Search results for "LIPOPOLYSACCHARIDE"

showing 10 items of 382 documents

COMPLEMENT-DEPENDENT B-CELL ACTIVATION BY COBRA VENOM FACTOR AND OTHER MITOGENS?

1974

It has been proposed that two distinct signals are required for the triggering of the precursors of antibody-forming bone marrow-derived cells (B cells): (a) the binding of antigen or of a mitogen to the corresponding receptor sites on B-cell membranes and (b) the interaction of activated C3 with the C3 receptor of B lymphocytes. There is growing evidence that B-cell mitogens and T (thymus-derived cell)-independent antigens are capable of activating the alternate pathway of the complement system (bypass). Therefore, the effect of another potent bypass inducer was investigated with regard to B-cell activation and the role of C3. Purified, pyrogen-free cobra venom factor was mitogenic for bot…

LipopolysaccharidesErythrocytesT-LymphocytesImmunologyHemolytic Plaque TechniqueMice Inbred StrainsLymphocyte ActivationTritiumArticleMiceAntigenPolysaccharidesLectinsConcanavalin AEscherichia coliAnimalsImmunology and AllergyCells CulturedImmune adherence reactionAntigens BacterialB-LymphocytesSheepbiologyVenomsPokeweed mitogenSnakesComplement System ProteinsMolecular biologyImmune Adherence ReactionComplement systemKineticsCell cultureConcanavalin AAntibody Formationbiology.proteinMitogensAntibodyFetal bovine serumThymidineJournal of Experimental Medicine
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A member of the Tlr family is involved in dsRNA innate immune response in Paracentrotus lividus sea urchin

2015

Abstract The innate immune response involves proteins such as the membrane receptors of the Toll-like family (TLRs), which trigger different intracellular signalling pathways that are dependent on specific stimulating molecules. In sea urchins, TLR proteins are encoded by members of a large multigenic family composed of 60–250 genes in different species. Here, we report a newly identified mRNA sequence encoding a TLR protein (referred to as Pl-Tlr) isolated from Paracentrotus lividus immune cells. The partial protein sequence contained the conserved Toll/IL-1 receptor (TIR) domain, the transmembrane domain and part of the leucine repeats. Phylogenetic analysis of the Pl-Tlr protein was acco…

LipopolysaccharidesEvolutionImmunologySettore BIO/05 - ZoologiaMediterranean sea urchinParacentrotus lividusImmune systemToll-like receptorPhylogeneticsbiology.animalAnimalsRNA MessengerGeneSea urchinPhylogenyRNA Double-StrandedImmune cellToll-like receptorInnate immune systembiologyEcologyToll-Like ReceptorsReceptors Interleukin-1biology.organism_classificationBiological EvolutionImmunity InnateProtein Structure TertiaryUp-RegulationCell biologyTransmembrane domainPoly I-CSea UrchinsGene expressionDevelopmental BiologyDevelopmental & Comparative Immunology
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Mitochondrial G protein coupled receptor kinase 2 regulates proinflammatory responses in macrophages.

2013

G-protein-coupled receptor kinase 2 (GRK2) levels are elevated in inflammation but its role is not clear yet. Here we show that GRK2 expression is dependent on NFκB transcriptional activity. In macrophages, LPS induces GRK2 accumulation in mitochondria increasing biogenesis. The overexpression of the carboxy-terminal domain of GRK2 (βARK-ct), known to displace GRK2 from plasma membranes, in macrophages induces earlier localization of GRK2 in mitochondria in response to LPS leading to increased mt-DNA transcription, reduced ROS production and cytokines expression. Our study shows the relevance of GRK2 subcellular localization in macrophage’s biology and its potential therapeutic properties i…

LipopolysaccharidesG-Protein-Coupled Receptor Kinase 2BiophysicsβARK-ctGRK2InflammationMitochondrionBiochemistryArticleProinflammatory cytokineMiceStructural BiologyGeneticsmedicineAnimalsHumansReceptorMolecular BiologyInflammationG protein-coupled receptor kinasebiologyKinaseSubcellular localizationBeta adrenergic receptor kinaseMacrophagesCell BiologySubcellular localizationCell biologyMitochondriabiology.proteinmedicine.symptomReactive Oxygen SpeciesSignal Transduction
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NFATc1 Induction in Peripheral T and B Lymphocytes

2013

Abstract NFAT transcription factors control the proliferation and survival of peripheral lymphocytes. We have reported previously that the short isoform NFATc1/αA whose generation is induced by immune receptor stimulation supports the proliferation and inhibits the activation-induced cell death of peripheral T and B cells. We will show in this study that in novel bacterial artificial chromosome transgenic mice that express EGFP under the control of entire Nfatc1 locus the Nfatc1/Egfp transgene is expressed as early as in double-negative thymocytes and in nonstimulated peripheral T and B cells. Upon immune receptor stimulation, Nfatc1/Egfp expression is elevated in B, Th1, and Th2 cells, but…

