Search results for "Rho"

showing 10 items of 2586 documents

Inhibition of small G proteins of the Rho family by statins orClostridium difficiletoxin B enhances cytokine-mediated induction of NO synthase II

2000

In order to investigate the involvement of Ras and/or Rho proteins in the induction of the inducible isoform of nitric oxide synthase (NOS II) we used HMG-CoA reductase inhibitors (statins) and Clostridium difficile toxin B (TcdB) as pharmacological tools. Statins indirectly inhibit small G proteins by preventing their essential farnesylation (Ras) and/or geranylgeranylation (Rho). In contrast, TcdB is a glucosyltransferase and inactivates Rho-proteins directly. Human A549/8- and DLD-1 cells as well as murine 3T3 fibroblasts were preincubated for 18 h with statins (1–100 μM) or TcdB (0.01–10 ng ml−1). Then NOS II expression was induced by cytokines. NOS II mRNA was measured after 4–8 h by R…

rho GTP-Binding ProteinsG proteinBacterial ToxinsMevalonic AcidNitric Oxide Synthase Type IISmall G ProteinClostridium difficile toxin BBiologyGene Expression Regulation EnzymologicMiceGeranylgeranylationBacterial ProteinsPolyisoprenyl PhosphatesPrenylationGTP-Binding ProteinsGene expressionAtorvastatinTumor Cells CulturedAnimalsHumansDrug InteractionsPyrrolesLovastatinPromoter Regions GeneticPharmacology3T3 CellsTransfectionMolecular biologyHeptanoic AcidsEnzyme InductionPapersCytokinesHydroxymethylglutaryl-CoA Reductase InhibitorsNitric Oxide SynthaseSignal transductionBritish Journal of Pharmacology
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Mtlinteracts with members of Egfr signaling and cell adhesion genes in the Drosophila eye

2011

Mtl is a member of the Rho family of small GTPases in Drosophila. It was shown that Mtl is involved in planar cell polarity (PCP) establishment, together with other members of the same family like Cdc42, Rac1, Rac2 and RhoA. However, while Rac1, Rac2 and RhoA function downstream of Dsh in Fz/PCP signaling and upstream of a JNK cassette, Mtl and Cdc42 do not. To determine the functional context of Mtl during PCP establishment in the Drosophila eye, we performed a loss-of-function screen to search for dominant modifiers of a sev>Mtl rough eye phenotype. In addition, genetic interaction assays with candidate genes were also carried out. Our results show that Mtl interacts genetically with memb…

rho GTP-Binding ProteinsGeneticsOmmatidial rotationRHOAbiologyCytoskeleton organizationCell PolarityCDC42Cell biologyErbB ReceptorsPhenotypeInsect ScienceCell polarityCell Adhesionbiology.proteinAnimalsDrosophila ProteinsImmunoglobulin superfamilyDrosophilaCompound Eye ArthropodReceptors Invertebrate PeptideCell adhesionpsychological phenomena and processesDrosophila ProteinSignal TransductionFly
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Activation of astroglial phospholipase D activity by phorbol ester involves ARF and Rho proteins.

2000

Primary cultures of rat cortical astrocytes express phospholipase D (PLD) isoforms 1 and 2 as determined by RT-PCR and Western blot. Basal PLD activity was strongly (10-fold) increased by 4beta-phorbol-12beta,13alpha-dibutyrate (PDB) (EC(50): 56 nM), an effect which was inhibited by Ro 31-8220 (0.1-1 microM), an inhibitor of protein kinase C (PKC), and by brefeldin A (10-100 microg/ml), an inhibitor of ADP-ribosylating factor (ARF) activation. Pretreatment of the cultures with Clostridium difficile toxin B-10463 (0.1-1 ng/ml), which inactivates small G proteins of the Rho family, led to a breakdown of the astroglial cytoskeleton; concomitantly, PLD activation by PDB was reduced by up to 50%…

