Search results for "Apoproteins"

showing 10 items of 13 documents

Cytosolic calcium rises and related events in ergosterol-treated Nicotiana cells

2011

International audience; The typical fungal membrane component ergosterol was previously shown to trigger defence responses and protect plants against pathogens. Most of the elicitors mobilize the second messenger calcium, to trigger plant defences. We checked the involvement of calcium in response to ergosterol using Nicotiana plumbaginifolia and Nicotiana tabacum cv Xanthi cells expressing apoaequorin in the cytosol. First, it was verified if ergosterol was efficient in these cells inducing modifications of proton fluxes and increased expression of defence-related genes. Then, it was shown that ergosterol induced a rapid and transient biphasic increase of free [Ca2þ]cyt which intensity dep…

0106 biological sciencesTime FactorsPhysiologyNicotiana tabacumPlant SciencesterolsSecond Messenger Systemstobacco01 natural scienceschemistry.chemical_compoundCytosolpolycyclic compoundsPhosphorylationCalcium signalingreactive oxygen species0303 health sciencesErgosterolelicitorbiologyergosterolHydrogen-Ion ConcentrationPlants Genetically ModifiedRecombinant ProteinsCell biologyBiochemistrySecond messenger systemReactive oxygen species; Calcium signature; Elicitor; Signal transduction; MAPKs; tobaccolipids (amino acids peptides and proteins)Protonssignal transductionCell Survivalnicotiana plumbaginifoliachemistry.chemical_elementnicotiana tabacumoxydantCalciumcalcium signature03 medical and health sciencesAequorinMAPKsBAPTAGenetics[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCalcium Signaling030304 developmental biologyMitogen-Activated Protein Kinase KinasesCalcium metabolismHydrogen Peroxidebiochemical phenomena metabolism and nutritionbiology.organism_classificationCytosolchemistryCalciumApoproteins010606 plant biology & botany
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Iron-loaded transferrin (Tf) is detrimental whereas iron-free Tf confers protection against brain ischemia by modifying blood Tf saturation and subse…

2018

Despite transferrin being the main circulating carrier of iron in body fluids, and iron overload conditions being known to worsen stroke outcome through reactive oxygen species (ROS)-induced damage, the contribution of blood transferrin saturation (TSAT) to stroke brain damage is unknown. The objective of this study was to obtain evidence on whether TSAT determines the impact of experimental ischemic stroke on brain damage and whether iron-free transferrin (apotransferrin, ATf)-induced reduction of TSAT is neuroprotective. We found that experimental ischemic stroke promoted an early extravasation of circulating iron-loaded transferrin (holotransferrin, HTf) to the ischemic brain parenchyma.…

0301 basic medicineU-PAGE urea-polyacrylamide gel electrophoresisMaleClinical BiochemistryExperimental strokeBiochemistryBrain IschemiaBrain ischemia0302 clinical medicineADC apparent diffusion coefficientApotransferrinDWI diffusion-weighted imagingTANDEM-1 Thrombolysis and Deferoxamine in Middle Cerebral Artery Occlusion clinical trialrHTf rat HTfrATf rat ATflcsh:QH301-705.5chemistry.chemical_classificationNeuronslcsh:R5-920ChemistryTransferrinExtravasationNS21 a medium supplement to grow neuronspDAPK-1 phosphorylated anti-death-associated protein kinase 1NeuroprotectionStrokeWB Western blotFemalemedicine.symptomlcsh:Medicine (General)Research PaperhHTf human HTfPC12 cell line derived from a pheochromocytoma of the rat adrenal medullamedicine.medical_specialtyIron OverloadBBB blood-brain barrierNMDAR N-methyl-D-aspartate receptorDCF dihydrofluoresceinIronWGA wheat germ agglutininHTf holotransferrinTransferrin receptorBrain damageTfR transferrin receptorDeferoxamineNeuroprotectionPI propidium iodide03 medical and health sciencesBrain damageCM conditioned mediumROS reactive oxygen speciesInternal medicine4-HNE 4-hydroxynonenalTf transferrinReceptors TransferrinmedicineFeRhoNoxTM-1 probe to detect Fe2+AnimalsHumansATf apotransferrinCM-H2DCFDA 5-chloromethyl-27-dichlorodihydrofluorescein diacetateMCAO middle cerebral artery occlusionDMT-1 divalent metal transporterB-27 a medium supplement to grow neuronsReactive oxygen speciesNMDA N-methyl-D-aspartateTSAT blood transferrin saturationTransferrin saturationBlood transferrin saturation (TSAT)Organic ChemistryNIR near infraredReactive oxygen species (ROS)medicine.diseasepMCAO permanent middle cerebral artery occlusionRatsPWI perfusion-weighted imaging030104 developmental biologyEndocrinologylcsh:Biology (General)TransferrinDAPK-1 anti-death-associated protein kinaseOGD oxygen/glucose deprivationTTC 235-triphenyl-tetrazolium chlorideLipid PeroxidationMCA middle cerebral arteryApoproteinsReactive Oxygen SpeciesMRI magnetic resonance imagingtMCAO transient middle cerebral artery occlusion030217 neurology & neurosurgeryhATf human ATf
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Carotenoid binding sites in LHCIIb

