Search results for "gtp-binding"

showing 10 items of 178 documents

Rho-mediated activation of PI(4)P5K and lipid second messengers is necessary for promotion of angiogenesis by Semaphorin 4D

2011

Phosphatidylinositol 4-phosphate 5-kinase (PI(4)P5K) is a type I lipid kinase that generates the lipid second messenger phospholipid phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and functions downstream of RhoA in actin organization. It is known to play an essential role in neurite remodeling, yielding a phenotype identical to that seen in cells treated with Semaphorin 4D (Sema4D), a protein that regulates proliferation, adhesion and migration in many different cell types. Plexin-B1, the receptor for Sema4D, activates RhoA in order to generate a pro-angiogenic signal in endothelial cells. Therefore, we looked in human umbilical vein endothelial cells (HUVEC) to determine if Plexin-B1 e…

Phosphatidylinositol 45-DiphosphateCancer ResearchRHOAPhysiologyAngiogenesisSemaphorin 4DClinical BiochemistrySEMA4DNeovascularization PhysiologicNerve Tissue ProteinsReceptors Cell SurfaceSemaphorinsSynaptojaninBiologySecond Messenger SystemsArticlePI(45)P2chemistry.chemical_compoundAntigens CDRhoSettore BIO/10 - BiochimicaHumansPlexin B1PhosphatidylinositolRho-associated protein kinaseCytoskeletonrho-Associated KinasesPI(4)P5KKinaseCell biologyPhosphotransferases (Alcohol Group Acceptor)AngiogenesiHEK293 CellschemistrySecond messenger systembiology.proteinCalciumrhoA GTP-Binding ProteinAngiogenesis
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Restoration of Clostridium difficile toxin-B-inhibited phospholipase D by phosphatidylinositol 4,5-bisphosphate.

1996

Receptor signalling to phospholipase D (PLD) in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor apparently involves Rho proteins. Since phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] has been recognized as an essential cofactor for PLD activity and since activated Rho proteins have been reported to stimulate the synthesis of PtdIns(4,5)P2, we studied whether in HEK cells PLD activity is regulated by PtdIns(4,5)P2 and, in particular, whether PtdIns(4,5)P2 can restore PLD activity inhibited by Clostridium difficile toxin B, which inactivates Rho proteins. Addition of MgATP to permeabilized HEK cells increased basal PLD activity and potentia…

Phosphatidylinositol 45-DiphosphateGTP'Bacterial ToxinsClostridium difficile toxin BBiologyBiochemistryCell Linechemistry.chemical_compoundBacterial ProteinsGTP-Binding ProteinsPhosphatidylcholineRhoB GTP-Binding ProteinPhospholipase DHumansPhosphatidylinositolEnzyme InhibitorsrhoB GTP-Binding ProteinPhospholipase DClostridioides difficileHEK 293 cellsCell MembraneMembrane ProteinsReceptors MuscarinicCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)chemistryPhosphatidylinositol 45-bisphosphateGuanosine 5'-O-(3-Thiotriphosphate)lipids (amino acids peptides and proteins)European journal of biochemistry
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Control of cellular phosphatidylinositol 4,5-bisphosphate levels by adhesion signals and Rho GTPases in NIH 3T3 fibroblasts

2000

The involvement of small GTPases of the Rho family in the control of phosphoinositide metabolism by adhesion signals was examined in NIH 3T3 fibroblasts. Abrogation of adhesion signals by detachment of cells from their substratum resulted in a time-dependent decrease in the cellular level of PtdIns(4,5)P2 by approximately 50%. This effect could be mimicked by treatment of adherent cells with Clostridium difficile toxin B and toxin B-1470, which inhibit specific subsets of Rho and Ras GTPases. Detachment of cells that had been pretreated with the clostridial toxins did not cause a further reduction in PtdIns(4,5)P2 levels, suggesting that the target GTPases are integrated into the control of…

