Search results for "Molecular sequence"

showing 10 items of 1972 documents

Characterization of small HSPs from Anemonia viridis reveals insights into molecular evolution of alpha crystallin genes among cnidarians.

2014

Gene family encoding small Heat-Shock Proteins (sHSPs containing α-crystallin domain) are found both in prokaryotic and eukaryotic organisms; however, there is limited knowledge of their evolution. In this study, two small HSP genes termed AvHSP28.6 and AvHSP27, both organized in one intron and two exons, were characterised in the Mediterranean snakelocks anemone Anemonia viridis. The release of the genome sequence of Hydra magnipapillata and Nematostella vectensis enabled a comprehensive study of the molecular evolution of α-crystallin gene family among cnidarians. Most of the H. magnipapillata sHSP genes share the same gene organization described for AvHSP28.6 and AvHSP27, differing from …

LipopolysaccharidesMarine and Aquatic SciencesGene ExpressionCnidarianSea anemoneGenomeAnemoniaGene duplicationProtein Isoformsalpha-CrystallinsPhylogenyGenomic organizationGeneticsMultidisciplinarybiologyReverse Transcriptase Polymerase Chain ReactionQTemperatureRMedicineAnemonia viridiSmall HSP; Anemonia viridis; Cnidarians; molecular evolutionResearch ArticleScienceMolecular Sequence DataMarine BiologySmall HSPEvolution MolecularCnidariaSpecies SpecificityMolecular evolutionMetals HeavySequence Homology Nucleic AcidAnimalsGene familyAmino Acid SequenceMolecular BiologyGeneEvolutionary BiologyBase SequenceSequence Homology Amino Acidmolecular evolutionGene Expression ProfilingEcology and Environmental SciencesBiology and Life SciencesAquatic EnvironmentsCell Biologybiology.organism_classificationHeat-Shock Proteins SmallSea AnemonesEarth SciencesPLoS ONE
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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 & 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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Potential biological role of laccase from the sponge Suberites domuncula as an antibacterial defense component

2014

Abstract Background Laccases are copper-containing enzymes that catalyze the oxidation of a wide variety of phenolic substrates. Methods We describe the first poriferan laccase from the marine demosponge Suberites domuncula. Results This enzyme comprises three characteristic multicopper oxidase homologous domains. Immunohistological studies revealed that the highest expression of the laccase is in the surface zone of the animals. The expression level of the laccase gene is strongly upregulated after exposure of the animals to the bacterial endotoxin lipopolysaccharide. To allow the binding of the recombinant enzyme to ferromagnetic nanoparticles, a recombinant laccase was prepared which con…

LipopolysaccharidesMolecular Sequence DataBiophysicsMulticopper oxidaseFerric CompoundsLigninBiochemistryMichaelis–Menten kineticsGene Expression Regulation EnzymologicSubstrate Specificitychemistry.chemical_compoundEscherichia coliAnimalsLigninAmino Acid SequenceMolecular BiologyPhylogenyLaccasechemistry.chemical_classificationDose-Response Relationship DrugSequence Homology Amino AcidbiologyReverse Transcriptase Polymerase Chain ReactionChemistryLaccaseHydrazonesSubstrate (chemistry)biology.organism_classificationRecombinant ProteinsAnti-Bacterial AgentsUp-RegulationSuberites domunculaKineticsEnzymeBiochemistryBiocatalysisNanoparticlesSuberitesOxidation-ReductionIron oxide nanoparticlesBiochimica et Biophysica Acta (BBA) - General Subjects
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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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The novel structure of the core oligosaccharide backbone of the lipopolysaccharide from the Plesiomonas shigelloides strain CNCTC 8089 (serotype O13)

2013

The new structure of the core oligosaccharide of Plesiomonas shigelloides CNCTC 80/89 (serotype O13) lipopolysaccharide has been investigated by chemical methods, (1)H and (13)C NMR spectroscopy and matrix-assisted laser-desorption/ionization time of flight (MALDI-TOF). It was concluded that the core oligosaccharide of P. shigelloides CNCTC 80/89 is a nonasaccharide with the following structure: The position of glycine was determined by MALDI-TOF MS/MS analyses.

LipopolysaccharidesSerotypechemistry.chemical_classificationbiologyStrain (chemistry)ChemistryStereochemistryMolecular Sequence DataOrganic ChemistryOligosaccharidesGeneral MedicineCarbon-13 NMROligosaccharideDEPTbiology.organism_classificationBiochemistryAnalytical ChemistryCarbohydrate SequenceBiochemistryPlesiomonas shigelloidesPlesiomonasTwo-dimensional nuclear magnetic resonance spectroscopyHeteronuclear single quantum coherence spectroscopyCarbohydrate Research
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Structure of a polysaccharide from the lipopolysaccharides of Vibrio vulnificus strains CECT 5198 and S3-I2-36, which is remarkably similar to the O-…

2009

High-molecular-mass polysaccharides were released by mild acid degradation of the lipopolysaccharides of two wild-type Vibrio vulnificus strain, a flagellated motile strain CECT 5198 and a non-flagellated non-motile strain S3-I2-36. Studies by sugar analysis and partial acid hydrolysis along with (1)H and (13)C NMR spectroscopies showed that the polysaccharides from both strains have the same trisaccharide repeating unit of the following structure: --4)-beta-d-GlcpNAc3NAcylAN-(1--4)-alpha-l-GalpNAmA-(1--3)-alpha-d-QuipNAc-(1--where QuiNAc stands for 2-acetamido-2,6-dideoxyglucose, GalNAmA for 2-acetimidoylamino-2-deoxygalacturonic acid, GlcNAc3NAcylAN for 2-acetamido-3-acylamino-2,3-dideoxy…

