Search results for "Monophenol Monooxygenase"

showing 10 items of 76 documents

Condition-Dependent Trade-Off Between Weapon Size and Immunity in Males of the European Earwig

2017

Abstract Investigating the expression of trade-offs between key life-history functions is central to our understanding of how these functions evolved and are maintained. However, detecting trade-offs can be challenging due to variation in resource availability, which masks trade-offs at the population level. Here, we investigated in the European earwig Forficula auricularia whether (1) weapon size trades off with three key immune parameters – hemocyte concentration, phenoloxidase and prophenoloxidase activity - and whether (2) expression and strength of these trade-offs depend on male body condition (body size) and/or change after an immune challenge. Our results partially confirmed conditi…

MaleSex CharacteristicsHemocytesInsectaMonophenol Monooxygenase[SDV]Life Sciences [q-bio][SDV.BA]Life Sciences [q-bio]/Animal biologyScienceQImmunityRArticle570 Life sciences[SDV.BA.ZI]Life Sciences [q-bio]/Animal biology/Invertebrate ZoologyAnimalsBody SizeInsect ProteinsMedicineLife History TraitsComputingMilieux_MISCELLANEOUS570 BiowissenschaftenScientific Reports
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Behavioural and physiological effects of the trophically transmitted cestode parasite, Cyathocephalus truncatus, on its intermediate host, Gammarus p…

2007

SUMMARYSome parasites with complex life-cycles are able to manipulate the behaviour of their intermediate hosts in a way that increases their transmission to the next host. Gammarids infected by the tapeworm Cyathocephalus truncatus (Cestoda: Spathebothriidea) are known to be more predated by fish than uninfected ones, but potential behavioural manipulation by the parasite has never been investigated. In this study, we tested the hypothesis that C. truncatus is able to manipulate the behaviour of one of its intermediate hosts, Gammarus pulex (Crustacea: Amphipoda). To assess if any behavioural change was linked to other phenotypic alterations, we also measured the immunity of infected and u…

Male[ SDV.MP.PAR ] Life Sciences [q-bio]/Microbiology and Parasitology/ParasitologyAmphipodaCestodaZoologyBiologyHost-Parasite InteractionsPredationOxygen Consumption[ SDV.EE.IEO ] Life Sciences [q-bio]/Ecology environment/SymbiosisPhototaxisAnimalsParasite hostingAmphipodacestodeSwimmingEnzyme Precursors[ SDE.BE ] Environmental Sciences/Biodiversity and EcologyBehavior AnimalMonophenol MonooxygenaseHost (biology)EcologyIntermediate hostbiology.organism_classificationSurvival AnalysisimmunityGammarus pulexInfectious DiseasesCestodaAnimal Science and ZoologyParasitologypathogenic effectsCatechol OxidaseGammaridaebehavioural manipulationParasitology
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Is there a role for antioxidant carotenoids in limiting self-harming immune response in invertebrates?

2007

Innate immunity relies on effectors, which produce cytotoxic molecules that have not only the advantage of killing pathogens but also the disadvantage of harming host tissues and organs. Although the role of dietary antioxidants in invertebrate immunity is still unknown, it has been shown in vertebrates that carotenoids scavenge cytotoxic radicals generated during the immune response. Carotenoids may consequently decrease the self-harming cost of immunity. A positive relationship between the levels of innate immune defence and circulating carotenoid might therefore be expected. Consistent with this hypothesis, we show that the maintenance and use of the prophenoloxidase system strongly cor…