2000

The major light-harvesting complex of photosystem II can be reconstituted in vitro from its bacterially expressed apoprotein with chlorophylls a and b and neoxanthin, violaxanthin, lutein, or zeaxanthin as the only xanthophyll. Reconstitution of these one-carotenoid complexes requires low-stringency conditions during complex formation and isolation. Neoxanthin complexes (containing 30–50% of the all-trans isomer) disintegrate during electrophoresis, exhibit a largely reduced resistance against proteolytic attack; in addition, energy transfer from Chl b to Chl a is easily disrupted at elevated temperature. Complexes reconstituted in the presence of either zeaxanthin or lutein contain nearly …

ChlorophyllLuteinPhotosynthetic Reaction Center Complex ProteinsPigment bindingLight-Harvesting Protein ComplexesXanthophyllsBiologyBinding CompetitiveBiochemistrySubstrate SpecificityLight-harvesting complexchemistry.chemical_compoundNeoxanthinZeaxanthinsTrypsinProtein PrecursorsCarotenoidPlant Proteinschemistry.chemical_classificationBinding SitesChlorophyll ALuteinPhotosystem II Protein Complexfood and beveragesPigments BiologicalPlantsbeta CaroteneCarotenoidseye diseasesZeaxanthinEnergy TransferchemistryBiochemistryXanthophyllElectrophoresis Polyacrylamide GelApoproteinsViolaxanthinEuropean Journal of Biochemistry
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De-epoxidation of Violaxanthin in Light-harvesting Complex I Proteins

2004

The conversion of violaxanthin (Vx) to zeaxanthin (Zx) in the de-epoxidation reaction of the xanthophyll cycle plays an important role in the protection of chloroplasts against photooxidative damage. Vx is bound to the antenna proteins of both photosystems. In photosystem II, the formation of Zx is essential for the pH-dependent dissipation of excess light energy as heat. The function of Zx in photosystem I is still unclear. In this work we investigated the de-epoxidation characteristics of light-harvesting complex proteins of photosystem I (LHCI) under in vivo and in vitro conditions. Recombinant LHCI (Lhcal-4) proteins were reconstituted with Vx and lutein, and the convertibility of Vx wa…

ChlorophyllLuteinPhotosystem IIPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesXanthophyllsPhotosystem IThylakoidsBiochemistrychemistry.chemical_compoundSolanum lycopersicumSpinacia oleraceaEscherichia coliMolecular BiologyPhotosystemchemistry.chemical_classificationBinding SitesPhotosystem I Protein ComplexChemistryfood and beveragesPigments BiologicalCell Biologybeta CaroteneRecombinant ProteinsChloroplastKineticsBiochemistryXanthophyllThylakoidEpoxy CompoundsApoproteinsViolaxanthinJournal of Biological Chemistry
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Water-Soluble Chlorophyll Protein (WSCP) Stably Binds Two or Four Chlorophylls

