Search results for "LIPID TRANSFER PROTEIN"

showing 10 items of 33 documents

Specific adduction of plant lipid transfer protein by an allene oxide generated by 9-lipoxygenase and allene oxide synthase

2006

International audience; Lipid transfer proteins (LTPs) are ubiquitous plant lipid-binding proteins that have been associated with multiple developmental and stress responses. Although LTPs typically bind fatty acids and fatty acid derivatives in a non-covalent way, studies on the LTPs of barley seeds have identified an abundantly occurring covalently modified form, LTP1b, the lipid ligand of which has resisted clarification. In the present study, this adduct was identified as the {alpha}-ketol 9-hydroxy-10-oxo-12(Z)-octadecenoic acid. Further studies on the formation of LTP1b demonstrated that the ligand was introduced by nucleophilic attack of the free carboxylate group of the Asp-7 residu…

Models Molecular0106 biological sciencesMagnetic Resonance SpectroscopyTime FactorsLIPID TRANSFER PROTEINAlleneLipoxygenaseLigands01 natural sciencesBiochemistrySubstrate SpecificityMiceLipoxygenasechemistry.chemical_compoundJasmonate2. Zero hungerchemistry.chemical_classificationALLENE OXIDE SYNTHASEMice Inbred BALB C0303 health sciencesbiologyfood and beveragesLIPID TRANSFER PROTEIN;LTP;ALLENE OXIDE SYNTHASE;PROTEINE DE TRANSFERT DE LIPIDE;REPONSE DE LA PLANTEIntramolecular OxidoreductasessynthaseBiochemistryprotéineLTPPlant lipid transfer proteinsLinoleic acidGas Chromatography-Mass Spectrometry03 medical and health sciencesprotéine végétaleréaction de défenseBiosynthesisAnimals[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular Biologymécanisme de défense030304 developmental biologyHybridomasFatty acidHordeumCell BiologyOxylipinenzymeoxylipineModels Chemicalchemistrybiology.proteinREPONSE DE LA PLANTEPROTEINE DE TRANSFERT DE LIPIDECarrier Proteins010606 plant biology & botany
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A lipid transfer protein binds to a receptor involved in the control of plant defence responses

2001

AbstractLipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.

Models Molecular0106 biological sciencesTime FactorsProtein ConformationPlasma protein bindingLigands01 natural sciencesBiochemistryProtein structureStructural BiologyReceptorAllosteryTriticumComputingMilieux_MISCELLANEOUSPlant Proteins0303 health sciencesFungal proteinfood and beveragesCell biologyBiochemistryPlant lipid transfer proteinsAllosteric SiteProtein BindingReceptorPhytophthoraLipid transfer proteinAllosteric regulationBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding CompetitiveFungal Proteins03 medical and health sciencesTobaccoGeneticsBinding site[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesDose-Response Relationship DrugAlgal ProteinsCell MembraneElicitinCell BiologyAntigens PlantModels TheoreticalLipid MetabolismElicitinCarrier Proteins010606 plant biology & botanyFEBS Letters
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Multiple IgE recognition on the major allergen of the Parietaria pollen Par j 2

2015

The interaction between IgE antibodies and allergens is a key event in triggering an allergic reaction. The characterization of this region provides information of paramount importance for diagnosis and therapy. Par j 2 Lipid Transfer Protein is one of the most important allergens in southern Europe and a well-established marker of sensitization in Parietaria pollen allergy. The main aim of this study was to map the IgE binding regions of this allergen and to study the pattern of reactivity of individual Parietaria-allergic patients. By means of gene fragmentation, six overlapping peptides were expressed in Escherichia coli, and their IgE binding activity was evaluated by immunoblotting in …

Models MolecularParietariaAdolescentBlotting WesternImmunoblottingMolecular Sequence DataEpitope mappingImmunologyProtein domainImmunoglobulin Emedicine.disease_causeEpitopelaw.inventionEpitopesAllergenlawmedicineHumansComputer SimulationAmino Acid SequenceCloning MolecularChildParietaria IgE Epitope mapping Molecular biology.Molecular BiologybiologyRhinitis Allergic SeasonalAllergensImmunoglobulin Ebiology.organism_classificationRecombinant ProteinsParietariaEpitope mappingImmunologybiology.proteinRecombinant DNAPollenElectrophoresis Polyacrylamide GelIgEPlant lipid transfer proteinsMolecular Immunology
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Fatty acids bind to the fungal elicitor cryptogein and compete with sterols

2001

Abstract Cryptogein is a proteinaceous elicitor of plant defense reactions which also exhibits sterol carrier properties. In this study, we report that this protein binds fatty acids. The stoichiometry of the fatty acid–cryptogein complex is 1:1. Linoleic acid and dehydroergosterol compete for the same site, but elicitin affinity is 27 times lower for fatty acid than for sterol. We show that C7 to C12 saturated and C16 to C22 unsaturated fatty acids are the best ligands. The presence of double bonds markedly increases the affinity of cryptogein for fatty acids. A comparison between elicitins and known lipid transfer proteins is discussed.