LipopolysaccharidesSpectrometry Mass Electrospray IonizationMagnetic Resonance SpectroscopyLipopolysaccharideStereochemistryMolecular Sequence DataMalatesVibrio vulnificusPolysaccharideBiochemistryAnalytical Chemistrychemistry.chemical_compoundTrisaccharideVibrio vulnificuschemistry.chemical_classificationMolecular StructurebiologyStrain (chemistry)Polysaccharides BacterialOrganic ChemistryAbsolute configurationGeneral Medicinebiology.organism_classificationPseudoalteromonasCarbohydrate SequencechemistryBiochemistryMalic acidBacteriaCarbohydrate Research
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Identification and characterization of a novel Ets-2-related nuclear complex implicated in the activation of the human interleukin-12 p40 gene promot…

1997

Interleukin-12 (IL-12) is a proinflammatory cytokine produced by antigen-presenting cells in response to many microbial infections. IL-12 plays an important role in the generation of T helper type-1 cells, which favor cell-mediated immune response. IL-12 is composed of two different subunits, p40 and p35, whose expression can be regulated concomitantly or differentially. Monocytic cells, the major producers of IL-12, can be primed by interferon-gamma (IFN-gamma) to produce optimal amounts of IL-12 in response to LPS stimulation as a consequence of bacterial infection. The priming effect is exerted primarily at the transcriptional level on the p40 promoter in conjunction with the effects of …

LipopolysaccharidesTranscription GeneticSequence HomologyStimulationbiosynthesis/geneticsBiochemistryChromatography Affinitychemistry.chemical_compoundMiceAnimals Base Sequence Cell Line Cell Nucleus; metabolism Chromatography; Affinity DNA-Binding Proteins Humans Interferon-gamma; pharmacology Interleukin-12; biosynthesis/genetics Kinetics Lipopolysaccharides; pharmacology Mice Molecular Sequence Data Nuclear Proteins; isolation /&/ purification/metabolism Promoter Regions; Genetic Protein-Tyrosine Kinases; metabolism Proto-Oncogene Protein c-ets-2 Proto-Oncogene Proteins; isolation /&/ purification/metabolism Repressor Proteins Sequence Homology; Nucleic Acid Trans-Activators; isolation /&/ purification/metabolism Transcription Factors Transcription; Genetic; drug effectsPromoter Regions GeneticChromatographyNuclear ProteinsMethylationProtein-Tyrosine KinasesInterleukin-12DNA-Binding ProteinsTranscriptionMolecular Sequence DataBiologyProinflammatory cytokineCell LineProto-Oncogene Protein c-ets-2Promoter RegionsInterferon-gammaGeneticSequence Homology Nucleic AcidProto-Oncogene ProteinsAnimalsHumansMolecular BiologyTranscription factorCell NucleusMolecular massBase SequenceNucleic Acidisolation /&/ purification/metabolismPromoterCell BiologyMolecular biologyIn vitroRepressor ProteinsKineticschemistryAffinitydrug effectsTrans-ActivatorspharmacologymetabolismDNATranscription Factors
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Characterization of two alternative Interleukin(IL)-10 5′UTR mRNA sequences, induced by lipopolysaccharide (LPS) stimulation of peripheral blood mono…

2009

Abstract IL-10 production shows a broad-spectrum of individual response, suggesting a genetic component of approximately 75%. Different polymorphisms located close to, or within the IL-10 gene has been demonstrated to influence its transcription rate whereas the post-transcriptional regulation of IL-10 production has not well elucidated. The main responsible elements at this control level are both the 5′- and 3′-untranslated regions (UTR's) of mRNAs, and as the 3′-UTR regions are mainly involved in the stability and decay rate of mRNAs, the 5′-UTR regions mediate the binding rate of the molecule with ribosomal 40S subunit as a cis-acting element. Herein are report data on the identification…

LipopolysaccharidesUntranslated regionFive prime untranslated regionmRNALPS stimulationMolecular Sequence DataImmunologyStimulationRegulatory Sequences Nucleic AcidBiologyPeripheral blood mononuclear cellInterleukin(IL)-10Secondary structureHumansEukaryotic Small Ribosomal SubunitRNA MessengerMolecular BiologyCells CulturedMessenger RNABase Sequence5′UTR regionInterleukinMolecular biologyInterleukin-10Interleukin 10Gene Expression RegulationLeukocytes MononuclearNucleic Acid Conformation5' Untranslated RegionsMolecular Immunology
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Core oligosaccharide of Escherichia coli B—the structure required for bacteriophage T4 recognition

2015

Abstract The structure of Escherichia coli B strain PCM 1935 core oligosaccharide has been investigated by 1H and 13C NMR spectroscopy, MALDI-TOF MS and ESI MSn. It was concluded that the core oligosaccharide is a pentasaccharide with the following structure: ESI MS/MS analysis revealed that the glycine (a minor component) is linked to the →3,7)- l -α- d -Hepp-(1→ residue.

Lipopolysaccharidesanimal structuresStereochemistryElectrospray ionizationMolecular Sequence Datamedicine.disease_causeBiochemistryAnalytical ChemistryBacteriophageResidue (chemistry)13c nmr spectroscopyEscherichia colimedicineBacteriophage T4Escherichia coliChromatographybiologyStrain (chemistry)ChemistryCore oligosaccharideOrganic ChemistryGeneral Medicinebiology.organism_classificationEscherichia coli B; Core oligosaccharide; glycine; NMR; MALDI-TOF; ESI MSCarbohydrate SequenceGlycineCarbohydrate Research
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