Search results for "Vertebrate"

showing 10 items of 830 documents

Origin of the prolactin-releasing hormone (PRLH) receptors: evidence of coevolution between PRLH and a redundant neuropeptide Y receptor during verte…

2004

We present seven new vertebrate homologs of the prolactin-releasing hormone receptor (PRLHR) and show that these are found as two separate subtypes, PRLHR1 and PRLHR2. Analysis of a number of vertebrate sequences using phylogeny, pharmacology, and paralogon analysis indicates that the PRLHRs are likely to share a common ancestry with the neuropeptide Y (NPY) receptors. Moreover, a micromolar level of NPY was able to bind and inhibit completely the PRLH-evoked response in PRLHR1-expressing cells. We suggest that an ancestral PRLH peptide started coevolving with a redundant NPY binding receptor, which then became PRLHR, approximately 500 million years ago. The PRLHR1 subtype was shown to have…

Prolactin-releasing hormoneGeneticsBase SequenceMolecular Sequence DataBiologyNeuropeptide Y receptorProlactinReceptors G-Protein-CoupledReceptors Neuropeptide YEvolution MolecularPhylogeneticsMolecular evolutionHormone receptorGene DuplicationGene duplicationVertebratesGeneticsAnimalsHumansReceptorPhylogenyGenomics
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Cloning of Sponge (Geodia cydonium) and Tunicate (Botryllus schlosseri) Proteasome Subunit Epsilon (PRCE): Implications about the Vertebrate MHC-Enco…

1996

Proteasomes are large protein complexes that play a major role in selective degradation of intracellular proteins. Eukaryotes feature seven different alpha and beta subunits. Two of the vertebrate housekeeping beta-subunits have MHC-encoded homologues that can substitute for the housekeeping counterparts upon interferon-gamma induction. In the present study we report the cloning of invertebrate beta-subunit proteasome epsilon (PRCE), from the marine sponge Geodia cydonium and from the colonial tunicate Botryllus schlosseri. Sequence comparisons revealed that the sponge and tunicate proteins are strikingly similar to vertebrate and yeast PRCEs and their MHC-linked counterparts the PRCCs (als…

Proteasome Endopeptidase ComplexDNA ComplementaryProtein subunitMolecular Sequence DataBiophysicsSaccharomyces cerevisiaeBotryllus schlosseriPolymerase Chain ReactionBiochemistryMiceMultienzyme ComplexesConsensus SequenceBotanyAnimalsHumansAmino Acid SequenceUrochordataCloning MolecularProtein precursorMolecular BiologyPhylogenyDNA Primerschemistry.chemical_classificationCloningBase SequenceSequence Homology Amino AcidbiologyProteinsCell Biologybiology.organism_classificationYeastPoriferaRatsAmino acidTunicateCell biologyCysteine EndopeptidaseschemistryProteasomeVertebratesChickensBiochemical and Biophysical Research Communications
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A tunicate (Botryllus schlosseri) cDNA reveals similarity to vertebrate antigen receptors

1996

Protein FoldingDNA ComplementaryProtein ConformationMolecular Sequence DataImmunologyBotryllus schlosseriSimilarity (network science)biology.animalComplementary DNAGeneticsAnimalsHumansAmino Acid SequenceUrochordataCloning MolecularBase SequenceSequence Homology Amino AcidbiologyVertebrateAnatomybiology.organism_classificationHuman geneticsTunicateReceptors AntigenEvolutionary biologyAntigen receptorsImmunogenetics
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Phylointeractomics reconstructs functional evolution of protein binding

2017

Molecular phylogenomics investigates evolutionary relationships based on genomic data. However, despite genomic sequence conservation, changes in protein interactions can occur relatively rapidly and may cause strong functional diversification. To investigate such functional evolution, we here combine phylogenomics with interaction proteomics. We develop this concept by investigating the molecular evolution of the shelterin complex, which protects telomeres, across 16 vertebrate species from zebrafish to humans covering 450 million years of evolution. Our phylointeractomics screen discovers previously unknown telomere-associated proteins and reveals how homologous proteins undergo functiona…

Proteomics0301 basic medicineLineage (evolution)ScienceTelomere-Binding ProteinsGeneral Physics and AstronomyGenomicsBiologyProteomicsArticleGeneral Biochemistry Genetics and Molecular BiologyConserved sequenceEvolution Molecular03 medical and health sciencesPhylogeneticsMolecular evolutionPhylogenomicsAnimalsCells CulturedConserved SequencePhylogenyGeneticsGenomeMultidisciplinaryQComputational BiologyGenomicsSequence Analysis DNAGeneral ChemistryTelomereProtein superfamily030104 developmental biologyEvolutionary biologyVertebratesSequence AlignmentProtein Binding
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Sialotranscriptomics of the argasid tick ornithodoros moubata along the trophogonic cycle

