Search results for "molecular"

showing 10 items of 32340 documents

FRI0030 Anti-TNF-α Antibody Targeted To Inflamed Synovial Tissue for The Treatment of Rheumatoid Arthritis

2016

Background TNF-α neutralizing molecules represent one of the most efficient therapeutic approaches to control inflammation in rheumatoid arthritis (RA). The widespread distribution in the body induces the inhibition of TNF-α in all the tissues, requesting the use of high dose of this expensive drug. Another problem that has not yet been solved in the management of RA patients is how to reduce and possibly avoid the side effects, particularly the increased risk of common and opportunistic infections, which may be associated with long-term administration of these therapeutic drugs. Objectives The aim of the present investigation was to show that a recombinant protein obtained by fusing a syno…

rheumatoid arthritisPathologymedicine.medical_specialtyImmunologyArthritisInflammationImmunofluorescenceGeneral Biochemistry Genetics and Molecular BiologyRheumatologyIn vivoAdalimumabmedicineImmunology and AllergyNeutralizing antibodyantigen induced arthritismedicine.diagnostic_testbiologybusiness.industrytarget therapyantigen induced arthritirheumatoid arthritimedicine.diseaseRheumatoid arthritisImmunologyrheumatoid arthritis; antigen induced arthritis; target therapy; immunotherapybiology.proteinTumor necrosis factor alphaimmunotherapymedicine.symptombusinessmedicine.drug
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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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Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O

2001

The pore-forming toxin streptolysin O (SLO) can be used to reversibly permeabilize adherent and nonadherent cells, allowing delivery of molecules with up to 100 kDa mass to the cytosol. Using FITC-labeled albumin, 10 5 –10 6 molecules were estimated to be entrapped per cell. Repair of toxin lesions depended on Ca 2+ -calmodulin and on intact microtubules, but was not sensitive to actin disruption or to inhibition of protein synthesis. Resealed cells were viable for days and retained the capacity to endocytose and to proliferate. The active domains of large clostridial toxins were introduced into three different cell lines. The domains were derived from Clostridium difficile B-toxin and Clo…

rho GTP-Binding ProteinsCell Membrane PermeabilityGlycosylationCell SurvivalBacterial ToxinsClostridium difficile toxin AClostridium difficile toxin BBiologymedicine.disease_causeCell LineBacterial ProteinsAlbuminsChlorocebus aethiopsTumor Cells CulturedmedicineAnimalsHumansSecretionParticle SizeActinMultidisciplinaryDose-Response Relationship DrugSecretory VesiclesProteinsBiological TransportDextransBiological SciencesActin cytoskeletonMolecular biologyRatsCell biologyCytosolImmunoglobulin GCOS CellsStreptolysinsras ProteinsClostridium botulinumStreptolysinProceedings of the National Academy of Sciences
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Late Activation of Stress-activated Protein Kinases/c-Jun N-terminal Kinases Triggered by Cisplatin-induced DNA Damage in Repair-defective Cells

2011

Although stress-activated protein kinases/c-Jun N-terminal kinases (SAPK/JNK) are rapidly activated by genotoxins, the role of DNA damage in this response is not well defined. Here we show that the SEK1/MKK4-mediated dual phosphorylation of SAPK/JNK (Thr-183/Tyr-185) correlates with the level of cisplatin-DNA adducts at late times (16–24 h) after drug treatment in both human and mouse cells. Transfection of platinated plasmid DNA also caused SAPK/JNK activation. A defect in transcription-coupled nucleotide excision repair resting on a mutation in Cockayne syndrome group B protein promoted the late SAPK/JNK activation following cisplatin exposure. Signaling to SAPK/JNK was accompanied by act…

rho GTP-Binding ProteinsDNA RepairMAP Kinase Kinase 4DNA repairDNA damageDNA damage response; DNA repair; cisplatin-DNA adducts; SAPK/JNKp38 mitogen-activated protein kinasesAntineoplastic AgentsCell Cycle ProteinsAtaxia Telangiectasia Mutated ProteinsProtein Serine-Threonine KinasesDNA and ChromosomesBiologyBiochemistryAtaxia Telangiectasia Mutated ProteinsDNA AdductsMiceRadiation IonizingAnimalsHumansDNA Breaks Double-StrandedMolecular BiologyReplication protein ACells CulturedMice KnockoutKinaseTumor Suppressor ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyMolecular biologyDNA-Binding ProteinsEnzyme Activationc-Jun N-terminal kinasesbiology.proteinCisplatinSignal TransductionNucleotide excision repairJournal of Biological Chemistry
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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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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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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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