Phosphatidylinositol 45-Diphosphaterac1 GTP-Binding Proteinrho GTP-Binding ProteinsBacterial ToxinsCellClostridium difficile toxin BRAC1GTPasePhospholipaseBiologyTransfectionBiochemistryMicechemistry.chemical_compoundPhosphoinositide Phospholipase CBacterial ProteinsCell AdhesionmedicineAnimalsPhosphorylationInositol phosphatechemistry.chemical_classificationPhospholipase CCytotoxinsPhosphoric Diester Hydrolases3T3 CellsMolecular biologyRecombinant ProteinsCell biologyKineticsPhosphotransferases (Alcohol Group Acceptor)medicine.anatomical_structurechemistryPhosphatidylinositol 45-bisphosphateType C PhospholipasesCalciumSignal TransductionEuropean Journal of Biochemistry
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Activation of the p75 neurotrophin receptor through conformational rearrangement of disulphide-linked receptor dimers.

2009

Ligand-mediated dimerization has emerged as a universal mechanism of growth factor receptor activation. Recent structural studies have shown that neurotrophins interact with dimers of the p75 neurotrophin receptor (p75NTR), but the actual mechanism of receptor activation has remained elusive. Here we show that p75NTR forms disulphide-linked dimers independently of neurotrophin binding through the highly conserved Cys257 in its transmembrane domain. Mutation of Cys257 abolished neurotrophin-dependent receptor activity but did not affect downstream signaling by the p75NTR/NgR/Lingo-1 complex in response to MAG, indicating the existence of distinct, ligand-specific activation mechanisms for p7…

Protein ConformationMutantNeuronesReceptor Nerve Growth FactorMiceProtein structureChlorocebus aethiopsNerve Growth FactorLow-affinity nerve growth factor receptorRNA Small InterferingReceptorskin and connective tissue diseasesReceptors neuralsCells CulturedNeuronsCell DeathGeneral NeuroscienceNF-kappa BCell biologyTransmembrane domainSIGNALINGOligopeptidesNeurotrophinProtein BindingSignal Transductionmusculoskeletal diseasesPROTEINSNeuroscience(all)Green Fluorescent ProteinsNerve Tissue ProteinsReceptors Nerve Growth FactorSuperior Cervical GanglionBiologyTransfectionMOLNEUROArticleGrowth factor receptorAnimalsHumansProtein Interaction Domains and MotifsReceptors Growth FactorCysteineBinding SitesMembrane Proteinsbiological factorsRatsnervous systemAnimals NewbornNeurotrophin bindingMutationbiology.proteinsense organsProtein MultimerizationrhoA GTP-Binding ProteinProteïnesNeuron
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Exosomes from metastatic cancer cells transfer amoeboid phenotype to non-metastatic cells and increase endothelial permeability: their emerging role …

2017

AbstractThe goal of this study was to understand if exosomes derived from high-metastatic cells may influence the behavior of less aggressive cancer cells and the properties of the endothelium. We found that metastatic colon cancer cells are able to transfer their amoeboid phenotype to isogenic primary cancer cells through exosomes, and that this morphological transition is associated with the acquisition of a more aggressive behavior. Moreover, exosomes from the metastatic line (SW620Exos) exhibited higher ability to cause endothelial hyperpermeability than exosomes from the non metastatic line (SW480Exos). SWATH-based quantitative proteomic analysis highlighted that SW620Exos are signific…

Proteomics0301 basic medicineRHOAEndotheliummetastatic cancer cellScienceCell PlasticityContext (language use)ExosomesArticlePermeability03 medical and health sciences0302 clinical medicineSettore BIO/13 - Biologia ApplicataCell Line Tumormetastatic cancer cells; Exosomes; tumor heterogeneitytumor heterogeneityHuman Umbilical Vein Endothelial CellsmedicineHumansEndotheliumrho-Associated KinasesMultidisciplinarybiologyQThrombinRPhenotypeMicrovesicles3. Good healthCell biologyEndothelial stem cellExosomePhenotype030104 developmental biologymedicine.anatomical_structureTumor progression030220 oncology & carcinogenesisColonic NeoplasmsCancer cellbiology.proteinMedicinerhoA GTP-Binding ProteinSignal Transduction
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Rho protein inactivation induced apoptosis of cultured human endothelial cells.

