Search results for "ciona intestinali"

showing 10 items of 113 documents

The expression of an immune-related phenoloxidase gene is modulated inCiona intestinalisovary, test cells, embryos and larva

2015

Two distinct Ciona intestinalis phenoloxidases (CinPO1, 2) had previously been cloned and sequenced. The CinPO2 is involved in innate immunity and is expressed by inflammatory hemocytes that populate the tunic and pharynx vessels as a response to LPS inoculation. In situ hybridization and immunohistochemistry assays on histological section, showed that the expression of this gene and the produced protein are shared with oogenesis, embryogenesis and larval morphogenesis. Intriguingly, upregulation of gene transcription was found in the test cell layer that envelopes the ovary follicle, ovulated egg, and gastrula, as well as it was modulated in the zygotic nucleus of outer balstomers of 32-ce…

Innate immune systembiologyMesenchymeEmbryogenesisEmbryoIn situ hybridizationbiology.organism_classificationOogenesisCell biologymedicine.anatomical_structureNeurulaembryonic structuresImmunologyGeneticsmedicineMolecular MedicineAnimal Science and ZoologyCiona intestinalisEcology Evolution Behavior and SystematicsDevelopmental BiologyJournal of Experimental Zoology Part B: Molecular and Developmental Evolution
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Localization of antimicrobial peptides in the tunic of Ciona intestinalis (Ascidiacea, Tunicata) and their involvement in local inflammatory-like rea…

2011

AbstractTunicates comprising a wide variety of different species synthesize antimicrobial peptides as important effector molecules of the innate immune system. Recently, two putative gene families coding for antimicrobial peptides were identified in the expressed sequence tag database of the tunicate Ciona intestinalis. Two synthetic peptides representing the cationic core region of one member of each of the families displayed potent antibacterial and antifungal activities. Moreover, the natural peptides were demonstrated to be synthesized and stored in distinct hemocyte types. Here, we investigated the presence of these natural peptides, namely Ci-MAM-A and Ci-PAP-A, in the tunic of C. int…

Innate immunityInnate immune systembiologyCiona intestinaliEffectorShort CommunicationImmunologyAntimicrobial peptidesTunicatebiology.organism_classificationCiona intestinalisTunicateTunicatesBiochemistryPutative geneImmunologyAntimicrobial peptidesCiona intestinalisTunicAntimicrobial peptideInnate immunity; Antimicrobial peptides; Tunic; Ciona intestinalis; Tunicates;PathogenAscidiaceaResults in Immunology
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A preliminary study on antimicrobial peptides in the naturally damaged tunic of Ciona intestinalis (Tunicata)

2011

Innate immunitySettore MED/07 - Microbiologia E Microbiologia ClinicaCiona intestinaliSettore BIO/13 - Biologia ApplicataascidianAMPs
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LPS challenge regulates gene expression and tissue localization of a Ciona intestinalis gene through an alternative polyadenylation mechanism

2013

LPS Ciona intestinalis alternative polyadenylation mechanism
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Phenoloxidases of different sizes are modulated by LPS inoculation into ciona intestinalis tunic and pharynx

2015

In the present study, to further characterize the pro-phenoloxidase (proPO) and active phenoloxidase (PO) involved in the Ciona intestinalis inflammatory response, tunic and pharynx homogenate supernatants were separated on high pressure liquid chromatography and fractions were assayed for the PO activity before and after LPS inoculation, as well as before and after trypsin treatment which activates proPO. The LPS inoculation per se did not significantly change the basal PO activity of the tunic homogenate supernatant (THS) and pharynx homogenate supernatant (PHS) restricted in two confluent peaks, whereas a significant enhancement was observable after the trypsin treatment. This trypsin ef…

LPSlcsh:Biology (General)inflammationascidianphenoloxidaseHPLClcsh:QH301-705.5pro-phenoloxidaseascidian; phenoloxidase; pro-phenoloxidase; HPLC; inflammation; LPS; Ciona intestinalisCiona intestinalis
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Effects of Tributyltin(IV) Chloride Exposure on Larvae ofCiona intestinalis (Urochordata): An Ultrastructural Study

1996

The effects of tributyltin(IV) chloride (TBT chloride) have been tested on embryos of the ascidian Ciona intestinalis, at two different stages of development: (1) before hatching (coiled larval stage) and (2) 2 h after hatching (swimming larval stage). In vivo observations carried out with a light microscope showed that embryos at the coiled larval stage did not hatch following exposure to TBT chloride. Severe anomalies in the swimming larva, mainly concerning the morphology of the tail, which appeared twisted and squatter than in the controls, were observed. Such anomalies were also found at a functional level, i.e. contractile movements were poor so that the larvae appeared motionless. Ul…

Larvaanimal structuresbiologyChemistryHatchingfungiEmbryogenesisGeneral Chemistrybiology.organism_classificationChlorideInorganic ChemistryAndrologychemistry.chemical_compoundembryonic structuresmedicineTributyltinUltrastructureCiona intestinalisMyofibrilmedicine.drugApplied Organometallic Chemistry
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Organometallic complexes with biological molecules: XVI. Endocrine disruption effects of tributyltin(IV)chloride on metamorphosis of the ascidian lar…

