Search results for "Polysaccharides"

showing 10 items of 413 documents

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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Cloning and expression of a novel component of the CAP superfamily enhanced in the inflammatory response to LPS of the ascidian Ciona intestinalis.

2010

The CAP superfamily is a group of proteins that have been linked to several biological functions such as reproduction, cancer, and immune defense. A differential screening between lipopolysaccharide (LPS)-challenged and naive Ciona intestinalis has been performed to identify LPS-induced genes. This strategy has allowed the isolation of a full-length 1471-bp cDNA encoding for a 413-amino-acid protein (CiCAP). In silico analysis has shown that this polypeptide displays a modular structure with similarities to vertebrate CAP-superfamily proteins and to a collagen-binding adhesin of Streptococcus mutans. Domain organization analysis and alignment of CiCAP to other vertebrate CAP proteins have r…

LipopolysaccharidesHistologyHemocytesSequence analysisIn silicoMolecular Sequence DataSettore BIO/05 - ZoologiaSequence alignmentPolymerase Chain ReactionPathology and Forensic MedicineComplementary DNAAnimalsCiona intestinalisAmino Acid SequenceRNA MessengerCloning MolecularGenePeptide sequenceIn Situ HybridizationPhylogenyInflammationMessenger RNAbiologyBase SequenceSequence Homology Amino AcidProteinsCell BiologySequence Analysis DNAbiology.organism_classificationMolecular biologyCiona intestinalisInnate immune system differential display CAP protein molecular biology ciona intestinalis (Tunicata)Sequence AlignmentCell and tissue research
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Inducible lectins with galectin properties and human IL1alpha epitopes opsonize yeast during the inflammatory response of the ascidian Ciona intestin…

2007

Studies on inducible ascidian lectins may shed light on the evolutionary emergence of cytokine functions. Here, we show that the levels of opsonins, with IL1alpha-epitopes, increase in Ciona intestinalis hemolymph as a response to an inflammatory stimulus and, in particular, to intratunic injection of lipopolysaccharide (LPS). The inflammatory agent promptly (within 4 h) enhances Ca(2+)-independent serum hemagglutinating and opsonizing activities, which are both inhibited by D-galactose and D-galactosides (alpha-lactose, N-acetyl-D-lactosamine, thio-digalactoside), suggesting that anti-rabbit erythrocyte lectins with galectin properties are involved as opsonins. Inducible galectin molecules…

LipopolysaccharidesHistologyLipopolysaccharideGalectinsSaccharomyces cerevisiaeCross ReactionsEpitopeEvolution . Inflammatory response . Phagocytosis . Opsonins . Lectins . IL1α-like galectins . Ascidian Ciona intestinalis (Tunicata)AntibodiesPathology and Forensic Medicinelaw.inventionchemistry.chemical_compoundEpitopesWestern blotPhagocytosisOpsonin ProteinslawHemolymphInterleukin-1alphaLectinsmedicineAnimalsHumansCiona intestinalisGalectinbiologymedicine.diagnostic_testGalactoseGalactosidesCell BiologyBlood ProteinsOpsonin Proteinsbiology.organism_classificationMolecular biologyBlood proteinsRecombinant ProteinsCiona intestinalisHemagglutininsBiochemistrychemistryRecombinant DNACalciumRabbitsCell and tissue research
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Flow cytometric investigation of neutrophil oxidative burst and apoptosis in physiological and pathological situations

2009

Flow cytometric analysis provides a rapid screen for abnormalities of polymorphonuclear neutrophils (PMN) function and reflect their behavior in vivo more accurately. This review summarizes the major fluorescent probes used to study PMN oxidative burst and apoptosis using flow cytometry (FCM). We also provide examples of FCM studies in physiological and pathological situations, illustrating the advantages of FCM for assessment of PMN oxidative burst and PMN apoptosis. These data point to the role of FCM in detecting primary immunodeficiencies such as IRAK4 deficiency and support the use of the assessment of the PMN oxidative burst for routine testing in patients with bacterial infections. W…

LipopolysaccharidesHistologyNeutrophilsSimian Acquired Immunodeficiency SyndromeApoptosisBiologyPathology and Forensic MedicineFlow cytometryAdjuvants ImmunologicIn vivomedicineAnimalsHumansReceptorNeutrophil oxidative burstPathologicalRespiratory Burstmedicine.diagnostic_testToll-Like ReceptorsImidazolesNADPH OxidasesCell BiologyFlow CytometryPhenotypeRespiratory burstInterleukin-1 Receptor-Associated KinasesOligodeoxyribonucleotidesApoptosisImmunologyReactive Oxygen SpeciesCytometry Part A
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Killed Candida albicans yeasts and hyphae inhibit gamma interferon release by murine natural killer cells.

2006

ABSTRACT Killed yeasts and hyphae of Candida albicans inhibit gamma interferon secretion by highly purified murine NK cells in response to the Toll-like receptor ligands lipopolysaccharide and zymosan. This effect, which is also observed in the presence of NK-activating cytokines (interleukin-2 [IL-2], IL-12, and IL-15), may represent a novel mechanism of immune evasion that contributes to the virulence of C. albicans .

LipopolysaccharidesHyphaLipopolysaccharideImmunologyHyphaeMicrobiologyNatural killer cellMicrobiologychemistry.chemical_compoundInterferon-gammaMiceImmune systemCandida albicansmedicineAnimalsInterferon gammaCandida albicansbiologyInterleukinsZymosanZymosanbiology.organism_classificationCorpus albicansToll-Like Receptor 2Killer Cells NaturalMice Inbred C57BLToll-Like Receptor 4Infectious Diseasesmedicine.anatomical_structurechemistryParasitologyFungal and Parasitic Infectionsmedicine.drugInfection and immunity
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IL-9 and IL-13 production by activated mast cells is strongly enhanced in the presence of lipopolysaccharide: NF-kappa B is decisively involved in th…

2001

Abstract Mast cells, due to their ability to produce a large panel of mediators and cytokines, participate in a variety of processes in adaptive and innate immunity. Herein we report that in primary murine bone marrow-derived mast cells activated with ionomycin or IgE-Ag the bacterial endotoxin LPS strongly enhances the expression of IL-9 and IL-13, but not IL-4. This costimulatory effect of LPS is absent in activated mast cells derived from the LPS-hyporesponsive mouse strain BALB/c-LPSd, although in these cells the proinflammatory cytokine IL-1 can still substitute for LPS. The enhanced production of mast cell-derived IL-13 in the presence of IL-1 is a novel observation. Coactivation of m…

LipopolysaccharidesImmunologyInflammationBone Marrow CellsBiologyProinflammatory cytokinechemistry.chemical_compoundMiceMice CongenicAdjuvants ImmunologicmedicineImmunology and AllergyAnimalsMast CellsPromoter Regions GeneticCells CulturedReporter geneMice Inbred BALB CMice Inbred C3HInnate immune systemBinding SitesInterleukin-13Interleukin-9NF-kappa BNFKB1Cell biologyInterleukin 33chemistryGene Expression RegulationIonomycinInterleukin 13Immunologymedicine.symptomSignal TransductionJournal of immunology (Baltimore, Md. : 1950)
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