2021

32 páginas, 8 tablas, 6 figuras

Proteomics0301 basic medicineSwinePhysiologyRC955-962Gene ExpressionDisease VectorsProteomicsBiochemistryTranscriptomeMedical Conditions0302 clinical medicineTicksArctic medicine. Tropical medicineGene expressionMedicine and Health SciencesHuman relapsing feverGeneticsbiologyEukaryotaGenomicsProteasesBody FluidsEnzymesBloodInfectious DiseasesFemaleMetabolic PathwaysAnatomyPublic aspects of medicineRA1-1270Transcriptome analysisVitellogeninsMetabolic Networks and PathwaysResearch ArticleIxodidaeArthropoda030231 tropical medicineTickSalivary glandsArthropod Proteins03 medical and health sciencesExocrine GlandsOrnithodoros moubataArachnidaGeneticsAnimalsXenobiotic MetabolismTick ControlOrnithodorosSalivaIllumina dye sequencingIxodesAsfarviridaeImmunityOrganismsPublic Health Environmental and Occupational HealthBiology and Life SciencesComputational BiologyProteinsGenome Analysisbiology.organism_classificationInvertebratesOrnithodoros moubataPhospholipases A2Species InteractionsMetabolism030104 developmental biologyAfricaEnzymologyMetalloproteasesAfrican swine feverTranscriptomeDigestive SystemZoology
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Unraveling the Composition of Insecticidal Crystal Proteins in Bacillus thuringiensis: a Proteomics Approach.

2020

ABSTRACT Bacillus thuringiensis (Bt) is the most widely used active ingredient for biological insecticides. The composition of δ-endotoxins (Cry and Cyt proteins) in the parasporal crystal determines the toxicity profile of each Bt strain. However, a reliable method for their identification and quantification has not been available, due to the high sequence identity of the genes that encode the δ-endotoxins and the toxins themselves. Here, we have developed an accurate and reproducible mass spectrometry-based method (liquid chromatography-tandem mass spectrometry-multiple reaction monitoring [LC-MS/MS-MRM]) using isotopically labeled proteotypic peptides for each protein in a particular mix…

ProteomicsInsecticidesProteomeQuantitative proteomicsBacillus thuringiensisProteomics01 natural sciencesApplied Microbiology and Biotechnology03 medical and health sciencesBiosafetyHemolysin ProteinsBacterial ProteinsTandem Mass SpectrometryBacillus thuringiensisInvertebrate Microbiology030304 developmental biologyPhytosanitary certificationActive ingredient0303 health sciencesChromatographyEcologybiologyBacillus thuringiensis ToxinsChemistry010401 analytical chemistrybiology.organism_classification0104 chemical sciencesEndotoxinsComposition (visual arts)FermentationFood ScienceBiotechnologyChromatography LiquidApplied and environmental microbiology
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Changes in the proteome of sea urchin Paracentrotus lividus coelomocytes in response to LPS injection into the body cavity.

2020

Background The immune system of echinoderm sea urchins is characterised by a high degree of complexity that is not completely understood. The Mediterranean sea urchin Paracentrotus lividus coelomocytes mediate immune responses through phagocytosis, encapsulation of non-self particles, and production of diffusible factors including antimicrobial molecules. Details of these processes, and molecular pathways driving these mechanisms, are still to be fully elucidated. Principal findings In the present study we treated the sea urchin P. lividus with the bacterial lipopolysaccharide (LPS) and collected coelomocytes at different time-points (1, 3, 6 and 24 hours). We have shown, using label-free q…

ProteomicsLipopolysaccharidesProteomeHydrolasesBiochemistry0302 clinical medicineParacentrotusMedicine and Health SciencesSea urchinCoelomocyteImmune ResponseCytoskeleton0303 health sciencesPhagocytesMultidisciplinarybiologyChemistryQREukaryotaAnimal ModelsCell biologyEnzymesEchinodermExperimental Organism Systems030220 oncology & carcinogenesisProteomeParacentrotusMedicineProtein Interaction NetworksCellular Structures and OrganellesNetwork AnalysisResearch ArticleEchinodermsComputer and Information Sciencesfood.ingredientScienceImmunologyLipopolysaccharideEndocytosisResearch and Analysis MethodsParacentrotus lividusLymphatic System03 medical and health sciencesfoodPhagocytosisbiology.animalHeat shock proteinDNA-binding proteinsAnimalsProtein Interactions030304 developmental biologyPhagocytosiAnimalOrganismsBiology and Life SciencesProteinsCell Biologybiology.organism_classificationInvertebratesCytoskeletal ProteinsGuanosine TriphosphataseProtein-Protein InteractionsPhagocyteImmune SystemSea UrchinsAnimal StudiesEnzymologyParacentrotuPLoS ONE
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CiliaCarta: An integrated and validated compendium of ciliary genes

2019

The cilium is an essential organelle at the surface of mammalian cells whose dysfunction causes a wide range of genetic diseases collectively called ciliopathies. The current rate at which new ciliopathy genes are identified suggests that many ciliary components remain undiscovered. We generated and rigorously analyzed genomic, proteomic, transcriptomic and evolutionary data and systematically integrated these using Bayesian statistics into a predictive score for ciliary function. This resulted in 285 candidate ciliary genes. We generated independent experimental evidence of ciliary associations for 24 out of 36 analyzed candidate proteins using multiple cell and animal model systems (mouse…

