Life Sciences [q-bio]/Food and Nutritionprotéineessaiprotein[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionhuman activitiespsychological phenomena and processeshealth care economics and organizationsfluorescent binding assays
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RAB18 Loss Interferes With Lipid Droplet Catabolism and Provokes Autophagy Network Adaptations

2020

Autophagy is dependent on appropriate lipid supply for autophagosome formation. The regulation of lipid acquisition and the autophagy network response to lipid-limiting conditions are mostly elusive. Here, we show that the knockout of the RAB GTPase RAB18 interferes with lipid droplet catabolism, causing an impaired fatty acid release. The resulting reduced lipid-droplet-derived lipid availability influences autophagy and provokes adaptive modifications of the autophagy network. These adjustments include increased expression and phosphorylation of ATG2B as well as augmented formation of the ATG12-ATG5 conjugate. Moreover, ATG9A shows an enhanced phosphorylation at amino acid residues tyrosi…

rab3 GTP-Binding ProteinsImmunoblottingGTPaseReal-Time Polymerase Chain Reaction03 medical and health sciences0302 clinical medicineMicroscopy Electron TransmissionStructural BiologyLipid dropletAutophagyHumansPhosphorylationTyrosineMolecular Biology030304 developmental biology0303 health sciencesMicroscopy ConfocalChemistryCatabolismAutophagyAutophagosomesLipid DropletsImmunohistochemistryCell biologyrab GTP-Binding ProteinsPhosphorylationlipids (amino acids peptides and proteins)RabCRISPR-Cas Systems030217 neurology & neurosurgeryRAB18HeLa CellsJournal of Molecular Biology
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Rac1 and PAK1 are upstream of IKK-ε and TBK-1 in the viral activation of interferon regulatory factor-3

2004

The anti-viral type I interferon (IFN) response is initiated by the immediate induction of IFN beta, which is mainly controlled by the IFN-regulatory factor-3 (IRF-3). The signaling pathways mediating viral IRF-3 activation are only poorly defined. We show that the Rho GTPase Rac1 is activated upon virus infection and controls IRF-3 phosphorylation and activity. Inhibition of Rac1 leads to reduced IFN beta promoter activity and to enhanced virus production. As a downstream mediator of Rac signaling towards IRF-3, we have identified the kinase p21-activated kinase (PAK1). Furthermore, both Rac1 and PAK1 regulate the recently described IRF-3 activators, I kappa B kinase- and TANK-binding kina…

rac1 GTP-Binding ProteinTranscription GeneticBiophysicsIκB kinaseProtein Serine-Threonine KinasesSignal transductionBiologyVirus ReplicationBiochemistryCell LineDogsPAK1Structural BiologyInterferonGeneticsmedicineAnimalsHumansPhosphorylationPromoter Regions Geneticp21-activated kinasesMolecular BiologyRNA Double-StrandedKinaseRho GTPaseI-Kappa-B KinaseNuclear ProteinsInterferon-betaCell BiologyCREB-Binding ProteinI-kappa B KinaseDNA-Binding ProteinsEnzyme Activationp21-Activated KinasesInfluenza A virusViral infectionAnti-viral responseTrans-ActivatorsCancer researchInterferon Regulatory Factor-3Transcription factorSignal transductionDimerizationTranscription FactorsInterferon regulatory factorsmedicine.drugFEBS Letters
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Physical inactivity increases oxidative stress, endothelial dysfunction, and atherosclerosis.

2005

Objective— Sedentary lifestyle is associated with increased cardiovascular events. The underlying molecular mechanisms are incompletely understood. Reactive oxygen species (ROS) contribute to endothelial dysfunction and atherosclerosis. An important source of vascular ROS is the NADPH oxidase. Methods and Results— C57BL6 mice were subjected to regular housing (physical inactivity) or voluntary training on running wheels (6 weeks). Inactivity increased vascular lipid peroxidation to 148±9% and upregulated superoxide release to 176±17% (L-012 chemiluminescence) and 188±29% (cytochrome C reduction assay), respectively. ROS production was predominantly increased in the endothelium and the medi…

