Search results for "Erythrocyte membrane"

showing 10 items of 59 documents

Red blood cell plasmalogens and docosahexaenoic acid are independently reduced in primary open-angle glaucoma

2009

International audience; Among several theories involved in the pathogenesis of primary open-angle glaucoma (POAG), the vascular theory considers the disease to be a consequence of reduced ocular blood flow associated with red blood cell abnormalities. Red blood cell membrane structure and function are influenced by their phospholipid composition. We investigated whether specific lipid entities that may affect the membrane physiology, namely, polyunsaturated fatty acids (PUFAs) and plasmalogens, are modified in POAG and whether these potential variations are related to the stage of glaucoma. Blood samples were collected from 31 POAG patients and 10 healthy individuals. The stage of glaucoma …

Malegenetic structuresGlaucomaPathogenesischemistry.chemical_compound0302 clinical medicine[SDV.IDA]Life Sciences [q-bio]/Food engineeringETHER-LIPIDSERYTHROCITEchemistry.chemical_classificationAged 80 and over0303 health sciencesMiddle AgedSensory Systemsmedicine.anatomical_structureBiochemistryDocosahexaenoic acidDisease ProgressionFemalelipids (amino acids peptides and proteins)Glaucoma Open-AnglePolyunsaturated fatty acidmedicine.medical_specialtySpectrometry Mass Electrospray IonizationOpen angle glaucomaDocosahexaenoic AcidsPhospholipidBiology03 medical and health sciencesCellular and Molecular NeuroscienceInternal medicinemedicineHumans[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringPLASMALOGENSPRIMARY OPEN-ANGLE GLAUCOMA (POGA)030304 developmental biologyAgedErythrocyte MembraneBlood flowDOCOSAHEXAENOIC ACID (DHA)medicine.diseaseeye diseasesOphthalmologyRed blood cellEndocrinologychemistryCase-Control Studies030221 ophthalmology & optometrysense organsVisual FieldsChromatography Liquid
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A new heterozygous mutation (L338N) in the human Gsalpha (GNAS1) gene as a cause for congenital hypothyroidism in Albright's hereditary osteodystroph…

2003

OBJECTIVE: To identify the molecular defect by which psychomotor retardation is caused in two brothers with congenital hypothyroidism who received adequate treatment with l-thyroxine. CASE REPORT: A six-year-old boy presented with psychomotor retardation and congenital primary hypothyroidism (CH). The patient had a normal blood thyrotrophin (TSH) level on neonatal screening, but low total serum thyroxine and triiodothyronine concentrations prompting thyroid hormone substitution shortly after birth. Nevertheless, psychomotor development was retarded and the patient underwent further investigation. Typical features of Albright's hereditary osteodystrophy (AHO) such as round face, obesity, and…

Malemedicine.medical_specialtyHeterozygoteGenotypeEndocrinology Diabetes and MetabolismThyrotropinFibrous Dysplasia PolyostoticEndocrinologyHypothyroidismInternal medicinemedicineGTP-Binding Protein alpha Subunits GsHumansOsteodystrophyChildAlbright's hereditary osteodystrophyPseudohypoparathyroidismPsychomotor retardationbusiness.industryThyroidErythrocyte MembranePrimary hypothyroidismGeneral MedicineSequence Analysis DNAmedicine.diseaseCongenital hypothyroidismPedigreeThyroxineEndocrinologymedicine.anatomical_structureMutationTriiodothyroninePseudopseudohypoparathyroidismCalciummedicine.symptomMetacarpusPsychomotor DisordersbusinessEuropean journal of endocrinology
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The superlattice model of lateral organization of membranes and its implications on membrane lipid homeostasis.

2008

AbstractMost biological membranes are extremely complex structures consisting of hundreds of different lipid and protein molecules. According to the famous fluid-mosaic model lipids and many proteins are free to diffuse very rapidly in the plane of the membrane. While such fast diffusion implies that different membrane lipids would be laterally randomly distributed, accumulating evidence indicates that in model and natural membranes the lipid components tend to adopt regular (superlattice-like) distributions. The superlattice model, put forward based on such evidence, is intriguing because it predicts that 1) there is a limited number of allowed compositions representing local minima in mem…

Membrane FluidityMembrane lipidsBiophysicsDistributionMolecular dynamicsBiology010402 general chemistry01 natural sciencesBiochemistryModels BiologicalPolar membrane03 medical and health sciencesMembrane LipidsMembrane MicrodomainsMembrane fluidityAnimalsHomeostasisHumansComputer SimulationPhospholipaseLipid bilayer phase behaviorDomain030304 developmental biology0303 health sciencesMembranesMolecular StructureErythrocyte MembraneBiological membraneCell BiologyMembrane transportModels TheoreticalLipid MetabolismLipids0104 chemical sciencesCell biologyErythrocytePhospholipidCholesterolMembraneBiophysicsModelElasticity of cell membranesBiochimica et biophysica acta
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The hemagglutinin of Staphylococcus saprophyticus binds to a protein receptor on sheep erythrocytes.

