Search results for " CIO"

showing 10 items of 50 documents

Upregulated transcription of phenoloxidase genes in the pharynx and endostyle of Ciona intestinalis in response to LPS

2015

We investigated the role of phenoloxidases (POs) in ascidians inflammatory reaction, a components of a copper-containing protein family involved in invertebrate immune system. In Ciona intestinalis two phenoloxidases (CinPO-1, CinPO-2) have been sequenced. In the present study, real time PCR analysis showed that both CinPO-1 and CinPO-2 genes were modulated by LPS inoculation suggesting that they are inducible and highly expressed in the inflamed pharynx. In situ hybridization disclosed CinPO-1 and CinPO-2 transcripts in pharynx hemocytes (granulocytes) and, mainly, in unilocular refractile granulocytes (URG) which mainly populated the inflamed tunic matrix. Interestingly, the genes are als…

LipopolysaccharidesAscidian Phenoloxidase Hemocyte Inflammation LPS Ciona intestinalisAscidian Phenoloxidase Hemocyte Inflammation LPS Ciona intestinalisHemocytesbiologyProtein familyMonophenol MonooxygenaseSettore BIO/05 - ZoologiaIn situ hybridizationReal-Time Polymerase Chain Reactionbiology.organism_classificationMolecular biologyCiona intestinalisUp-RegulationReal-time polymerase chain reactionImmune systemTranscription (biology)ImmunologyAnimalsCiona intestinalisGeneIn Situ HybridizationEcology Evolution Behavior and SystematicsEndostyle
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Ciona intestinalis interleukin 17-like genes expression is upregulated by LPS challenge

2015

In humans, IL-17 is a proinflammatory cytokine that plays a key role in the clearance of extracellular bacteria promoting cell infiltration and production of several cytokines and chemokines. Here, we report on three Ciona intestinalis IL-17 homologues (CiIL17-1, CiIL17-2, CiIL17-3). The gene organisation, phylogenetic tree and modelling supported the close relationship with the mammalian IL-17A and IL-17F suggesting that the C. intestinalis IL-17 genes share a common ancestor in the chordate lineages. Real time PCR analysis showed a prompt expression induced by LPS inoculation suggesting that they are involved in the first phase of inflammatory response. In situ hybridization assays disclo…

LipopolysaccharidesChemokineLPSHemocytesAscidianMolecular Sequence DataImmunologySettore BIO/05 - ZoologiaIn situ hybridizationBiologyGranulocyteProinflammatory cytokineExtracellularmedicineAnimalsHumansProtein IsoformsCiona intestinalisAmino Acid SequenceGenePhylogenyInflammationBase SequenceInterleukin-17InterleukinSequence Analysis DNAbiology.organism_classificationCiona intestinalisCell biologyinterleukin IL17 hemocytemedicine.anatomical_structureImmunologybiology.proteinAscidian; interleukin IL17 hemocyte; inflammation; LPS; Ciona intestinalisSequence AlignmentDevelopmental Biology
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Isolation and expression of a novel MBL-like collectin cDNA enhanced by LPS injection in the body wall of the ascidian Ciona intestinalis

2009

Collectins are a family of calcium-dependent lectins that are characterized by their collagen-like domains. Considerable interest has been focused on this class of proteins because of their ability to interact with components of the complement system activating a cascade of events responsible for the activation of the innate immune system. A differential screening between LPS-challenged and naïve Ciona intestinalis has been performed allowing the isolation of a full length cDNA encoding for a 221 AA protein. In silico analysis has shown that this polypeptide displays protein domains with similarities to mannose-binding lectins. A phylogenetic analysis suggested that C. intestinalis MBL has …

LipopolysaccharidesDNA ComplementaryIn silicoMolecular Sequence DataImmunologyProtein domainCollectinIn situ hybridizationBiologyCytoplasmic GranulesComplementary DNAAnimalsCiona intestinalisAmino Acid SequenceMolecular BiologyPhylogenyMannose-binding lectin innate immune system LPS Ciona intestinalisInnate immune systemBase Sequencebiology.organism_classificationMolecular biologyCollectinsCiona intestinalisProtein Structure TertiaryComplement systemMolecular Immunology
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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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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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Inflamed adult pharynx tissues and swimming larva of Ciona intestinalis share CiTNFalpha-producing cells.