LipopolysaccharidesGene isoformChromosomes Artificial BacterialProgrammed cell deathTransgeneGreen Fluorescent ProteinsImmunologyGene ExpressionMice TransgenicStimulationImmune receptorBiologyLymphocyte ActivationT-Lymphocytes RegulatoryAntibodiesMiceTh2 CellsGenes ReporterTransforming Growth Factor betaAnimalsProtein IsoformsImmunology and AllergyPromoter Regions GeneticTranscription factorCell ProliferationB-LymphocytesNFATC Transcription Factorsintegumentary systemNF-kappa BCD28NFATTh1 CellsMolecular biologyMice Inbred C57BLTh17 CellsThe Journal of Immunology
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Expressional control of the ‘constitutive’ isoforms of nitric oxide synthase (NOS I and NOS III)

1998

Nitric oxide synthase (NOS) exists in three established isoforms. NOS I (NOS1, ncNOS) was originally discovered in neurons. This enzyme and splice variants thereof have since been found in many other cells and tissues. NOS II (NOS2, iNOS) was first identified in murine macrophages, but can also be induced in many other cell types. NOS III (NOS3, ecNOS) is expressed mainly in endothelial cells. Whereas NOS II is a transcriptionally regulated enzyme, NOS I and NOS III are considered constitutively expressed proteins. However, evidence generated in recent years indicates that these two isoforms are also subject to expressional regulation. In view of the important biological functions of these …

LipopolysaccharidesGene isoformNitric Oxide Synthase Type IIITranscription GeneticNOS1Nitric Oxide Synthase Type IBiochemistryTranscription (biology)GeneticsTranscriptional regulationAnimalsHumansRNA MessengerGrowth SubstancesMolecular BiologyTranscription factorRegulation of gene expressionPolymorphism GeneticbiologyChemistryChromosome MappingLysophosphatidylcholinesNitric Oxide Synthase Type IIIEstrogensExonsCell biologyIsoenzymesLipoproteins LDLOxygenNitric oxide synthaseGene Expression Regulationbiology.proteinCytokinesNitric Oxide SynthaseGene DeletionBiotechnologyThe FASEB Journal
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The major allergen of the Parietaria pollen contains an LPS-binding region with immuno-modulatory activity

2013

Background The major allergens in Parietaria pollen, Par j 1 and Par j 2, have been identified as lipid transfer proteins. The family of the Par j 1 allergens is composed of two isoforms, which differ by the presence of a 37 amino acid peptide (Par37) exclusive to the Par j 1.0101 isoform. The goal of this study was to elucidate the biological properties of the Par37 peptide. Methods In silico analysis, spectrofluorimetric experiments and in vitro cell culture assays were used to identify the biological properties of Par37. In addition, a mouse model of sensitization was used to study the influence of Par37 in the murine immune response. Results In silico analysis predicted that Par37 displ…

LipopolysaccharidesGene isoformParietariaIn silicoMolecular Sequence DataImmunologySettore BIO/11 - Biologia MolecolarePeptideBiologyAntibodiesInterferon-gammaMiceIn vivoAnimalsHumansImmunologic FactorsImmunology and AllergyAmino Acid SequencePlant ProteinsPolymyxin Bchemistry.chemical_classificationanimal modelallergens; animal models; environment; pollens.Allergensbiology.organism_classificationIn vitroAmino acidParietariachemistryBiochemistryLeukocytes MononuclearCytokinesPollenpollens.FemalePeptidesenvironmentSequence AlignmentPlant lipid transfer proteinsSpleenallergenProtein Binding
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Identification from a Positional Scanning Peptoid Library of in Vivo Active Compounds That Neutralize Bacterial Endotoxins

2005

4 pages, 3 figures, 1 table.-- PMID: 15715495 [PubMed].-- Printed version published Feb 24, 2005.-- Supporting information available at: http://pubs.acs.org/doi/suppl/10.1021/jm040834i

LipopolysaccharidesGram-negative bacteriaDatabases FactualLipopolysaccharideStereochemistryLipopolysaccharide (LPS)Peptidemedicine.disease_causeLipid AMiceVivo active compoundsPeptoidschemistry.chemical_compoundIn vivoGram-Negative BacteriaDrug DiscoverymedicineAnimalsPositional scanning peptoid libraryPeptide librarychemistry.chemical_classificationbiologyTumor Necrosis Factor-alphaToxinPeptoidbiology.organism_classificationLipid ABiochemistrychemistryMolecular Medicinelipids (amino acids peptides and proteins)Journal of Medicinal Chemistry
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Enhanced expression of a cloned and sequenced Ciona intestinalis TNFa-like (CiTNFa) gene during the LPS-induced inflammatory response.