rac1 GTP-Binding Proteinmedicine.medical_specialtyEndotheliumNitric Oxide Synthase Type IIIArteriosclerosisNitric Oxide Synthase Type IIBiologymedicine.disease_causechemistry.chemical_compoundMiceApolipoproteins EInternal medicinePhysical Conditioning AnimalmedicineAnimalsNADH NADPH OxidoreductasesRNA MessengerEndothelial dysfunctionLife Stylechemistry.chemical_classificationReactive oxygen speciesNADPH oxidaseSuperoxideNeuropeptidesNADPH Oxidase 1NADPH Oxidasesmedicine.diseasePhosphoproteinsMice Mutant Strainsrac GTP-Binding ProteinsMice Inbred C57BLVasodilationOxidative Stressmedicine.anatomical_structureEndocrinologychemistryNOX1biology.proteinNADPH Oxidase 1Endothelium VascularNitric Oxide SynthaseCardiology and Cardiovascular MedicineReactive Oxygen SpeciesOxidative stressArteriosclerosis, thrombosis, and vascular biology
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Rho GTPases in human breast tumours: expression and mutation analyses and correlation with clinical parameters

2002

In the present study, we addressed the question of a putative relevance of Rho proteins in tumour progression by analysing their expression on protein and mRNA level in breast tumours. We show that the level of RhoA, RhoB, Rac1 and Cdc42 protein is largely enhanced in all tumour samples analysed (n=15) as compared to normal tissues originating from the same individual. The same is true for 32P-ADP-ribosylation of Rho proteins which is catalysed by Clostridium botulinum exoenzyme C3. Also the amount of Rho-GDI and ERK2 as well as the level of overall 32P-GTP binding acvitity was tumour-specific elevated, yet to a lower extent than Rho proteins. Although the amount of Rho proteins was enhance…

rac1 GTP-Binding Proteinrho GTP-Binding ProteinsCancer ResearchRHOAProliferation indexRHOBBlotting WesternDNA Mutational AnalysisRhoCGene ExpressionBreast NeoplasmsRAC1breast tumoursCDC42Polymerase Chain ReactionRho GTPasesRhoB GTP-Binding ProteinHumansBreastRNA Messengercdc42 GTP-Binding ProteinrhoB GTP-Binding Proteinmutation analysisADP Ribose TransferasesMitogen-Activated Protein Kinase 1biologyGenetics and GenomicsMolecular biologyOncologyCdc42 GTP-Binding ProteinMutationtumour progressionDisease Progressionbiology.proteinFemaleGuanosine TriphosphaterhoA GTP-Binding ProteinBritish Journal of Cancer
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Rac1 protein signaling is required for DNA damage response stimulated by topoisomerase II poisons.

2012

To investigate the potency of the topoisomerase II (topo II) poisons doxorubicin and etoposide to stimulate the DNA damage response (DDR), S139 phosphorylation of histone H2AX (γH2AX) was analyzed using rat cardiomyoblast cells (H9c2). Etoposide caused a dose-dependent increase in the γH2AX level as shown by Western blotting. By contrast, the doxorubicin response was bell-shaped with high doses failing to increase H2AX phosphorylation. Identical results were obtained by immunohistochemical analysis of γH2AX focus formation, comet assay-based DNA strand break analysis, and measuring the formation of the topo II-DNA cleavable complex. At low dose, doxorubicin activated ataxia telangiectasia m…

rac1 GTP-Binding Proteinrho GTP-Binding ProteinsDNA damageAntineoplastic AgentsBiochemistryPoisonsCell LineHistonesNeoplasmsmedicineAnimalsTopoisomerase II InhibitorsDoxorubicinMolecular BiologyEtoposidebiologyCell DeathTopoisomeraseCell BiologyMolecular biologyImmunohistochemistryRatsComet assayHistoneDNA Topoisomerases Type IIDNA Topoisomerases Type Ibiology.proteinPhosphorylationTopoisomerase-II InhibitorHydroxymethylglutaryl-CoA Reductase Inhibitorsmedicine.drugDNA DamageSignal TransductionThe Journal of biological chemistry
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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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Low levels of both xanthine dehydrogenase and of cellular retinol binding protein are responsible for retinoic acid deficiency in malignant human mam…