2010

In situ hybridisation and immunohistochemistry analyses have shown that the Ciona intestinalis tumour necrosis factor alpha gene (CiTNFalpha), which has been previously cloned and sequenced, is expressed either during the inflammatory pharynx response to lipopolysaccharide (LPS) or during the swimming larval phase of development. Granulocytes with large granules and compartment/morula cells are CiTNFalpha-producing cells in both inflamed pharynx and larvae. Pharynx vessel endothelium also takes part in the inflammatory response. Haemocyte nodules in the vessel lumen or associated with the endothelium suggest the involvement of CiTNFalpha in recruiting lymphocyte-like cells and promoting the…

LipopolysaccharidesPathologymedicine.medical_specialtyHistologyHemocytesEndotheliumEvolutionMesenchymeSettore BIO/05 - ZoologiaInflammationIn situ hybridizationBiologyAscidia Ciona intestinalisPathology and Forensic MedicinemedicineAnimalsCiona intestinalisTumour necrosis factor; Pharynx; Inflammation; Haemocytes; Larval development; Innate immunity; Evolution; Ascidia Ciona intestinalisIn Situ Hybridization FluorescencePhylogenyInflammationInnate immunityInnate immune systemTumor Necrosis Factor-alphaPharynxMetamorphosis BiologicalHaemocytePharyngitisCell Biologybiology.organism_classificationImmunohistochemistryCiona intestinalismedicine.anatomical_structureLarval developmentLarvaImmunohistochemistryPharynxmedicine.symptomTumour necrosis factorGranulocytesCell and tissue research
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The prophenoloxidase system is activated during the tunic inflammatory reaction of Ciona intestinalis

2008

Phenoloxidase (PO) activity was examined in the tunic tissue of Ciona intestinalis following lipopolysaccharide (LPS) intratunic injection. Tunic homogenate supernatant (THS), assayed with the Dopa-MBTH reaction, displayed Ca(2+)-independent PO activity that was raised by LPS and further enhanced by proteases. Specific inhibitors (tropolone, phenylthiourea, diethylthiocarbamate) supported the specificity of the reaction. Assay with soybean trypsin inhibitor showed that, in the tunic, PO activation with trypsin was not significantly inhibited suggesting that proteases diverse from serine proteases were involved. In vivo experiments were carried out by injecting isosmotic medium or LPS, and T…

LipopolysaccharidesProteasesHistologyBlotting WesternSettore BIO/05 - ZoologiaEnzyme-Linked Immunosorbent AssayPathology and Forensic MedicinemedicineAnimalsCiona intestinalisInflammationchemistry.chemical_classificationEnzyme PrecursorsbiologyKunitz STI protease inhibitorprophenoloxidase Ciona intestinalisCell BiologyProphenoloxidasebiology.organism_classificationTrypsinImmunohistochemistryMolecular biologyIn vitroCiona intestinalisUp-RegulationCionaEnzymechemistryPhenoloxidase . Hemocyte . Tunic . Inflammation . Lipopolysaccharide . SDS-polyacrylamide gel electrophoresis . Ciona intestinalisElectrophoresis Polyacrylamide GelCatechol Oxidasemedicine.drugCell and Tissue Research
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Ciona intestinalis galectin (CiLgals-a and CiLgals-b) genes are differentially expressed in endostyle zones and challenged by LPS

2015

Abstract Immunohistochemical and in situ hybridization assays were performed to answer the question whether the endostyle, that is the initial gastro-intestinal trait of Ciona intestinalis pharynx, is involved in galectin (CiLgals-a and CiLgals-b) production during the pharynx inflammatory response to LPS inoculation. Specific anti-CiLgal-a and anti-CiLgals-b antibodies, and oligonucleotide probes, that mark inflammatory hemocytes inside the pharynx vessels and vessel epithelium as shown by a previous paper, were assayed on endostyle histological sections. For the first time, we show that galectins are produced by endostyle zones, and both CiLgals-a and –b genes are upregulated by LPS. CiLg…

LipopolysaccharidesSignal peptideLPSAscidianGalectinsOligonucleotidesSettore BIO/05 - ZoologiaIn situ hybridizationAquatic ScienceBiologyendostyleDownregulation and upregulationotorhinolaryngologic diseasesmedicineExtracellularAnimalsEnvironmental ChemistryCiona intestinalisIn Situ HybridizationGalectinAscidian Galectin Endostyle Inflammation Ciona intestinalisgalectinGeneral Medicinebiology.organism_classificationImmunohistochemistryMolecular biologyEpitheliumCiona intestinalismedicine.anatomical_structureItalyinflammationImmunologyPharynxEndostyle
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Isolation and characterization of a LPS induced MD2-like protein in Ciona intestinalis

2015

The MD2 (Myeloid Differentiation factor-2) protein belongs to the ML superfamily. This group of proteins contain a specific lipid binding domain (ML domain) that plays an important role in lipid recognition and metabolism. In vertebrates, MD-2 is involved in innate immune response as co-receptor in the LPS/TLR4 signaling pathway; MD2 recognizes and binds the bacterial lipid A and drives the TLR4 activation. Two TLR isoforms, CiTLR-1 and CiTLR-2, were identified in Ciona intestinalis with a TIR domain most similar to human TLR4 and TLR 6 respectively. Using a PCR-based subtractive hybridization strategy for isolation of differentially expressed genes between LPS-challenged and naïve C. intes…

MD2 LPS Ciona intestinalisSettore BIO/05 - Zoologia
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