2008

A tumor necrosis factor-alpha (TNFalpha)-like gene from Ciona intestinalis (CiTNF alpha-like) body wall challenged with bacterial lipopolysaccharide (LPS) was cloned and sequenced 4 h after LPS inoculation. An open reading frame of 936 bp encoding a propeptide of 312 amino acids (35.4 kDa) displaying a transmembrane domain from positions 7 to 29, a TACE cleavage site, and a mature peptide domain of 185 amino acids (20.9 kDa), was determined with a predicted isoelectric point of 9.4. The phylogenetic tree based on deduced amino acid sequences of invertebrate TNF-like protein and vertebrate TNFs supported the divergence between the ascidian and vertebrate TNF families, whereas D. melanogaster…

LipopolysaccharidesHemocytesHistologyMolecular Sequence DataSettore BIO/05 - ZoologiaGene ExpressionPathology and Forensic MedicineWestern blotGene expressionHemolymphmedicineTNFα . CiTNFα-like . CiTNFα-like expression . Inflammatory response . Pharynx . Hemocytes . Ciona intestinalis (Tunicata)AnimalsCiona intestinalisAmino Acid SequenceCloning MolecularPeptide sequencePhylogenyInflammationchemistry.chemical_classificationBase Sequencebiologymedicine.diagnostic_testTumor Necrosis Factor-alphaCell Biologybiology.organism_classificationMolecular biologyCiona intestinalisAmino acidTransmembrane domainOpen reading framechemistrySequence Alignment
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FACIT collagen (1α-chain) is expressed by hemocytes and epidermis during the inflammatory response of the ascidian Ciona intestinalis

2007

Based on previous cloning and sequencing study, real-time PCR and in situ hybridization assays of the inflamed body wall of LPS-injected Ciona intestinalis showed the enhanced gene expression of a collagen with FACIT structural features (Ci-type IX-Col 1alpha-chain). By using specific antibodies raised against an opportunely chosen Ci-type IX-Col synthetic peptide, the fibroblast property of hemocytes challenged in vitro with LPS (at 4h) was displayed by flow cytometry, while immunocytochemistry identified hemocytes with large granules (morula cells) as collagen-producing cells. Hemocyte lysate supernatant analyzed in immunoblotting contained a 60 kDa band identifiable as 1alpha-chain-Ci-ty…

LipopolysaccharidesHemocytesImmunologyImmunocytochemistryIn situ hybridizationCollagen Type IXFACIT collagenExtracellular matrixParacrine CommunicationEscherichia colimedicineAnimalsCiona intestinalisFibroblastIn Situ HybridizationInflammationbiologyEpidermis (botany)Gene Expression Profilingbiology.organism_classificationImmunohistochemistryMolecular biologyCiona intestinalisExtracellular Matrixmedicine.anatomical_structureEpidermal CellsImmunologyEpidermisWound healingProtein Processing Post-TranslationalProcollagenDevelopmental BiologyDevelopmental & Comparative Immunology
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In vitro induction of cecropin genes — an immune response in a Drosophila blood cell line

1992

The Drosophila melanogaster cell line mbn-2 was explored as a model system to study insect immune responses in vitro. This cell line is of blood cell origin, derived from larval hemocytes of the mutant lethal (2) malignant blood neoplasm (1(2)mbn). The mbn-2 cells respond to microbial substances by the activation of cecropin genes, coding for bactericidal peptides. The response is stronger than that previously described for SL2 cells, and four other tested Drosophila cell lines were totally unresponsive. Bacterial lipopolysaccharide, algal laminarin (a beta-1,3-glucan), and bacterial flagellin were strong inducers, bacterial peptidoglycan fragments gave a weaker response, whereas a formyl-m…

LipopolysaccharidesHemocytesTranscription GeneticLipopolysaccharideBiophysicsGenes InsectBiochemistryCell LineBlood cellchemistry.chemical_compoundImmune systemPolysaccharidesGene expressionmedicineAnimalsCycloheximideGlucansMolecular BiologybiologyfungiCell Biologybiology.organism_classificationCell biologyDrosophila melanogasterCecropinmedicine.anatomical_structurechemistryCell cultureInsect HormonesLarvaImmunologyPeptidoglycanDrosophila melanogasterAntimicrobial Cationic PeptidesFlagellinSignal TransductionBiochemical and Biophysical Research Communications
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