2017

Water-soluble chlorophyll proteins (WSCPs) of class IIa from Brassicaceae form tetrameric complexes containing one chlorophyll (Chl) per apoprotein but no carotenoids. The complexes are remarkably stable toward dissociation and protein denaturation even at 100 °C and extreme pH values, and the Chls are partially protected against photooxidation. There are several hypotheses that explain the biological role of WSCPs, one of them proposing that they function as a scavenger of Chls set free upon plant senescence or pathogen attack. The biochemical properties of WSCP described in this paper are consistent with the protein acting as an efficient and flexible Chl scavenger. At limiting Chl concen…

ChlorophyllModels Molecular0106 biological sciences0301 basic medicineProtein DenaturationHot TemperatureLightLight-Harvesting Protein ComplexesGene ExpressionThylakoids01 natural sciencesBiochemistryProtein Structure SecondaryDissociation (chemistry)law.inventionchemistry.chemical_compoundlawpolycyclic compoundsDenaturation (biochemistry)CarotenoidPlant Proteinschemistry.chemical_classificationSinglet OxygenProtein Stabilityfood and beveragesHydrogen-Ion ConcentrationBiochemistryRecombinant DNAOxidation-ReductionProtein BindingRecombinant Fusion ProteinsBrassicamacromolecular substancesBiology03 medical and health sciencesProtein DomainsTetramerPlant senescenceChlorophyll APeasWaterOxygen030104 developmental biologyWater solubleSolubilitychemistryChlorophyllProtein MultimerizationApoproteins010606 plant biology & botanyBiochemistry
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Early folding events during light harvesting complex II assembly in vitro monitored by pulsed electron paramagnetic resonance

2016

Efficient energy transfer in the major light harvesting complex II (LHCII) of green plants is facilitated by the precise alignment of pigments due to the protein matrix they are bound to. Much is known about the import of the LHCII apoprotein into the chloroplast via the TOC/TIC system and its targeting to the thylakoid membrane but information is sparse about when and where the pigments are bound and how this is coordinated with protein folding. In vitro, the LHCII apoprotein spontaneously folds and binds its pigments if the detergent-solubilized protein is combined with a mixture of chlorophylls a and b and carotenoids. In the present work, we employed this approach to study apoprotein fo…

ChlorophyllModels Molecular0301 basic medicineProtein FoldingPigment bindingLight-Harvesting Protein ComplexesBiophysicsBiochemistrylaw.invention03 medical and health scienceslawElectron paramagnetic resonancePlant ProteinsPulsed EPRChemistryElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyProtein tertiary structureProtein Structure TertiaryChloroplastFolding (chemistry)KineticsCrystallography030104 developmental biologyEnergy TransferThylakoidProtein foldingApoproteinsProtein BindingBiochimica et Biophysica Acta (BBA) - Bioenergetics
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The Light-Harvesting Chlorophyll a/b Complex Can Be Reconstituted in Vitro from Its Completely Unfolded Apoprotein

2003

The major light-harvesting chlorophyll a/b protein (LHCIIb) of higher plants is one of the few membrane proteins that can be refolded in vitro. During folding, the apoprotein is assembled with pigments to form a structurally authentic and functional pigment--protein complex. All reconstitution procedures used so far include solubilization of the apoprotein in sodium dodecyl sulfate (SDS) where the protein adopts approximately half of its alpha-helical folding present in the native structure. This paper shows that this preformed alpha-helix is not a prerequisite for LHCIIb folding in vitro. The apoprotein can also be reconstituted starting from a solution in guanidinium hydrochloride (Gnd) w…

ChlorophyllProtein FoldingChlorophyll ACircular DichroismPhotosynthetic Reaction Center Complex ProteinsKineticsLight-Harvesting Protein Complexesfood and beveragesBiochemistryFluorescenceIn vitroFolding (chemistry)B vitaminschemistry.chemical_compoundPigmentSpectrometry FluorescenceBiochemistrychemistryMembrane proteinvisual_artvisual_art.visual_art_mediumSodium dodecyl sulfateApoproteinsBiochemistry
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Potential use of 68Ga-apo-transferrin as a PET imaging agent for detecting Staphylococcus aureus infection.