Phytophthora0106 biological sciencesDouble bondLinoleic acidBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding Competitive01 natural sciencesBiochemistryFungal ProteinsLinoleic AcidLIAISON MOLECULAIREStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundStructural BiologyErgosterolGeneticsPlant defense against herbivoryMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSSterol030304 developmental biologychemistry.chemical_classification0303 health sciencesAlgal ProteinsFatty AcidsProteinsFatty acidLipid–protein interactionElicitinCell BiologyFatty acidElicitinSterol3. Good healthElicitorSterolschemistryBiochemistrylipids (amino acids peptides and proteins)Plant lipid transfer proteinsProtein Binding010606 plant biology & botany
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Are elicitins cryptograms in plant-oomycete communications?

1999

Stimulation of plant natural defenses is an important challenge in phytoprotection prospects. In that context, elicitins, which are small proteins secreted by Phytophthora and Pythium species, have been shown to induce a hypersensitive-like reaction in tobacco plants. Moreover, these plants become resistant to their pathogens, and thus this interaction constitutes an excellent model to investigate the signaling pathways leading to plant resistance. However, most plants are not reactive to elicitins, although they possess the functional signaling pathways involved in tobacco responses to elicitin. The understanding of factors involved in this reactivity is needed to develop agronomic applica…

Phytophthora0106 biological sciences[SDV]Life Sciences [q-bio]Molecular Sequence DataMutagenesis (molecular biology technique)Context (language use)01 natural sciencesHost-Parasite InteractionsEvolution MolecularFungal Proteins03 medical and health sciencesCellular and Molecular NeuroscienceErgosterolGene Expression Regulation FungalTobaccoPlant defense against herbivoryAmino Acid SequenceMolecular BiologyPhylogenyComputingMilieux_MISCELLANEOUSPlant Diseases030304 developmental biologyPharmacologyOomycete0303 health sciencesBase SequencebiologyAlgal Proteinsfungifood and beveragesElicitinCell Biologybiology.organism_classification[SDV] Life Sciences [q-bio]Plants ToxicOomycetesBiochemistryMolecular MedicinePhytophthoraSequence AlignmentPlant lipid transfer proteinsFunction (biology)BiotechnologySignal Transduction010606 plant biology & botany
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Modulation of the Biological Activity of a Tobacco LTP1 by Lipid Complexation

2004

Plant lipid transfer proteins (LTPs) are small, cysteine-rich proteins secreted into the extracellular space. They belong to the pathogenesis-related proteins (PR-14) family and are believed to be involved in several physiological processes including plant disease resistance, although their precise biological function is still unknown. Here, we show that a recombinant tobacco LTP1 is able to load fatty acids and jasmonic acid. This LTP1 binds to specific plasma membrane sites, previously characterized as elicitin receptors, and is shown to be involved in the activation of plant defense. The biological properties of this LTP1 were compared with those of LTP1-linolenic and LTP1-jasmonic acid…

Phytophthora0106 biological sciences[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringCyclopentanesPlasma protein bindingBiologyFatty Acid-Binding ProteinsLigands01 natural sciencesMass SpectrometryFatty acid-binding proteinCell membrane03 medical and health scienceschemistry.chemical_compoundTobacco[SDV.IDA]Life Sciences [q-bio]/Food engineeringExtracellularmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringOxylipinsMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesDose-Response Relationship DrugCircular DichroismJasmonic acidCell MembraneFatty AcidsElicitinBiological activityArticlesCell Biology[SDV.IDA] Life Sciences [q-bio]/Food engineeringLipid MetabolismLipidsRecombinant Proteinsmedicine.anatomical_structureBiochemistrychemistryPHYTOPHTORA PARASITICACarrier ProteinsTRANSFERT LIPIDIQUEPlant lipid transfer proteinsChromatography LiquidProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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Plasma Proteins, Yolk Proteins and Metal-Binding Proteins