2002

Small GTP-binding Rho GTPases regulate important signaling pathways in endothelial cells, but little is known about their role in endothelial cell apoptosis. Clostridial cytotoxins specifically inactivate GTPases by glucosylation [ Clostridium difficile toxin B-10463 (TcdB-10463), C. difficile toxin B-1470 (TcdB-1470)] or ADP ribosylation ( C. botulinum C3 toxin). Exposure of human umbilical cord vein endothelial cells (HUVEC) to TcdB-10463, which inhibits RhoA/Rac1/Cdc42, or to C3 toxin, which inhibits RhoA, -B, -C, resulted in apoptosis, whereas inactivation of Rac1/Cdc42 with TcdB-1470 was without effect, suggesting that Rho inhibition was responsible for endothelial apoptosis. Disruptio…

Pulmonary and Respiratory Medicinerac1 GTP-Binding Proteinrho GTP-Binding ProteinsProgrammed cell deathUmbilical VeinsEndotheliumPhysiologyBacterial ToxinsCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisBcl-2-associated X proteinBacterial ProteinsPhysiology (medical)Proto-Oncogene ProteinsmedicineCyclic AMPIn Situ Nick-End LabelingHumanscdc42 GTP-Binding ProteinCells Culturedbcl-2-Associated X ProteinAdenosine Diphosphate RibosebiologyCaspase 3Intracellular Signaling Peptides and ProteinsCell BiologyCaspase 9Cell biologyNeoplasm ProteinsEndothelial stem cellmedicine.anatomical_structureCdc42 GTP-Binding ProteinProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisCaspasesbiology.proteinMyeloid Cell Leukemia Sequence 1 ProteinEndothelium VascularSignal transductionCarrier ProteinsrhoA GTP-Binding ProteinBH3 Interacting Domain Death Agonist ProteinSignal TransductionAmerican journal of physiology. Lung cellular and molecular physiology
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Amyloid-Beta Induces Different Expression Pattern of Tissue Transglutaminase and Its Isoforms on Olfactory Ensheathing Cells: Modulatory Effect of In…

2021

Abstract Alzhèimer Disease (AD) is characterized by protein aggregates in the brain, including amyloid-beta (Aβ), a substrate for tissue transglutaminase (TG2). We assessed the effect of full native peptide of Aβ (1–42), the fragments (25–35 and 35–25) on TG2 expression and its isoforms (Long and Short) on mouse Olfactory Ensheathing Cells (OECs). The levels of cytoskeletal proteins, Vimentin and Glial Fibrillary Acid Protein, were also studied. The effect of the pre-treatment with Indicaxanthin on cell viability, total Reactive Oxygen Species, superoxide anion and apoptotic pathway activation was assessed. Since Nestin is co-expressed in pluripotent stem cells with cyclin D1, their levels …

Pyridinestissue transglutaminase; olfactory ensheathing cells; amyloid-beta; oxidative stress; Indicaxanthin; self-renewalApoptosisAmyloid‐betaIndicaxanthinVimentinself-renewallcsh:ChemistryNestinMicechemistry.chemical_compoundProtein IsoformsCyclin D1lcsh:QH301-705.5SpectroscopybiologySuperoxideOpuntiaCell DifferentiationGeneral MedicineOlfactory Bulbamyloid-betaBetaxanthinsComputer Science ApplicationsCell biologyIndicaxanthinAmyloid betaTissue transglutaminase; Olfactory Ensheathing Cells; Amyloid-Beta; oxidative stress; In-dicaxanthin; self-renewalArticleGene Expression Regulation EnzymologicCatalysisInorganic ChemistryCyclin D1Alzheimer DiseaseGTP-Binding ProteinsGlial Fibrillary Acidic ProteinAnimalsHumansVimentinProtein Glutamine gamma Glutamyltransferase 2Viability assayPhysical and Theoretical ChemistryMolecular BiologyAmyloid beta-PeptidesTransglutaminasesOrganic ChemistryTissue transglutaminaseNestinSelf‐renewalNerve Regenerationlcsh:Biology (General)lcsh:QD1-999chemistryOxidative stressOlfactory ensheathing cellsbiology.proteinOlfactory ensheathing gliaReactive Oxygen SpeciesInternational Journal of Molecular Sciences
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The Enterotoxin from Clostridium difficile (ToxA) Monoglucosylates the Rho Proteins