2009

The seeming impairment of retinoid metabolism in human breast tumor cells has been attributed to the lower expression of cellular retinol binding proteins (CRBPs), of alcohol/retinol dehydrogenases, or aldehyde/retinaldehyde dehydrogenases. In a previous study we indicated that xanthine dehydrogenase (XDH) is able to oxidize actively both all-trans-retinol (t-ROL) bound to the CRBP (holo-CRBP) and all-trans-retinaldehyde (t-RAL) to all-trans-retinoic acid (t-RA) in human mammary epithelial cells (HMEC). Since both XDH and CRBP are required for the biosynthesis of t-RA, we have inspected their bioavailability in both estrogen-responsive and nonresponsive human mammary epithelial cancer cells…

retinoic acid biosynthesis tumor mammary cellsXanthine DehydrogenaseCellular differentiationRetinoic acidBreast NeoplasmsTretinoinBiologyGeneral Biochemistry Genetics and Molecular BiologyCell Linechemistry.chemical_compoundHistory and Philosophy of ScienceBiosynthesisCell Line TumorSettore BIO/10 - BiochimicaHumansMammary Glands HumanRadiometryChromatography High Pressure LiquidGeneral NeuroscienceRetinolRetinol-Binding Proteins CellularMolecular biologyRetinol binding proteinBiochemistrychemistryXanthine dehydrogenaseCell cultureCancer cell
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Rho GTPases Are Involved in the Regulation of NF-κB by Genotoxic Stress

2001

A common cellular response to genotoxic agents and inflammatory cytokines is the activation of NF-kappaB. Here, we addressed the question of whether small GTPases of the Rho family are involved in the stimulation of NF-kappaB signaling by genotoxic agents or TNFalpha in HeLa cells. Inhibition of isoprenylation of Rho proteins by use of the HMG-CoA reductase inhibitor lovastatin attenuated UV-, doxorubicin-, and TNFalpha-induced degradation of IkappaBalpha as well as drug-stimulated DNA binding activity of NF-kappaB. Furthermore, NF-kappaB-regulated gene expression stimulated by either UV irradiation or treatment with TNFalpha was abrogated by lovastatin pretreatment. This indicates that iso…

rho GTP-Binding ProteinsBacterial ToxinsClostridium difficile toxin BGenotoxic StressGTPaseBiologyProinflammatory cytokinechemistry.chemical_compoundBacterial ProteinsNF-KappaB Inhibitor alphamedicineHumansLovastatinTumor Necrosis Factor-alphaNF-kappa BNF-kappa B p50 SubunitNF-κBCell BiologyCell biologyDNA-Binding ProteinsIκBαchemistryDoxorubicinI-kappa B ProteinsTumor necrosis factor alphaLovastatinHeLa CellsSignal Transductionmedicine.drugExperimental Cell Research
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Cytotoxic necrotizing factor type 2 produced by virulent Escherichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin s…

1994

Cytotoxic necrotizing factor type 2 (CNF2) produced by Escherichia coli strains isolated from intestinal and extraintestinal infections is a dermonecrotic toxin of 110 kDa. We cloned the CNF2 gene from a large plasmid carried by an Escherichia coli strain isolated from a lamb with septicemia. Hydropathy analysis of the deduced amino acid sequence revealed a largely hydrophilic protein with two potential hydrophobic transmembrane domains. The N-terminal half of CNF2 showed striking homology (27% identity and 80% conserved residues) to the N-terminal portion of Pasteurella multocida toxin. Methylamine protection experiments and immunofluorescence studies suggested that CNF2 enters the cytosol…

rho GTP-Binding ProteinsBacterial ToxinsMolecular Sequence DataRestriction Mapping[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyIn Vitro TechniquesSEQUENCE GENIQUEmedicine.disease_causeCell LineGTP-binding protein regulatorsGTP-Binding ProteinsmedicineEscherichia coliHumansCloning MolecularCytoskeletonEscherichia coliPeptide sequence[SDV.BC] Life Sciences [q-bio]/Cellular BiologyActinAdenosine Diphosphate RiboseMultidisciplinaryBase SequenceSequence Homology Amino AcidCytotoxinsBinding proteinEscherichia coli ProteinsMolecular biologyActinsCytosolTransmembrane domainActin CytoskeletonBiochemistryGenes BacterialFACTEUR CYTOTOXIQUE NECROSANTSequence AlignmentResearch Article
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