Search results for "Arid"

showing 10 items of 1382 documents

Ciona intestinalis peroxinectin is a novel component of the peroxidase–cyclooxygenase gene superfamily upregulated by LPS

2013

Peroxinectins function as hemoperoxidase and cell adhesion factor involved in invertebrate immune reaction. In this study, the ascidian (Ciona intestinalis) peroxinectin gene (CiPxt) and its expression during the inflammatory response have been examined. CiPxt is a new member of the peroxidase-cyclooxygenase gene superfamily that contains both the peroxidase domain and the integrin KGD (Lys-Gly-Asp) binding motif. A phylogenetic tree showed that CiPxt is very close to the chordate group and appears to be the outgroup of mammalian MPO, EPO and TPO clades. The CiPxt molecular structure model resulted superimposable to the human myeloperoxidase. The CiPxt mRNA expression is upregulated by LPS …

LipopolysaccharidesModels MolecularHemocytesLPSAmino Acid MotifsMolecular Sequence DataPeroxinectinImmunologyIntegrinSettore BIO/05 - ZoologiaChordatePeroxinectin;Peroxidase;Inflammation;LPS;Ciona intestinalisAnimalsCiona intestinalisAmino Acid SequenceRNA MessengerCell adhesionPhylogenyPeroxidaseInflammationRegulation of gene expressionSequence Homology Amino AcidbiologyCell adhesion moleculeAnimal Structuresbiology.organism_classificationMolecular biologyImmunity InnateProtein Structure TertiaryCiona intestinalisGene Expression RegulationPeroxidasesOrgan SpecificityMyeloperoxidaseembryonic structuresImmunologybiology.proteinCell Adhesion MoleculesDevelopmental BiologyEndostyleDevelopmental & Comparative Immunology
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Inducible galectins are expressed in the inflamed pharynx of the ascidian Ciona intestinalis

2011

Although ascidians belong to a key group in chordate phylogenesis, amino acid sequences of Ciona intestinalis galectin-CRDs (CiLgals-a and -b) have been retained too divergent from vertebrate galectins. In the present paper, to contribute in disclosing Bi-CRD galectin evolution a novel attempt was carried out on CiLgals-a and -b CRDs phylogenetic analysis, and their involvement in ascidian inflammatory responses was shown. CiLgals resulted aligned with Bi-CRD galectins from vertebrates (Xenopus tropicalis, Gallus gallus, Mus musculus, Homo sapiens), cephalochordates (Branchiostoma floridae), echinoderms (Strongylocentrotus purpuratus) and a mono-CRD galectin from the ascidian Clavelina pict…

LipopolysaccharidesModels Molecularanimal structuresHemocytesTime FactorsGalectinsBlotting WesternMolecular Sequence DataCiona intestinalis galectinsSettore BIO/05 - ZoologiaSequence alignmentChordateAquatic ScienceAdjuvants ImmunologicPhylogeneticsBranchiostoma floridaeEnvironmental ChemistryAnimalsCiona intestinalisAmino Acid SequencePeptide sequencePhylogenyGalectinbiologyGeneral MedicineAnatomybiology.organism_classificationMolecular biologyStrongylocentrotus purpuratuseye diseasesCiona intestinalisProtein Structure TertiaryUp-Regulationembryonic structuresPharynxSequence Alignment
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Potential biological role of laccase from the sponge Suberites domuncula as an antibacterial defense component

2014

Abstract Background Laccases are copper-containing enzymes that catalyze the oxidation of a wide variety of phenolic substrates. Methods We describe the first poriferan laccase from the marine demosponge Suberites domuncula. Results This enzyme comprises three characteristic multicopper oxidase homologous domains. Immunohistological studies revealed that the highest expression of the laccase is in the surface zone of the animals. The expression level of the laccase gene is strongly upregulated after exposure of the animals to the bacterial endotoxin lipopolysaccharide. To allow the binding of the recombinant enzyme to ferromagnetic nanoparticles, a recombinant laccase was prepared which con…

LipopolysaccharidesMolecular Sequence DataBiophysicsMulticopper oxidaseFerric CompoundsLigninBiochemistryMichaelis–Menten kineticsGene Expression Regulation EnzymologicSubstrate Specificitychemistry.chemical_compoundEscherichia coliAnimalsLigninAmino Acid SequenceMolecular BiologyPhylogenyLaccasechemistry.chemical_classificationDose-Response Relationship DrugSequence Homology Amino AcidbiologyReverse Transcriptase Polymerase Chain ReactionChemistryLaccaseHydrazonesSubstrate (chemistry)biology.organism_classificationRecombinant ProteinsAnti-Bacterial AgentsUp-RegulationSuberites domunculaKineticsEnzymeBiochemistryBiocatalysisNanoparticlesSuberitesOxidation-ReductionIron oxide nanoparticlesBiochimica et Biophysica Acta (BBA) - General Subjects
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A Lipopolysaccharide Antigen of the Treponema

1958

IMMUNOCHEMICAL studies carried out by D'Alessandro et al. 1 on a non-pathogenic, culturable treponeme, the so-called Reiter treponeme, revealed the presence of four antigenic components: (1) a thermolabile protein; (2) a specific, thermostable antigen with polysaccharide characteristics; (3) a lipoid, corresponding to the ubiquitous lipidic antigen cardiolipin; (4) another lipoid similar to the organ-specific cerebral antigen of Witebsky2. These studies led to the conclusion that the treponemes, like other organisms, are mosaics of antigens, and a safe basis was established for a better understanding of the complex serological response of the infected host.

