Search results for "alignment"

showing 10 items of 627 documents

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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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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The major allergen of the Parietaria pollen contains an LPS-binding region with immuno-modulatory activity

2013

Background The major allergens in Parietaria pollen, Par j 1 and Par j 2, have been identified as lipid transfer proteins. The family of the Par j 1 allergens is composed of two isoforms, which differ by the presence of a 37 amino acid peptide (Par37) exclusive to the Par j 1.0101 isoform. The goal of this study was to elucidate the biological properties of the Par37 peptide. Methods In silico analysis, spectrofluorimetric experiments and in vitro cell culture assays were used to identify the biological properties of Par37. In addition, a mouse model of sensitization was used to study the influence of Par37 in the murine immune response. Results In silico analysis predicted that Par37 displ…

LipopolysaccharidesGene isoformParietariaIn silicoMolecular Sequence DataImmunologySettore BIO/11 - Biologia MolecolarePeptideBiologyAntibodiesInterferon-gammaMiceIn vivoAnimalsHumansImmunologic FactorsImmunology and AllergyAmino Acid SequencePlant ProteinsPolymyxin Bchemistry.chemical_classificationanimal modelallergens; animal models; environment; pollens.Allergensbiology.organism_classificationIn vitroAmino acidParietariachemistryBiochemistryLeukocytes MononuclearCytokinesPollenpollens.FemalePeptidesenvironmentSequence AlignmentPlant lipid transfer proteinsSpleenallergenProtein Binding
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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 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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LPS challenge regulates gene expression and tissue localization of a Ciona intestinalis gene through an alternative polyadenylation mechanism.

2013

A subtractive hybridization strategy for the identification of differentially expressed genes was performed between LPS-challenged and naive Ciona intestinalis. This strategy allowed the characterization of two transcripts (Ci8short and Ci8long) generated by the use of two Alternative Polyadenylation sites. The Ci8long transcript contains a protein domain with relevant homology to several components of the Receptor Transporting Protein (RTP) family not present in the Ci8short mRNA. By means of Real Time PCR and Northern Blot, the Ci8short and Ci8long transcripts showed a different pattern of gene expression with the Ci8short mRNA being strongly activated after LPS injection in the pharynx. …

LipopolysaccharidesPolyadenylationCiona intestinaliSettore BIO/05 - Zoologialcsh:MedicineGene ExpressionBiochemistryGene expressionGene Orderlcsh:Science3' Untranslated RegionsPhylogenyIn Situ HybridizationRegulation of gene expressionMultidisciplinaryInnate ImmunityCiona intestinalisPhylogeneticsProtein TransportCytochemistryResearch ArticleDNA ComplementaryMolecular Sequence DataImmunologyIn situ hybridizationBiologyPolyadenylationModel OrganismsGeneticsAnimalsCiona intestinalisEvolutionary SystematicsNorthern blotAmino Acid SequenceRNA MessengerBiologyEvolutionary BiologyBase SequenceThree prime untranslated regionlcsh:RImmunityComputational BiologyProteinsImmune Defensebiology.organism_classificationMolecular biologyGenesinflammationSuppression subtractive hybridizationlcsh:Q5' Untranslated RegionsCiona intestinalis; inflammationSequence AlignmentPloS one
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A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at the plasma membrane.

2011

http://linkinghub.elsevier.com/; International audience; Concentration gradients regulate many cell biological and developmental processes. In rod-shaped fission yeast cells, polar cortical gradients of the DYRK family kinase Pom1 couple cell length with mitotic commitment by inhibiting a mitotic inducer positioned at midcell. However, how Pom1 gradients are established is unknown. Here, we show that Tea4, which is normally deposited at cell tips by microtubules, is both necessary and, upon ectopic cortical localization, sufficient to recruit Pom1 to the cell cortex. Pom1 then moves laterally at the plasma membrane, which it binds through a basic region exhibiting direct lipid interaction. …