rho GTP-Binding ProteinsIndolesADP ribosylation factorBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BBiologyRats Sprague-Dawleychemistry.chemical_compoundWestern blotBacterial ProteinsPhorbol EstersmedicinePhospholipase DPhospholipase D activityAnimalsEnzyme InhibitorsMolecular BiologyProtein kinase CCells CulturedProtein Kinase CProtein Synthesis InhibitorsBrefeldin Amedicine.diagnostic_testPhospholipase DADP-Ribosylation FactorsSerum Albumin BovineCell BiologyBrefeldin AMolecular biologyRatsEnzyme ActivationchemistryAstrocyteslipids (amino acids peptides and proteins)Biochimica et biophysica acta
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Metabotropic glutamate receptors activate phospholipase D in astrocytes through a protein kinase C-dependent and Rho-independent pathway.

2003

Metabotropic glutamate receptors (mGluRs) are G protein-coupled receptors that mediate phospholipase D (PLD) activation in brain, but the mechanism underlying this response remains unclear. Here we used primary cultures of astrocytes as a cell model to explore the mechanism that links mGluRs to PLD. Glutamate activated both phospholipase C (PLC) and PLD with equal potency and this effect was mimicked by L-cysteinesulfinic acid, a putative neurotransmitter previously shown to activate mGluRs coupled to PLD, but not PLC, in adult brain. PLD activation by glutamate was dependent on Ca(2+) mobilization and fully blocked by both protein kinase C (PKC) inhibitors and PKC down-regulation, suggesti…

rho GTP-Binding ProteinsIndolesBacterial ToxinsGlutamic AcidBiologyReceptors Metabotropic GlutamateSulfenic AcidsMaleimidesRats Sprague-DawleyCellular and Molecular NeuroscienceBacterial ProteinsStress FibersmedicinePhospholipase DAnimalsCysteineEgtazic AcidProtein kinase CCells CulturedProtein Kinase CChelating AgentsPharmacologyProtein Synthesis InhibitorsBrefeldin APhospholipase CDose-Response Relationship DrugEndothelin-1Phospholipase DADP-Ribosylation FactorsMetabotropic glutamate receptor 6Glutamate receptorDNAMolecular biologyRatsenzymes and coenzymes (carbohydrates)medicine.anatomical_structureMetabotropic receptorMetabotropic glutamate receptorAstrocytesType C PhospholipasesTetradecanoylphorbol Acetatelipids (amino acids peptides and proteins)AstrocyteNeuropharmacology
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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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Rho GTPases: Promising Cellular Targets for Novel Anticancer Drugs

2006

Ras-homologous (Rho) GTPases play a pivotal role in the regulation of numerous cellular functions associated with malignant transformation and metastasis. Rho GTPases are localized at membranes and become activated upon stimulation of cell surface receptors. In their GTP-bound (=active) state, Rho proteins bind to effector proteins, thereby triggering specific cellular responses. Members of the Rho family of small GTPases are key regulators of actin reorganization, cell motility, cell-cell and cell-extracellular matrix (ECM) adhesion as well as of cell cycle progression, gene expression and apoptosis. Each of these functions is of importance for the development and progression of cancer. Fu…

rho GTP-Binding ProteinsPharmacologyCancer ResearchRHOAbiologyChemistryRHOBFarnesyltransferaseAntineoplastic AgentsRAC1GTPaseCell biologyCell Transformation NeoplasticOncologyPrenylationDrug Resistance NeoplasmTumor progressionDrug Discoverybiology.proteinAnimalsHumansEnzyme InhibitorsLipid modificationMutagensCurrent Cancer Drug Targets
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Inhibition of Protein Isoprenylation Impairs Rho-Regulated Early Cellular Response to Genotoxic Stress