LipopolysaccharidesMultidisciplinaryTreponemaLipopolysaccharidebiologybiology.organism_classificationMicrobiologySerologychemistry.chemical_compoundBlood serumchemistryAntigenPolysaccharidesCardiolipinsCardiolipinTreponemaAntigensThermolabileNature
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New insight into the inhibition of the inflammatory response to experimental delayed-type hypersensitivity reactions in mice by scropolioside A.

2006

Scropolioside A, an iridoid isolated from Scrophularia auriculata ssp. pseudoauriculata, showed anti-inflammatory properties against different experimental models of delayed-type hypersensitivity. This iridoid reduced the oedema induced by oxazolone by 79% (72 h) at 0.5 mg/ear while reducing that induced by sheep red blood cells by 47% (18 h), 45% (24 h) and 36% (48 h) at 10 mg/kg. In vivo it reduced both oedema formation and cell infiltration whereas in vitro it reduced the proliferation of activated T-lymphocytes (IC50 of 67.74 microM). Treatment with scropolioside A (100 microM) 18 and 24 h after phytohemagglutinin stimulation increased the number of cells arrested in the subG(0) phase w…

LipopolysaccharidesNecrosisErythrocytesLeukotriene B4NeutrophilsT-LymphocytesAnti-Inflammatory AgentsStimulationInflammationApoptosisLymphocyte proliferationPharmacologyBiologyLeukotriene B4DinoprostoneNitric oxideCell LineOxazolonechemistry.chemical_compoundMiceGlucosidesmedicineAnimalsEdemaHumansHypersensitivity DelayedPyransPharmacologySheepPancreatic ElastaseCaspase 3MacrophagesOxazoloneEarAllergenschemistryDelayed hypersensitivityImmunologyCytokinesFemalemedicine.symptomEuropean journal of pharmacology
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Oxidative stress and innate immunity responses in cigarette smoke stimulated nasal epithelial cells

2013

Cigarette smoke extracts (CSE) may play a significant role in diseases of the upper airway including chronic rhinosinusitis. Even short term exposure of cigarette smoke has adverse effects on mitochondrial functions and redox homeostasis in tissues which may progress to further complications associated with chronic smoking. Cigarette smoke alters toll-like receptor 4 (TLR4) expression and activation in bronchial epithelial cells. Carbocysteine is an anti-oxidant and mucolytic agent. The effects of carbocysteine on CSE induced oxidative stress and on associated innate immune and inflammatory responses in nasal epithelial cells are largely unknown. The present study was aimed to assess in CSE…

LipopolysaccharidesNecrosisNeutrophilsPhalloidineCARB CSE Cigarette smoke LPS Nasal epithelial cells ROS Reactive oxygen species TLR4 carbocysteine cigarette smoke extracts lipolysaccharide reactive oxygen species toll like receptor 4Fluorescent Antibody TechniqueApoptosisMucous membrane of noseCell SeparationBiologyToxicologymedicine.disease_causeCell LineNecrosisSmokeTobaccomedicineHumansExpectorantschemistry.chemical_classificationReactive oxygen speciesInnate immune systemCarbocysteineEpithelial CellsCarbocysteineTobacco ProductsGeneral MedicineActinsImmunity InnateToll-Like Receptor 4Nasal MucosaOxidative StresschemistryApoptosisImmunologyTLR4medicine.symptomReactive Oxygen SpeciesOxidative stressToxicology in Vitro
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Interaction of dicaffeoylquinic derivatives with peroxynitrite and other reactive nitrogen species.

2008

Plant phenolic antioxidants, among them catechins and hydroxycinnamoyl conjugates, constitute a well defined class of inhibitors of reactive nitrogen species (RNS). To gain deeper insight in this field, we examined the effects of 3,5-di-O-caffeoylquinic acid (DCA), its methyl ester (DCE) and epigallocatechin gallate (EGCG) in nitrative and oxidative processes. These compounds were found to be strong inhibitors of the nitration of tyrosine residues induced by ONOO- in bovine seroalbumin, with their IC50 values (10-40 microM) notably decreasing in the presence of bicarbonate. When studied on the intracellular protein tyrosine nitration induced by ONOO- in cultured murine fibroblasts as well a…

LipopolysaccharidesNeutrophilsBicarbonateBiophysicsQuinic AcidNitric Oxide Synthase Type IIEpigallocatechin gallateBiochemistryCatechinNitric oxidechemistry.chemical_compoundInhibitory Concentration 50MiceNitrationPeroxynitrous AcidAnimalsHumansTyrosineMolecular BiologyReactive nitrogen speciesNitritesNitratesNitrotyrosineMacrophagesSerum Albumin BovineFibroblastsReactive Nitrogen SpeciesStimulation ChemicalBicarbonateschemistryBiochemistryTetradecanoylphorbol AcetateTyrosineCattleOxidation-ReductionPeroxynitriteArchives of biochemistry and biophysics
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A role for Toll-like receptor mediated signals in neutrophils in the pathogenesis of the anti-phospholipid syndrome.