2001

The effects of tributyltin(IV)chloride (TBT) on the metamorphosis of ascidian larvae of Ciona intestinalis, 2 h after hatching, were investigated. Ascidians are protochordates that lack thyroid follicles and possess thyroid hormones (THs) and their precursors, 3-monoiodo-tyrosine (MIT) and 3,5-diiodo-tyrosine (DIT), in their endostyle. According to recent findings, these hormones are also present at larval stages, localize in mesenchymal cells and their function seems to be mainly related to larval transformations. Here, we investigate the effects of TBT on thyroxine (T4) content and localization by exposing larvae of C. intestinalis for different times to TBT concentrations known to block …

Larvaanimal structuresbiologyChemistrymedia_common.quotation_subjectfungiThyroidGeneral Chemistrybiology.organism_classificationCell biologyInorganic ChemistryToxicologychemistry.chemical_compoundmedicine.anatomical_structuremedicineTributyltinEndocrine systemCiona intestinalisMetamorphosismedia_commonHormoneEndostyleApplied Organometallic Chemistry
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LPS injection reprograms the expression and the 3′ UTR of a CAP gene by alternative polyadenylation and the formation of a GAIT element in Ciona inte…

2016

The diversification of cellular functions is one of the major characteristics of multicellular organisms which allow cells to modulate their gene expression, leading to the formation of transcripts and proteins with different functions and concentrations in response to different stimuli. CAP genes represent a widespread family of proteins belonging to the cysteine-rich secretory protein, antigen 5 and pathogenesis-related 1 superfamily which, it has been proposed, play key roles in the infection process and the modulation of immune responses in host animals. The ascidian Ciona intestinalis represents a group of proto-chordates with an exclusively innate immune system that has been widely st…

Lipopolysaccharides0301 basic medicineGene isoformUntranslated regionCiona intestinalisCAP proteinPolyadenylationGAIT element LPSPolyadenylationImmunologySettore BIO/05 - ZoologiaBiologyPolyadenylationPolymerase Chain Reaction03 medical and health sciencesExonGene expressionAnimalsCiona intestinalisAmino Acid SequenceRegulatory Elements Transcriptional3' Untranslated RegionsMolecular BiologyGeneIn Situ HybridizationGeneticsBase SequenceThree prime untranslated regionGene Expression Profilingbiology.organism_classificationCiona intestinalis030104 developmental biologyGene Expression RegulationRNA Cap-Binding ProteinsTranscriptomeSequence AlignmentMolecular Immunology
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Identification of CPE and GAIT elements in 3’UTR of macrophage migration inhibitory factor (MIF) involved in inflammatory response induced by LPS in …

2018

Innate immune responses face infectious microorganisms by inducing inflammatory responses. Multiple genes within distinct functional categories are coordinately and temporally regulated by transcriptional 'on' and 'off' switches that account for the specificity of gene expression in response to external stimuli. Mechanisms that control transcriptional and post-transcriptional regulation are important in coordinating the initiation and resolution of inflammation. Macrophage migration inhibitory factor (MIF) is an important cytokine that, in Ciona robusta, is related to inflammatory response. It is well known that in C. robusta, formerly known as Ciona intestinalis, the pharynx is involved in…

Lipopolysaccharides0301 basic medicineUntranslated regionImmunology03 medical and health sciences0302 clinical medicineGene expressionAnimalsCiona intestinalisAmino Acid SequenceRNA Processing Post-Transcriptional3' Untranslated RegionsMacrophage Migration-Inhibitory FactorsMolecular BiologyGenePhylogenyInflammationRegulation of gene expressionInnate immune systemBase SequencebiologyThree prime untranslated regionbiology.organism_classificationImmunity InnateCiona intestinalisUp-RegulationAscidianMacrophage migration inhibitory factorInflammationLPSCiona robustaCell biology030104 developmental biologyGene Expression Regulation030220 oncology & carcinogenesisMacrophage migration inhibitory factorSequence AlignmentMolecular Immunology
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Evolutionary and transcriptional analyses of a pentraxin-like component family involved in the LPS inflammatory response of Ciona robusta

2020

Pentraxins (PTXs) are a superfamily of conserved proteins which are components of the humoral arm of innate immunity. They are considered to be functional ancestors of antibodies and are classified into short and long types. In this study, we show that a pentraxin-like component (Ptx-like) with a C-terminal PTX domain, highly homologous to the short PTX of H. sapiens CRP, and a long N-terminal domain typical of long PTXs, is involved in the inflammatory response of Ciona robusta under LPS exposure in vivo. Analyses of protein domains as well as 3D modelling and phylogenetic tree supported the close relationship of Ptx-like with mammalian CRP, suggesting that C. robusta Ptx-like shares a com…

Lipopolysaccharides3D model0301 basic medicineLPSTranscription GeneticProtein domainSettore BIO/05 - ZoologiaChordateSettore BIO/08 - AntropologiaAquatic ScienceEvolution Molecular03 medical and health sciencesDownregulation and upregulationIn vivoAnimalsEnvironmental ChemistryCiona robustaPTXsInflammationInnate immune systemPentraxinsbiologyPhylogenetic tree04 agricultural and veterinary sciencesGeneral Medicinebiology.organism_classificationImmunity InnateCiona intestinalisCell biologyC-Reactive Protein030104 developmental biologyMultigene Family040102 fisheriesbiology.protein0401 agriculture forestry and fisheriesAntibodyFish & Shellfish Immunology
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