1994

The extracellular fluid of the metazoans is not only a transport vehicle but also, for the majority of the body’s cells, their growth environment. Proteins play an important role here, providing colloid-osmotic pressure and acting as buffers. The most important parameter in this respect is their concentration which, depending upon the species, the developmental stage and the physiological conditions, can vary from less than 1 to more than 200 mg/ml (Table 5.1). In addition to these general functions, individual plasma proteins have various specific roles, e.g. in the transport of substances, in defence reactions, in blood clotting or in the solution of clots. At least in the case of the mor…

Retinol binding proteinMembrane proteinAntifreeze proteinChemistryExtracellular fluidExtracellularBiophysicsMetal binding proteinsPlant lipid transfer proteinsBlood proteins
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One precursor, three apolipoproteins: The relationship between two crustacean lipoproteins, the large discoidal lipoprotein and the high density lipo…

2014

The novel discoidal lipoprotein (dLp) recently detected in the crayfish, differs from other crustacean lipoproteins in its large size, apoprotein composition and high lipid binding capacity, We identified the dLp sequence by transcriptome analyses of the hepatopancreas and mass spectrometry. Further de novo assembly of the NGS data followed by BLAST searches using the sequence of the high density lipoprotein/1-glucan binding protein (HDL-BGBP) of Astacus leptodactylus as query revealed a putative precursor molecule with an open reading frame of 14.7 kb and a deduced primary structure of 4889 amino acids. The presence of an N-terminal lipid bind- ing domain and a DUF 1943 domain suggests the…

Sequence analysisLipoproteinsBlotting WesternMolecular Sequence DataHepatopancreasSequence alignmentBiologyMass SpectrometryProtein structureCrustaceaHemolymphLectinsAnimalsProtein IsoformsAmino Acid SequenceMolecular BiologyPeptide sequenceFurinBinding proteinProtein primary structureSequence Analysis DNACell BiologyImmunohistochemistryProtein Structure TertiaryApolipoproteinsBiochemistrybiology.proteinlipids (amino acids peptides and proteins)Carrier ProteinsLipoproteins HDLSequence AlignmentPlant lipid transfer proteinsBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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Binding, Interaction, and Organization of Proteins with Lipid Model Membranes

1991

Model membrane systems are used to investigate protein recognition and binding at interfaces. Fluorescence microscopy results are presented for interactions of the proteins, phospholipase A2 and antifluorescyl IgG, at lipid monolayer interfaces. Total internal reflection fluorescence measurements are used to quantify albumin and IgG adsorption to supported lipid monolayers.

Total internal reflection fluorescence microscopeOrientations of Proteins in Membranes databaseMembraneMembrane proteinChemistryMonolayerBiophysicsFluorescence microscopeBiological membranePlant lipid transfer proteins
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α-Tocopherol Modulates Phosphatidylserine Externalization in Erythrocytes

2006

Objective— The aim of the present study was to assess the effect of α-tocopherol, the main vitamin E isomer on phosphatidylserine (PS) exposure at the surface of circulating erythrocytes, and to determine consequences on erythrocyte properties. Methods and Results— In vitro α-tocopherol enrichment of isolated erythrocytes significantly decreased PS externalization as assessed by lower Annexin V-fluorescein isothiocyanate labeling. Plasma phospholipid transfer protein (PLTP) transfers vitamin E, and both α-and γ-tocopherol accumulated in circulating erythrocytes from PLTP-deficient homozygous (PLTP −/− ) mice as compared with wild-type mice. In agreement with in vitro studies, vitamin E–enr…

Vitaminmedicine.medical_specialtyErythrocytesWhole Blood Coagulation Timemedicine.medical_treatmentalpha-TocopherolPhospholipidCell SeparationPhosphatidylserinesBiologyFibrin Fibrinogen Degradation ProductsMicechemistry.chemical_compoundAnnexinIn vivoPhospholipid transfer proteinInternal medicinemedicineAnimalsTocopherolPhospholipid Transfer ProteinsBlood CoagulationMice KnockoutVitamin EErythrocyte MembraneHomozygotePhosphatidylserinePhenotypeEndocrinologychemistryBiochemistryCardiology and Cardiovascular MedicineOxidation-ReductionBiomarkersArteriosclerosis, Thrombosis, and Vascular Biology
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