2000

Activation of c-Jun N-terminal kinases (JNKs) and nuclear factor-kappaB (NF-kappaB) are early cellular responses to genotoxic stress involved in the regulation of gene expression. Pretreatment of cells with the hydroxymethyl glutaryl-CoA reductase inhibitor lovastatin blocked stimulation of JNK1 activity by UV irradiation and by treatment with the alkylating compound methyl methanesulfonate but did not affect activation of extracellular signal-regulated kinase 2 by UV light. Lovastatin also attenuated UV-induced degradation of the NF-kappaB inhibitor IkappaBalpha. The effects of lovastatin on UV-triggered stimulation of JNK1 as well as on IkappaBalpha degradation were reverted by cotreatmen…

rho GTP-Binding ProteinsProtein PrenylationStimulationClostridium difficile toxin BCHO CellsGenotoxic StressBiologychemistry.chemical_compoundCricetinaemedicineAnimalsHumansMitogen-Activated Protein Kinase 8LovastatinPharmacologyMutagenicity TestsKinaseFarnesyltransferase inhibitorNF-kappa BMethyl methanesulfonateCell biologyIκBαchemistryMolecular MedicineLovastatinHydroxymethylglutaryl-CoA Reductase InhibitorsMitogen-Activated Protein KinasesHeLa CellsSignal Transductionmedicine.drugMolecular Pharmacology
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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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Lovastatin inhibits Rho-regulated expression of E-selectin by TNFalpha and attenuates tumor cell adhesion.

2003

E-selectin mediated cell-cell adhesion plays an important role in inflammatory processes and extravasation of tumor cells. Tumor necrosis factor-alpha (TNF-alpha) induces E-selectin gene and protein expression in primary human endothelial cells (HUVEC) and in an endothelial cell line (EA.hy-926). As shown by ELISA and FACS analyses, HMG-CoA reductase inhibitors (e.g., lovastatin) impair the TNF-alpha stimulated increase in E-selectin protein expression. Similar results were obtained for E-selectin mRNA expression and promoter activity, indicating that the effect of lovastatin is based on inhibition of gene expression. The effective inhibitory concentration of lovastatin was in a physiologic…

rho GTP-Binding ProteinsRHOATranscription GeneticRHOBAntineoplastic AgentsBiochemistryCell MovementCell Line TumorNeoplasmsGene expressionE-selectinGeneticsmedicineCell AdhesionHumansLovastatinCell adhesionMolecular BiologyCells CulturedbiologyTumor Necrosis Factor-alphaCell biologybiology.proteinCancer researchTumor necrosis factor alphaLovastatinEndothelium VascularSignal transductionE-SelectinBiotechnologymedicine.drugSignal TransductionFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Inhibition of Rho modulates cytokine-induced prostaglandin E2 formation in renal mesangial cells.

2003

Stimulation of rat mesangial cells for 24 h with interleukin-1β(IL-1β) plus forskolin (Fk) leads to a marked increase in prostaglandin E 2 (PGE 2 ) synthesis. This effect is further enhanced by the small G-protein Rho inhibitor toxin A. A similar increase in PGE 2 formation is obtained with Y27632, a Rho-dependent kinase inhibitor, and with lovastatin, a hydroxymethylglutaryl-coenzyme A inhibitor which depletes cells from geranylgeranyl moieties and thus blocks Rho activation. In parallel to the increased PGE 2 synthesis, a potentiation of IL-1β-induced secretory group IIA phospholipases A 2 (sPLA 2 -IIA) protein expression also occurs by Rho inhibition. However, only toxin A triggers an in…

rho GTP-Binding Proteinsmedicine.medical_treatmentBlotting WesternProstaglandinBiologyDinoprostonePhospholipases Achemistry.chemical_compoundmedicineAnimalsProstaglandin E2Molecular BiologyCells CulturedForskolinMesangial cellKinaseColforsinCell BiologyMolecular biologyGlomerular MesangiumRatsPhospholipases A2Cytokinechemistrylipids (amino acids peptides and proteins)Lovastatinmedicine.drugProstaglandin EInterleukin-1Biochimica et biophysica acta
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