ProteomicsSensory ReceptorsNematodaSocial SciencesCiliopathiesBiochemistrySensory disorders Donders Center for Medical Neuroscience [Radboudumc 12]Transcriptome0302 clinical medicineAnimal CellsPsychologyRETINAL PHOTORECEPTOR CELLSExomeNeurons0303 health sciences030302 biochemistry & molecular biologyEukaryotaGenomicsPRIMARY CILIUMthecilium3. Good healthNucleic acidsGenetic interferenceOsteichthyesMedicineEpigeneticsCellular Structures and OrganellesCellular Typesproteomic databasesSensory Receptor CellsScienceeducationCiliary genesLEBER CONGENITAL AMAUROSISGenomics03 medical and health sciencesGeneticsCiliaCaenorhabditis elegansIDENTIFICATIONMUTATIONSEmbryosciliaOrganismsBiology and Life SciencesBayes TheoremMolecular Sequence Annotationmedicine.diseaseInvertebratesFishciliary proteomeAnimal StudiesCaenorhabditisGene expressionembryos030217 neurology & neurosurgeryDevelopmental BiologyNeurosciencePhotoreceptorsCandidate geneEmbryologyOligonucleotidesMorpholinoDatabase and Informatics MethodsRNA interferenceBayesian classifierTRANSITION ZONEZebrafishAntisense OligonucleotidesZebrafishGeneticsMultidisciplinarySpectrometric Identification of ProteinsProteomic DatabasesNucleotidesCiliumQStable Isotope Labeling by Amino Acids in Cell CultureRphotoreceptorsMetabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6]Animal ModelsPhenotypeINTRAFLAGELLAR TRANSPORTDIFFERENTIATIONPhenotypeExperimental Organism SystemsCaenorhabditis ElegansVertebratesSensory PerceptionResearch ArticleSignal TransductionEXPRESSIONStable isotope labeling by amino acids in cell cultureComputational biologyBiologyResearch and Analysis MethodsSOLUTE-CARRIER-PROTEINModel OrganismsmedicineAnimalsdata integration030304 developmental biologyAfferent NeuronsReproducibility of ResultsCell Biologyzebrafishbiology.organism_classificationCiliopathyRenal disorders Radboud Institute for Molecular Life Sciences [Radboudumc 11]Biological DatabasesCellular NeuroscienceRNAOSCP1CiliaCartaPLoS ONE
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The Globin Gene Repertoire of Lampreys: Convergent Evolution of Hemoglobin and Myoglobin in Jawed and Jawless Vertebrates

2014

Agnathans (jawless vertebrates) occupy a key phylogenetic position for illuminating the evolution of vertebrate anatomy and physiology. Evaluation of the agnathan globin gene repertoire can thus aid efforts to reconstruct the origin and evolution of the globin genes of vertebrates, a superfamily that includes the well-known model proteins hemoglobin and myoglobin. Here, we report a comprehensive analysis of the genome of the sea lamprey (Petromyzon marinus )w hich revealed 23 intact globin genes and two hemoglobin pseudogenes. Analyses of the genome of the Arctic lamprey (Lethenteron camtschaticum) identified 18 full length and five partial globin gene sequences. The majority of the globin …

PseudogeneEvolution Molecularbiology.animalGene DuplicationGeneticsAnimalsGlobinMolecular BiologyEcology Evolution Behavior and SystematicsDiscoveriesPhylogenyAgnathaGeneticsGenomebiologyLampreyMyocardiumCytoglobinVertebrateLampreysGnathostomatabiology.organism_classificationArctic lampreyGlobinsOrgan SpecificityVertebratesPseudogenes
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Tropomyosin: A panallergen that causes a worldwide allergic problem

2021

Background: Panallergens are proteins that take part in key processes of organisms and, therefore, are ubiquitously distributed with highly conserved sequences and structures. One class of these panallergens is composed of the tropomyosins. The highly heat-stable tropomyosins comprise the major allergens in crustaceans and mollusks, which make them important food allergens in exposed populations. Tropomyosins are responsible for a widespread immunoglobulin E cross-reactivity among allergens from different sources. Allergic tropomyosins are expressed in many species, including parasites and insects. Methods: This panallergen class is divided, according to it capacity of induced allergic symp…

Pulmonary and Respiratory Medicineinsect allergymacromolecular substancesCross Reactionsmedicine.disease_causeImmunoglobulin EConserved sequencetropomyosinAllergenFood allergybiology.animalmedicineImmunology and AllergyHumansAmino Acid Sequenceseafood allergyGeneticsfood allergybiologybusiness.industryVertebrateGeneral MedicineArticlesAllergensImmunoglobulin Emedicine.diseasemusculoskeletal systemTropomyosinIgE cross-reactivitypanallergenAllergic responsebiology.proteinhouse-dust mite allergyAllergistsbusinesstissuesFood Hypersensitivity
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