Search results for "ciona intestinali"

showing 10 items of 113 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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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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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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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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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 &amp; 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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