MaleantioxidantMESH : Immunity Natural[ SDV.IMM.IA ] Life Sciences [q-bio]/Immunology/Adaptive immunologyAntioxidantsMESH: Linear ModelsMESH: AmphipodaHemolymphMESH : Linear ModelsHemolymphMESH: AnimalsMESH : FemaleCarotenoidchemistry.chemical_classificationbiologyEffectorMonophenol Monooxygenasefood and beveragesProphenoloxidaseMESH : AmphipodaAgricultural and Biological Sciences (miscellaneous)MESH : Monophenol Monooxygenase[SDV.IMM.IA]Life Sciences [q-bio]/Immunology/Adaptive immunologyMESH : AntioxidantsFemaleGeneral Agricultural and Biological SciencesResearch ArticleMESH: Monophenol MonooxygenaseMESH : Maleimmune costsecological immunologyMESH : Hemolymph[ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyImmune systemImmunityAnimalsAmphipodaMESH: Immunity NaturalMESH : CarotenoidsInnate immune systemMESH: HemolymphMESH: Antioxidants[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologybiochemical phenomena metabolism and nutritionbiology.organism_classificationCarotenoidsImmunity InnateMESH: MaleGammarus pulexchemistryImmunologyMESH: CarotenoidsLinear ModelsbacteriaMESH : AnimalsMESH: Female
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Temporal patterns in immune responses to a range of microbial insults (Tenebrio molitor).

2008

8 pages; International audience; Much work has elucidated the pathways and mechanisms involved in the production of insect immune effector systems. However, the temporal nature of these responses with respect to different immune insults is less well understood. This study investigated the magnitude and temporal variation in phenoloxidase and antimicrobial activity in the mealworm beetle Tenebrio molitor in response to a number of different synthetic and real immune elicitors. We found that antimicrobial activity in haemolymph increased rapidly during the first 48h after a challenge and was maintained at high levels for at least 14 days. There was no difference in the magnitude of responses …

MealwormProphenoloxidaseTime FactorsPhysiology[ SDV.BA.ZI ] Life Sciences [q-bio]/Animal biology/Invertebrate ZoologyAntimicrobial peptidesBacillus subtilisMicrobiologyImmune systemDownregulation and upregulationHemolymphHemolymphEscherichia coliAnimals[ SDV.IMM ] Life Sciences [q-bio]/ImmunologyTenebrioEnzyme PrecursorsbiologyMonophenol MonooxygenaseZone of inhibitionLong-lasting immunityProphenoloxidaseAntimicrobialbiology.organism_classificationHaemolymphInsect ScienceHost-Pathogen InteractionsInsect immunityPhenoloxidaseAntimicrobial peptidesCatechol OxidaseAntimicrobial Cationic PeptidesBacillus subtilis
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Synthesis and analysis of activity of a potential anti-melanoma prodrug with a hydrazine linker

2013

A potential anti-melanoma prodrug containing a phenolic activator, a hydrazine linker, and a nitrogen mustard effector - (N-{4-[bis-(2-chloroethyl)amino]benzoyl}-N'-(4-hydroxybenzyl)hydrazine) has been synthesized in seven steps. Spectrophotometric measurements of its oxidation by tyrosinase showed a rapid increase of absorbance at 337 nm. HPLC analysis demonstrated that two major products were formed. However, during the reaction one of the products was converted into the other. The stable product with a maximum of absorption at 337 nm was isolated and identified as 5,6-dihydroxy-1H-indazol-1-yl 4-[bis-(2-chloroethyl)amino]benzoate. It was formed by a cyclization of the enzymatically gener…

MelphalanStereochemistryTyrosinaseHydrazineMelanoma Experimentaltyrosinasechemistry.chemical_compoundMiceNucleophileCell Line TumorDrug DiscoverymedicineAnimalsProdrugsMechlorethamineTyrosineneoplasmsPharmacologyanti-melanoma prodrugChemistryMonophenol MonooxygenaseOrganic Chemistrynitrogen mustardhydrazineGeneral MedicineProdrugNitrogen mustardHydrazinesCyclizationLinkermedicine.drugEuropean Journal of Medicinal Chemistry
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Oxygen as a morphogenic factor in sponges: expression of a tyrosinase gene in the sponge Suberites domuncula

2004

Sponges live in a symbiotic relationship with microorganisms, especially bacteria. Here we show, using the demosponge Suberites domuncula as a model, that the sponge expresses the enzyme tyrosinase which synthesizes diphenols from monophenolic compounds. It is assumed that these products serve as carbon source for symbiotic bacteria to grow.

