Search results for " Lipid"

showing 10 items of 481 documents

Eight-week consumption of milk enriched with omega 3 fatty acids raises their blood concentrations yet does not affect lipids and cardiovascular dise…

2014

Adequate concentrations of omega 3 fatty acids (FA) may be maintained by consuming foods naturally rich in or functional foods enriched with those essential FA. We assessed the effects of an 8-week consumption of milk enriched with 400. mg of omega 3 FA on blood lipid levels and selected cardiovascular risk factors in adult healthy volunteers. Participants (n= 157) were randomized to consume - for eight weeks - either 500. mL/day of 1% fat milk providing 150. mg of eicosapentaenoic (EPA), 150. mg of docosahexaenoic (DHA), and 100. mg of α-linolenic (ALA) acids or 500. mL/day of non-enriched 1% fat milk. At week 8, we observed significant increments of blood EPA and DHA in the intervention g…

PharmacologyEicosapentaenoic acidmedicine.diagnostic_testHomocysteineBlood lipidsPhysiologyMilk enriched with fish oilBiologyEicosapentaenoic acidLeukotriene B4Thromboxane B2Thromboxane B2chemistry.chemical_compoundDocosahexaenoic acidchemistryDocosahexaenoic acidHealthy volunteersmedicineDisease riskOmega 3 fatty acidPharmacology (medical)Food scienceLipid profileDocosahexaenoic acid; Eicosapentaenoic acid; Leukotriene B4; Milk enriched with fish oil; Omega 3 fatty acids; Thromboxane B2; Pharmacology; Pharmacology (medical); Food ScienceFood Science
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Clinical benefits of ezetimibe use: is absence of proof, proof of absence?

2012

Doggrell reviewed the evidence regarding the clinical benefits of ezetimibe in the July issue of Expert Opinion on Pharmacotherapy [1]. The author concludes that since clinical outcome data are sti...

Pharmacologymedicine.medical_specialtybusiness.industryMEDLINEGeneral Medicinecardiovascular risk ezetimibe lipids therapyPharmacotherapyEzetimibeExpert opinionMedicinePharmacology (medical)Outcome databusinessIntensive care medicinemedicine.drug
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Cold exposure enhances fat utilization but not non-esterified fatty acids, glycerol or catecholamines availability during submaximal walking and runn…

2013

Cold exposure modulates the use of carbohydrates and fat during exercise. This phenomenon has mostly been observed in controlled cycling studies, but not during walking and running when core temperature and oxygen consumption are controlled, as both may alter energy metabolism. This study aimed at examining energy substrate availability and utilization during walking and running in the cold when core temperature and oxygen consumption are maintained. Ten lightly clothed male subjects walked or ran for 60-min, at 50% and 70% of maximal oxygen consumption, respectively, in a climatic chamber set at 0°C or 22°C. Thermal, cardiovascular, and oxidative responses were measured every 15-…

Physiologykylmäaltistuscold exposurerasvahapotchemistry.chemical_elementBlood lipidsOxidative phosphorylationglycerol030204 cardiovascular system & hematologyBiologyOxygenthermal responseslcsh:Physiologyrasva-aineenvaihdunta03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAnimal sciencePhysiology (medical)fatHeart rateGlycerolglyseroliOriginal Research Articleta315Exerciselcsh:QP1-981kuormauskuormitusfat metabolismVO2 max030229 sport sciencesRespiratory quotientGlucosechemistryBiochemistrykatakolamiinitEnergy sourceEnergy Metabolismkatekoliamiinit
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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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Enhanced in vivo targeting of murine nonparenchymal liver cells with monophosphoryl lipid A functionalized microcapsules.

2014

A broad spectrum of infectious liver diseases emphasizes the need of microparticles for targeted delivery of immunomodulatory substances to the liver. Microcapsules (MCs) are particularly attractive for innovative drug and vaccine formulations, enabling the combination of antigen, drugs, and adjuvants. The present study aimed to develop microcapsules characterized by an enhanced liver deposition and accelerated uptake by nonparenchymal liver cells (NPCs). Initially, two formulations of biodegradable microcapsules were synthesized from either hydroxyethyl starch (HES) or mannose. Notably, HES-MCs accumulated primarily in the liver, while mannose particles displayed a lung preference. Functio…

