Search results for "inflammation"

showing 10 items of 2662 documents

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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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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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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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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Study of Potential Anti-Inflammatory Effects of Red Wine Extract and Resveratrol through a Modulation of Interleukin-1-Beta in Macrophages

2018

Inflammation has been described as an initiator event of major diseases with significant impacts in terms of public health including in cardiovascular disease, autoimmune disorders, eye diseases, age-related diseases, and the occurrence of cancers. A preventive action to reduce the key processes leading to inflammation could be an advantageous approach to reducing these associated pathologies. Many studies have reported the value of polyphenols such as resveratrol in counteracting pro-inflammatory cytokines. We have previously shown the potential of red wine extract (RWE) and the value of its qualitative and quantitative polyphenolic composition to prevent the carcinogenesis process. In thi…

LipopolysaccharidesInflammasomesred wine extractInterleukin-1betainflammation;interleukins;polyphenols;red wine extract;resveratrolAnti-Inflammatory AgentsWinelcsh:TX341-641resveratrolArticleCell LineMiceNLR Family Pyrin Domain-Containing 3 ProteinAnimalspolyphenolsPlant ExtractsMacrophagesfood and beveragesCARD Signaling Adaptor Proteins[SDV.AEN] Life Sciences [q-bio]/Food and NutritionRAW 264.7 Cellsinterleukinsinflammation[SDV.AEN]Life Sciences [q-bio]/Food and Nutritionlcsh:Nutrition. Foods and food supplyPhytotherapyNutrients
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Mitophagy in myeloid cells : role in infection with gram-negative bacteria

2017

Sepsis and related organ dysfunctions remain a leading cause of mortality in intensive care units. Increasing evidences have shed light on an unexpected link between mitochondria and immune cell functions. Alterations in mitochondrial functions have been reported in peripheral blood cells in sepsis. We hypothesize here that mitophagy might impact on phagocyte functions in the context of bacterial infection. Mitophagy is a mitochondria-dedicated autophagy that governs the elimination of dysfunctional mitochondria. We demonstrated here in vivo and in vitro that macrophages exposed to Gram-negative bacteria or their cell wall component LPS display a marked inhibition of mitophagy that constitu…

LipopolysaccharidesInflammation[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologyMacrophagesSepsisMyeloid cellsMitophagyCellules myeloidesMitophagie[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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Transcriptomic Analyses Reveal 2 and 4 Family Members of Cytochromes P450 (CYP) Involved in LPS Inflammatory Response in Pharynx of Ciona robusta

2021

Cytochromes P450 (CYP) are enzymes responsible for the biotransformation of most endogenous and exogenous agents. The expression of each CYP is influenced by a unique combination of mechanisms and factors including genetic polymorphisms, induction by xenobiotics, and regulation by cytokines and hormones. In recent years, Ciona robusta, one of the closest living relatives of vertebrates, has become a model in various fields of biology, in particular for studying inflammatory response. Using an in vivo LPS exposure strategy, next-generation sequencing (NGS) and qRT-PCR combined with bioinformatics and in silico analyses, compared whole pharynx transcripts from naïve and LPS-exposed C. robusta…

LipopolysaccharidesLPSCytochromeQH301-705.5cytochrome P450In silicoInflammationArticleGene Expression Regulation EnzymologicCatalysisInorganic ChemistryTranscriptomeCytochrome P-450 Enzyme SystemmicroRNAmedicineAnimalsBiology (General)Physical and Theoretical ChemistryQD1-999Ciona robusta<i>Ciona robusta</i>Molecular BiologyGenePhylogenySpectroscopymiRNAInflammationGeneticschemistry.chemical_classificationbiologyGene Expression ProfilingOrganic ChemistryHigh-Throughput Nucleotide SequencingCytochrome P450General MedicineCiona intestinalisComputer Science ApplicationsChemistryEnzymechemistryMultigene FamilyNGSbiology.proteinPharynxmedicine.symptomTranscriptomeInternational Journal of Molecular Sciences
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Pro-oxidant activity of indicaxanthin from Opuntia ficus indica modulates arachidonate metabolism and prostaglandin synthesis through lipid peroxide …

2014

Macrophages come across active prostaglandin (PG) metabolism during inflammation, shunting early production of pro-inflammatory towards anti-inflammatory mediators terminating the process. This work for the first time provides evidence that a phytochemical may modulate the arachidonate (AA) metabolism in lipopolysaccharide (LPS)-stimulated RAW 264.7 macrophages, promoting the ultimate formation of anti-inflammatory cyclopentenone 15deoxy-PGJ2. Added 1 h before LPS, indicaxanthin from Opuntia Ficus Indica prevented activation of nuclear factor-κB (NF-κB) and over-expression of PGE2 synthase-1 (mPGES-1), but up-regulated cyclo-oxygenase-2 (COX-2) and PGD2 synthase (H-PGDS), with final product…

LipopolysaccharidesLipid PeroxidesLipopolysaccharidePyridinesPhytochemicalsClinical BiochemistryProstaglandinIndicaxanthinmedicine.disease_causeBiochemistryCell LineMiceStructure-Activity Relationshipchemistry.chemical_compoundmedicineAnimalslcsh:QH301-705.5Inflammationlcsh:R5-920Arachidonic AcidNADPH oxidaseDose-Response Relationship DrugLipid peroxidebiologyMacrophagesOrganic ChemistryOpuntiaMetabolismOxidantsPro-oxidantBetaxanthinslcsh:Biology (General)chemistryBiochemistryOxidative stressFruitIndicaxanthin Phytochemicals Eicosanoids Inflammation Oxidative stress.Prostaglandinsbiology.proteinEicosanoidslipids (amino acids peptides and proteins)lcsh:Medicine (General)IndicaxanthinOxidative stressResearch PaperRedox Biology
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Interaction of TLR2 and TLR4 ligands with the N-terminal domain of Gp96 amplifies innate and adaptive immune responses.

2006

Activation of dendritic cells by ligands for Toll-like receptors (TLR) is a crucial event in the initiation of innate and adaptive immune responses. Several classes of TLR ligands have been identified that interact with distinct members of the TLR-family. TLR4 ligands include lipopolysaccharide derived from different Gram-negative bacteria and viral proteins. Recent reports have demonstrated the TLR-mediated activation of dendritic cells by heat shock proteins (HSPs). However, doubts were raised as to what extent this effect was due to lipopolysaccharide contaminations of the HSP preparations. We re-examined this phenomenon using Gp96 or its N-terminal domain, nominally endotoxin-free (0.5 …

LipopolysaccharidesLipopolysaccharideBiologyCD8-Positive T-LymphocytesBiochemistrychemistry.chemical_compoundMiceImmune systemDogsHeat shock proteinAnimalsHumansReceptorMolecular BiologyInflammationMice Inbred BALB CInnate immune systemMembrane GlycoproteinsCCL18Cell BiologyToll-Like Receptor 2Cell biologyEndotoxinsMice Inbred C57BLToll-Like Receptor 4TLR2BiochemistrychemistryTLR4The Journal of biological chemistry
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