MicroorganismTyrosinaseMolecular Sequence DataGeneral Physics and AstronomyMicrobiologyDemospongeStructural BiologyAnimalsHumansGeneral Materials ScienceAmino Acid SequenceSymbiosisPhylogenychemistry.chemical_classificationbiologyMonophenol MonooxygenaseCell Biologybiology.organism_classificationPoriferaOxygenSuberites domunculaSpongeEnzymechemistryBiochemistrySequence AlignmentBacteriaSymbiotic bacteriaMicron
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Similar enzyme activation and catalysis in hemocyanins and tyrosinases

2006

This review presents the common features and differences of the type 3 copper proteins with respect to their structure and function. In spite of these differences a common mechanism of activation and catalysis seems to have been preserved throughout evolution. In all cases the inactive proenzymes such as tyrosinase and catecholoxidase are activated by removal of an amino acid blocking the entrance channel to the active site. No other modification at the active site seems to be necessary to enable catalytic activity. Hemocyanins, the oxygen carriers in many invertebrates, also behave as silent inactive enzymes and can be activated in the same way. The molecular basis of the catalytic process…

Models MolecularCopper proteinmedicine.medical_treatmentTyrosinaseCatalysisEnzyme activatorProtein structureGeneticsmedicineAnimalsHumanschemistry.chemical_classificationbiologyMonophenol MonooxygenaseActive siteHemocyaninGeneral MedicineProtein Structure TertiaryAmino acidEnzyme ActivationOxygenEnzymeBiochemistrychemistryHemocyaninsbiology.proteinProtein BindingGene
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Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins

2003

Models MolecularInnate immune systemMonophenol MonooxygenaseTyrosinasemedicine.medical_treatmentImmunologyAntimicrobial peptidesHemocyaninBiologyAntimicrobialMicrobiologyAnti-Infective AgentsBiochemistryHemocyaninsMetalloproteinsmedicineAnimalsArthropodsDevelopmental BiologyDevelopmental & Comparative Immunology
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Homology modelling of hemocyanins and tyrosinases: pitfalls in automated approaches.

2004

Models MolecularMonophenol Monooxygenasemedicine.medical_treatmentGeneral Physics and AstronomyHemocyaninCell BiologyComputational biologyAstacoideaBiologyBioinformaticsStructural BiologyHemocyaninsmedicineAnimalsGeneral Materials ScienceHomology (anthropology)Micron (Oxford, England : 1993)
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Structural Mechanism of SDS-Induced Enzyme Activity of Scorpion Hemocyanin Revealed by Electron Cryomicroscopy

2009

Summary Phenoloxidases (POs) occur in all organisms and are involved in skin and hair coloring in mammals, and initiating melanization in wound healing. Mutation or overexpression of PO can cause albinism or melanoma, respectively. SDS can convert inactive PO and the oxygen carrier hemocyanin (Hc) into enzymatically active PO. Here we present single-particle cryo-EM maps at subnanometer resolution and pseudoatomic models of the 24-oligomeric Hc from scorpion Pandinus imperator in resting and SDS-activated states. Our structural analyses led to a plausible mechanism of Hc enzyme PO activation: upon SDS activation, the intrinsically flexible Hc domain I twists away from domains II and III in …

Models MolecularPROTEINSCopper proteinProtein Conformationmedicine.medical_treatmentProtein subunitArticleScorpions03 medical and health sciencesEnzyme activatorSurface-Active AgentsProtein structureStructural BiologyCatalytic DomainmedicineAnimalsBinding siteMolecular Biology030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMonophenol Monooxygenase030302 biochemistry & molecular biologyCryoelectron MicroscopyActive siteSodium Dodecyl SulfateHemocyaninEnzyme ActivationProtein SubunitsBiochemistryHemocyaninsbiology.proteinOxygen bindingStructure
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