MESH : Molecular Sequence Data[SDV]Life Sciences [q-bio]CellMESH: Cell CycleMESH: Amino Acid SequenceAmino Acid Sequence; Cell Cycle; Cell Membrane/metabolism; Microtubule-Associated Proteins/metabolism; Molecular Sequence Data; Phosphorylation; Protein Kinases/chemistry; Protein Kinases/metabolism; Schizosaccharomyces/cytology; Schizosaccharomyces/metabolism; Schizosaccharomyces pombe Proteins/metabolism; Sequence AlignmentMESH : Phosphorylation0302 clinical medicinePhosphorylation0303 health sciencesKinaseMESH : Amino Acid SequenceMESH : Sequence AlignmentCell CycleCortical gradientMESH : Schizosaccharomyces pombe ProteinsFission yeastCell biologymedicine.anatomical_structureMESH: SchizosaccharomycesPom1PhosphorylationMicrotubule-Associated ProteinsMESH : Cell MembraneMolecular Sequence DataMESH: Sequence AlignmentMESH : Protein KinasesBiologyGeneral Biochemistry Genetics and Molecular BiologyPom1Dephosphorylation03 medical and health sciencesMicrotubuleMESH : Cell CycleSchizosaccharomycesCell cortexmedicineAmino Acid SequenceMitosisMESH: Protein Kinases030304 developmental biologyMESH: Molecular Sequence Data[ SDV ] Life Sciences [q-bio]Phosphorylation cycleMESH: PhosphorylationBiochemistry Genetics and Molecular Biology(all)Cell MembraneMESH: Schizosaccharomyces pombe ProteinsMESH: Microtubule-Associated ProteinsMESH : SchizosaccharomycesMESH : Microtubule-Associated ProteinsSchizosaccharomyces pombe ProteinsDYRK family kinaseProtein KinasesSequence Alignment030217 neurology & neurosurgeryMESH: Cell Membrane
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Cloning and expression of genes involved in conidiation and surface properties of Penicillium camemberti grown in liquid and solid cultures.

2008

International audience; Based on bioinformatic data on model fungi, the rodA and wetA genes encoding, respectively, a RodA hydrophobin protein and the WetA protein involved in conidiation mechanisms, were PCR-cloned and characterized for the first time in Penicillium camemberti. These results, completed by a sequence of the brlA gene (available in GenBank), which encodes a major transcriptional regulator also involved in the conidiation mechanism, were used to compare, by qRT-PCR, the expression of the three genes in liquid and solid cultures in a synthetic medium. While expression of the brlA and wetA genes increased dramatically in both culture conditions after 4 days of growth, expressio…

MESH: Sequence Analysis DNAMESH : Spores FungalMESH : Molecular Sequence DataConidiationMESH: Amino Acid SequenceMESH: Base SequenceGene Expression Regulation FungalGene expressionMESH : Fungal ProteinsCloning MolecularFungal proteinMESH : Amino Acid SequenceMESH : Sequence AlignmentGeneral MedicineSpores FungalMESH: MyceliumCell biologyWetaPenicillium camembertiMESH: Fungal ProteinsMESH : HydrophobicityHydrophobic and Hydrophilic InteractionsMESH : MyceliumMESH: Gene Expression Regulation FungalHyphaMESH : Cloning MolecularHydrophobinMolecular Sequence DataMESH: Sequence AlignmentBiologyMicrobiologyMicrobiologyFungal ProteinsMESH: Spores FungalMESH : Gene Expression Regulation FungalMESH: Cloning Molecular[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMolecular BiologyGene[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: PenicilliumMESH: HydrophobicityMESH: Molecular Sequence DataBase SequenceMyceliumPenicilliumSequence Analysis DNAMESH : Penicilliumbiology.organism_classificationCulture MediaMESH: Culture MediaMESH : Base SequenceMESH : Culture MediaSequence AlignmentMESH : Sequence Analysis DNA
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Identification and characterization of a gene encoding a putative mouse Rho GTPase activating protein gene 8, Arhgap8.

2003

Rho GTPase activating proteins promote the intrinsic GTP hydrolysis activity of Rho family proteins. We isolated a putative mouse ortholog of the human Rho GTPase activating protein 8, ARHGAP8. The open reading frame encodes a peptide of 387 amino acids with high homology to human ARHGAP8 in its N-terminal domain. Both radiation hybrid mapping and fluorescent in situ hybridization localized the gene to mouse chromosome 15E. The 23 kb genomic Arhgap8 sequence consists of eight exons and seven introns. Northern blot and RT-PCR analyses showed that a transcript of approximately 1.9 kb is ubiquitously expressed in various adult mouse tissues with particularly strong expression in kidney.

MaleARHGAP8DNA ComplementaryGTPase-activating proteinMolecular Sequence DataGene ExpressionGTPaseBiologyExonMiceGene expressionGeneticsAnimalsAmino Acid SequenceRNA MessengerCloning MolecularGenePeptide sequenceIn Situ Hybridization FluorescenceRadiation Hybrid MappingBase SequenceSequence Homology Amino AcidGTPase-Activating ProteinsChromosome MappingGeneral MedicineExonsSequence Analysis DNABlotting NorthernMolecular biologyIntronsOpen reading frameGenesSequence AlignmentGene
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