2010

Abstract Introduction 67 Ga citrate has been extensively used to detect infection and inflammation since 1971. However, its clinical utility is compromised due to several limitations. The present project explored whether 68 Ga- apo -transferrin ( 68 Ga-TF), when prepared in vitro, is a useful agent for positron emission tomography (PET) imaging of bacterial infection. Methods An infection was induced in male Wistar rats by injecting 5×10 5 CFU units of Staphyococcus aureus in the right thigh muscle. 68 Ga-TF was synthesized by mixing 68 GaCl 3 with apo -transferrin (TF, 2 mg) in sodium carbonate (0.1 M, pH 7.0) and incubating at 40°C for 1 h. Animals were injected with 10–15 MBq of 68 Ga-TF…

MaleCancer ResearchPathologymedicine.medical_specialtyBiodistributionStaphylococcus aureusMicrococcaceaeInflammationGalliumGallium RadioisotopesPharmacologyStaphylococcal infectionsmedicine.disease_causeLesionmedicineAnimalsRadiology Nuclear Medicine and imagingRats WistarProteus mirabilischemistry.chemical_classificationbiologybusiness.industryTransferrinStaphylococcal Infectionsbiology.organism_classificationmedicine.diseaseIn vitroRatschemistryStaphylococcus aureusTransferrinPositron-Emission TomographyMolecular Medicinemedicine.symptombusinessApoproteinsProteus InfectionsNuclear medicine and biology
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A novel haemoprotein induced by isosafrole pretreatment in the rat

1978

Abstract Sodium dodecyl sulphate-polyacrylamide gel electrophoresis has been used to demonstrate that pretreatment of rats with isosafrole results in the formation of a novel species of cytochrome P-450 (mol. wt. 54,000) quite distinct from that induced by phenobarbitone pretreatment (mol. wt. 50,000) or 3-methylcholanthrene (mol. wt. 58,000).

MaleHemeproteinCytochromeSodiumBiophysicschemistry.chemical_elementDioxolesBiochemistrychemistry.chemical_compoundCytochrome P-450 Enzyme SystemIsomerismSafroleMoleAnimalsMolecular BiologyGel electrophoresisChromatographybiologyChemistrySpectrum AnalysisCell BiologyRatsMolecular WeightBiochemistryIsosafroleEnzyme InductionPhenobarbitalMicrosomes Liverbiology.proteinApoproteinsMethylcholanthreneBiochemical and Biophysical Research Communications
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The mitochondrial genome of fission yeast: inability of all introns to splice autocatalytically, and construction and characterization of an intronle…

1991

In this paper we report the inability of four group I introns in the gene encoding subunit I of cytochrome c oxidase (cox1) and the group II intron in the apocytochrome b gene (cob) to splice autocatalytically. Furthermore we present the characterization of the first cox1 intron in the mutator strain anar-14 and the construction and characterization of strains with intronless mitochondrial genomes. We provide evidence that removal of introns at the DNA level (termed DNA splicing) is dependent on an active RNA maturase. Finally we demonstrate that the absence of introns does not abolish homologous mitochondrial recombination.

Mitochondrial DNARNA MitochondrialRNA SplicingMolecular Sequence DataBiologyDNA MitochondrialGenomeElectron Transport Complex IVConsensus SequenceSchizosaccharomycesGeneticsGroup I catalytic intronAmino Acid SequenceCloning MolecularMolecular BiologyGeneGeneticsBase SequenceIntronRNAGroup II intronCytochromes bCytochrome b GroupIntronsMitochondriaRNA splicingNucleic Acid ConformationRNAApoproteinsMolecular and General Genetics MGG
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