1995

The enterotoxin from Clostridium difficile (ToxA) is one of the causative agents of the antibiotic-associated pseudomembranous colitis. In cultured monolayer cells ToxA exhibits cytotoxic activity to induce disassembly of the actin cytoskeleton, which is accompanied by morphological changes. ToxA-induced depolymerization of actin filaments is correlated with a decrease in the ADP-ribosylation of the low molecular mass GTP-binding Rho proteins (Just, I., Selzer, J., von Eichel-Streiber, C., and Aktories, K. (1995) J. Clin. Invest. 95, 1026-1031). Here we report on the identification of the ToxA-induced modification of Rho. Applying electrospray mass spectrometry, the mass of the modification…

RHOAGlycoside HydrolasesBacterial ToxinsClostridium difficile toxin ARAC1macromolecular substancesEnterotoxinBiochemistrySubstrate SpecificityEnterotoxinsGTP-Binding ProteinsTumor Cells CulturedAmino AcidsMolecular BiologyActinbiologyMolecular massClostridioides difficileCell BiologyPseudomembranous colitisActin cytoskeletonMolecular biologycarbohydrates (lipids)GlucoseBiochemistrybiology.proteinrhoA GTP-Binding ProteinJournal of Biological Chemistry
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Rho prevents apoptosis through Bcl-2 expression: Implications for interleukin-2 receptor signal transduction

1997

Here we describe a Rho-mediated apoptosis suppression pathway driven by Bcl-2 expression in the interleukin (IL)-4- or IL-2-dependent murine T cell line TS1 alpha beta. IL-2, but not IL-4, induces Bcl-2 expression through RhoA activation which is inhibited by the specific Rho family inhibitor, Clostridium difficile Toxin B, as well as by a dominant negative RhoA mutant. Using transient transfections of RhoA mutants tagged with the vesicular stomatitis virus glycoprotein, we show that a constitutively active RhoA mutant induces Bcl-2 expression and prevents apoptosis upon IL-4 withdrawal. Finally, we have identified the signaling pathway involved together with RhoA in Bcl-2 induction and sho…

RHOAImmunologyDown-RegulationClostridium difficile toxin AApoptosisClostridium difficile toxin BTransfectionCell LineMicePhosphatidylinositol 3-Kinaseschemistry.chemical_compoundGTP-Binding ProteinsAnimalsHumansImmunology and AllergyPhosphatidylinositolProtein kinase AProtein Kinase CbiologyKinaseInterleukinReceptors Interleukin-2Molecular biologyCell biologyProto-Oncogene Proteins c-bcl-2chemistrybiology.proteinInterleukin-2Signal transductionrhoA GTP-Binding ProteinSignal TransductionEuropean Journal of Immunology
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Clostridium difficile toxin A induces expression of the stress-induced early gene product RhoB.

2004

Clostridium difficile toxin A monoglucosylates the Rho family GTPases Rho, Rac, and Cdc42. Glucosylation leads to the functional inactivation of Rho GTPases and causes disruption of the actin cytoskeleton. A cDNA microarray revealed the immediate early gene rhoB as the gene that was predominantly up-regulated in colonic CaCo-2 cells after treatment with toxin A. This toxin A effect was also detectable in epithelial cells such as HT29 and Madin-Darby canine kidney cells, as well as NIH 3T3 fibroblasts. The expression of RhoB was time-dependent and correlated with the morphological changes of cells. The up-regulation of RhoB was approximately 15-fold and was based on the de novo synthesis of …

RHOAPyridinesRHOBBacterial ToxinsClostridium difficile toxin ARAC1GTPaseBiochemistryp38 Mitogen-Activated Protein KinasesGene Expression Regulation EnzymologicGene productEnterotoxinsStress PhysiologicalRhoB GTP-Binding ProteinHumansrhoB GTP-Binding ProteinMolecular BiologyOligonucleotide Array Sequence AnalysisbiologyImidazolesCell BiologyRhoBClostridium difficileActin cytoskeletonMolecular biologyUp-Regulationbiology.proteinGene expressionCaco-2 CellsThe Journal of biological chemistry
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