Polymers and PlasticsLiver cytologyKupffer CellsMonophosphoryl Lipid AMannoseBioengineeringCapsulesReceptors Cell SurfacePharmacologyBiomaterialsMinor Histocompatibility Antigenschemistry.chemical_compoundInterferon-gammaMiceImmune systemDrug Delivery SystemsAntigenPhagocytosisIn vivoAntigens CDMaterials ChemistryAnimalsSecretionLectins C-TypeCD40 AntigensInterleukin-6Tumor Necrosis Factor-alphaLiver DiseasesDendritic CellsIn vitroMice Inbred C57BLToll-Like Receptor 4Lipid AchemistryBiochemistryLiverNanoparticlesFemaleBiomacromolecules
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A lipocentric view of peptide-induced pores

2010

Although lipid membranes serve as effective sealing barriers for the passage of most polar solutes, nonmediated leakage is not completely improbable. A high activation energy normally keeps unassisted bilayer permeation at a very low frequency, but lipids are able to self-organize as pores even in peptide-free and protein-free membranes. The probability of leakage phenomena increases under conditions such as phase coexistence, external stress or perturbation associated to binding of nonlipidic molecules. Here, we argue that pore formation can be viewed as an intrinsic property of lipid bilayers, with strong similarities in the structure and mechanism between pores formed with participation …

Pore Forming Cytotoxic ProteinsCell Membrane PermeabilityMembrane permeabilityMembrane lipidsPore energeticsBiophysicsThermal fluctuationsReviewMolecular Dynamics SimulationSurface tensionMembrane LipidsAnti-Infective AgentsLipid bilayerChemistryBilayerLipidic poreGeneral MedicinePermeationCrystallographyMembrane permeabilityMembraneBiophysicsAntimicrobial peptidePore structurePorosityPore-forming proteinsEuropean Biophysics Journal
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Correct oligomerization is a prerequisite for insertion of the central molecular domain of staphylococcal α-toxin into the lipid bilayer

1995

Staphylococcal alpha-toxin is a primarily hydrophilic molecule that binds as a monomer to target membranes and then aggregates to form amphiphilic oligomers that represent water-filled transmembrane channels. Current evidence indicates that a region located in the center of the molecule inserts deeply into the bilayer. In the present study, we sought to determine whether membrane insertion was triggered by the oligomerization process, and whether insertion correlated with pore formation. Double mutants of alpha-toxin were prepared in which His-35 was replaced by Arg, and cysteine residues were introduced at positions 69, 130 and 186. Substitution of His-35 with Arg rendered the toxin molecu…

Pore formationBacterial ToxinsLipid BilayersMolecular ConformationBiophysics(Staphylococcus)Arginineα-ToxinBiochemistryHemolysin ProteinsMembrane Lipidschemistry.chemical_compound2-NaphthylamineAmphiphileOligomerizationCysteineLipid bilayerFluorescent DyesTransmembrane channelsPore-forming toxinBilayerCell BiologyMembraneMonomerchemistryBiochemistryMutationPore-forming toxinBiophysicsMembrane insertionCysteineBiochimica et Biophysica Acta (BBA) - Biomembranes
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The membrane environment modulates self-association of the human GpA TM domain--implications for membrane protein folding and transmembrane signaling.

2010

Abstract The influence of lipid bilayer properties on a defined and sequence-specific transmembrane helix–helix interaction is not well characterized yet. To study the potential impact of changing bilayer properties on a sequence-specific transmembrane helix–helix interaction, we have traced the association of fluorescent-labeled glycophorin A transmembrane peptides by fluorescence spectroscopy in model membranes with varying lipid compositions. The observed changes of the glycophorin A dimerization propensities in different lipid bilayers suggest that the lipid bilayer thickness severely influences the monomer–dimer equilibrium of this transmembrane domain, and dimerization was most effici…

Protein FoldingLipid BilayersMolecular Sequence DataBiophysicsGpABiochemistryFluorescenceMembrane LipidsOrientations of Proteins in Membranes databaseMembrane fluidityFluorescence Resonance Energy TransferHumansAmino Acid SequenceGlycophorinsBilayerLipid bilayerIntegral membrane proteinBinding SitesChemistryBilayerPeripheral membrane proteinTemperatureMembrane ProteinsCell BiologyTransmembrane proteinCell biologyTransmembrane domainCholesterolSpectrometry FluorescenceFRETPhosphatidylcholineslipids (amino acids peptides and proteins)Transmembrane helix–helix interactionProtein MultimerizationPeptidesHydrophobic and Hydrophilic InteractionsSignal TransductionBiochimica et biophysica acta
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