2012

The anti-phospholipid syndrome (APS) is characterized by recurrent thrombosis and occurrence of anti-phospholipid antibodies (aPL). aPL are necessary, but not sufficient for the clinical manifestations of APS. Growing evidence suggests a role of innate immune cells, in particular polymorphonuclear neutrophils (PMN) and Toll-like receptors (TLR) to be additionally involved. aPL activate endothelial cells and monocytes through a TLR4-dependent signalling pathway. Whether this is also relevant for PMN in a similar way is currently not known. To address this issue, we used purified PMN from healthy donors and stimulated them in the presence or absence of human monoclonal aPL and the TLR4 agonis…

LipopolysaccharidesNeutrophilsImmunology610 MedizinImmunoglobulinslcsh:MedicineInflammationApoptosisImmunopathologyBiologyNeutrophil ActivationAutoimmune DiseasesPhagocytosisimmune system diseases610 Medical sciencesmedicineHumansInterleukin 8L-SelectinReceptorlcsh:ScienceBiologyImmune ResponseneoplasmsRespiratory BurstInflammationToll-like receptorMultidisciplinaryInnate immune systemCD11b AntigenCoagulation DisordersEffectorInterleukin-8lcsh:RImmunityHematologyAntiphospholipid SyndromeFlow CytometryInnate ImmunityRespiratory burstToll-Like Receptor 4ImmunologyTLR4MedicineClinical Immunologylcsh:Qmedicine.symptomResearch ArticleSignal TransductionPLoS ONE
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Expression and function of the non-neuronal cholinergic system in endothelial cells

2003

Increasing evidence has shown the expression of the non-neuronal cholinergic system in endothelial cells. In the present experiments the expression of choline acetyltransferase (ChAT) was investigated in human endothelial cells by anti-ChAT immunohistochemistry and anti-ChAT immunofluorescence. Positive ChAT immunoreactivity was found in cultures of human umbilical endothelial cells (HUVEC) and a human angiosarcoma cell line (HAEND). In HUVEC and HAEND choline acetyltransferase activity and small amounts of acetylcholine were also detected. Positive ChAT-immunoreactivity was demonstrated in situ in endothelial cells of the human umbilical cord. In addition, in experiments with confocal lase…

LipopolysaccharidesNicotinePathologymedicine.medical_specialtyEndotheliumPhysostigmineeducationHuman skinBiologyImmunofluorescenceGeneral Biochemistry Genetics and Molecular BiologyCell LineCholine O-Acetyltransferasemental disordersTumor Cells CulturedmedicineHumansNicotinic AgonistsGeneral Pharmacology Toxicology and PharmaceuticsChromatography High Pressure LiquidMicroscopy Confocalmedicine.diagnostic_testCell adhesion moleculeAntibodies MonoclonalGeneral MedicineImmunohistochemistryCholine acetyltransferaseAcetylcholinehumanitiesCell biologymedicine.anatomical_structureNicotinic agonistnervous systemCell cultureCholinesterase InhibitorsEndothelium VascularCell Adhesion MoleculesAcetylcholineSignal Transductionmedicine.drugLife Sciences
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Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1—evidence for direct and …

2009

Heme oxygenase-1 (HO-1) is highly protective in various pathophysiological states such as cardiovascular and neurodegenerative diseases. HO-1-derived bilirubin is an efficient scavenger of reactive oxygen and nitrogen species (RONS). It remains to determine whether conversion of biliverdin to bilirubin is an essential step for HO-1-conferred protection of endothelial cells. RONS scavenging activities of biliverdin versus bilirubin were assessed by different RONS generating systems and detection techniques. We also silenced the biliverdin reductase (BVR) or HO-1 gene in cultured primary human endothelial cells (HUVECs) and measured the effect on RONS formation upon stimulation with lipopolys…

LipopolysaccharidesOxidoreductases Acting on CH-CH Group DonorsUmbilical VeinsXanthine OxidaseNeutrophilsBilirubinNitrosationModels BiologicalAntioxidantschemistry.chemical_compoundPeroxynitrous AcidLeukocytespolycyclic compoundsHumansGene SilencingMolecular BiologyHemeReactive nitrogen speciesRespiratory BurstBiliverdinAngiotensin IIBiliverdineBiliverdin reductaseEndothelial CellsBilirubinFree Radical ScavengersAngiotensin IIMitochondriaEndothelial stem cellHeme oxygenasechemistryBiochemistryCytoprotectionGene Knockdown TechniquesTyrosineReactive Oxygen SpeciesCardiology and Cardiovascular MedicineHeme Oxygenase-1Journal of Molecular and Cellular Cardiology
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