1997

Staphylococcus saprophyticus, an important cause of urinary tract infections, produces two major surface proteins, the S. saprophyticus surface-associated protein (Ssp) and the hemagglutinin, which mediates fibronectin binding and also functions as the major adhesion of the organism. The hemagglutinating and fibronectin binding functions probably reside on different parts of the molecule. To identify a receptor on eukaryotic cells, binding and inhibition studies with acidic and neutral glycosphingolipids, carbohydrates, and proteins of sheep erythrocyte membranes were conducted. S. saprophyticus did not bind to any glycosphingolipid and no inhibition was observed when hemagglutination assay…

Microbiology (medical)HemagglutinationStaphylococcusImmunologyBiologyBacterial AdhesionGlycosphingolipidsMicrobiologyImmunology and AllergyAnimalsHumanschemistry.chemical_classificationStaphylococcus saprophyticusSheepHemagglutinationErythrocyte MembraneMembrane ProteinsGeneral MedicineBlood ProteinsHemagglutininLigand (biochemistry)biology.organism_classificationMolecular WeightBiochemistryMembrane proteinchemistryFibronectin bindingGalactose oxidaseGlycoproteinMedical microbiology and immunology
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Pore formation by Vibrio cholerae cytolysin follows the same archetypical mode as beta-barrel toxins from gram-positive organisms.

2009

Vibrio cholerae cytolysin (VCC) forms SDS-stable heptameric beta-barrel transmembrane pores in mammalian cell membranes. In contrast to structurally related pore formers of gram-positive organisms, no oligomeric prepore stage of assembly has been detected to date. In the present study, disulfide bonds were engineered to tie the pore-forming amino acid sequence to adjacent domains. In their nonreduced form, mutants were able to bind to rabbit erythrocytes and to native erythrocyte membranes suspended in PBS solution and form SDS-labile oligomers. These remained nonfunctional and represented the long-sought VCC prepores. Disulfide bond reduction in these oligomers released the pore-forming se…

Models MolecularPore Forming Cytotoxic ProteinsMutantBiologyIn Vitro Techniquesmedicine.disease_causeGram-Positive BacteriaBiochemistryModels Biologicalchemistry.chemical_compoundProtein structureGeneticsmedicineAnimalsCysteineProtein Structure QuaternaryMolecular BiologyPeptide sequenceVibrio choleraeCytotoxinsErythrocyte MembraneTransmembrane proteinRecombinant ProteinsMonomerMembraneBiochemistrychemistryVibrio choleraeMutagenesis Site-DirectedCytolysinRabbitsBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Functional size of complement and perforin pores compared by confocal laser scanning microscopy and fluorescence microphotolysis

1991

Abstract Confocal laser scanning microscopy and fluorescence microphotolysis (also referred to as fluorescence photobleaching recovery) were employed to study the transport of hydrophilic fluorescent tracers through complement and perforin pores. By optimizing the confocal effect it was possible to determine the exclusion limit of the pores in situ, i.e. without separation of cells and tracer solution. Single-cell flux measurements by fluorescence microphotolysis yielded information on the sample population distribution of flux rates. By these means a direct comparison of complement and perforin pores was made in sheep erythrocyte membranes. In accordance with previous studies employing a v…

Pore Forming Cytotoxic ProteinsIn situCell Membrane PermeabilityConfocalBiophysicsAntigen-Antibody ComplexIn Vitro TechniquesBiologyBiochemistryTumor Cells CulturedmedicineAnimalsHumansMembrane GlycoproteinsSheepPerforinLasersCell MembraneErythrocyte MembraneMembrane ProteinsComplement System ProteinsCell BiologyFluorescencePhotobleachingCell biologyRed blood cellmedicine.anatomical_structureMembranePerforinMicroscopy Electron Scanningbiology.proteinCytolysinBiochimica et Biophysica Acta (BBA) - Biomembranes
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Mode of primary binding to target membranes and pore formation induced by Vibrio cholerae cytolysin (hemolysin).

1997

Vibrio cholerae cytolysin (VCC) is produced by many non-choleratoxigenic strains of V. cholerae, and possibly represents a relevant pathogenicity determinant of these bacteria. The protein is secreted as a pro-toxin that is proteolytically cleaved to yield the active toxin with a molecular mass of approximately 63 kDa. We here describe a simple procedure for preparative isolation of mature VCC from bacterial culture supernatants, and present information on its mode of binding and pore formation in biological membranes. At low concentrations, toxin monomers interact with a high-affinity binding site on highly susceptible rabbit erythrocytes. This as yet unidentified binding site is absent on…

Pore-forming toxinBinding SitesToxinCytotoxinsErythrocyte MembraneMolecular Sequence DataAerolysinHemolysinBiologymedicine.disease_causeBiochemistryTransmembrane proteinMolecular WeightBiochemistryVibrio choleraemedicineAnimalsHumansCytolysinAmino Acid SequenceRabbitsBinding siteVibrio choleraeEuropean journal of biochemistry
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Factors affecting the amount and the mode of merocyanine 540 binding to the membrane of human erythrocytes. A comparison with the binding to leukemia…

1995

Abstract In the presence of albumin Merocyanine 540 (MC540) exhibits a very limited binding to the outer surface of the membrane of normal erythrocytes, whereas pronounced binding is observed to leukemia cells. To find out whether this difference is due to differences in the composition or structural organization of the cell membrane we analyzed effects of a number of covalent and non-covalent perturbations of the red cell membrane on the binding and fluorescence characteristics of membrane-bound MC540. It is shown that exposure of the cells to cationic chlorpromazine, neuraminidase or photodynamic treatment with AlPcS 4 as sensitizer caused a limited increase (30–50%) of MC540 binding, tog…

Radiation-Sensitizing AgentsTMA-DPHHot TemperatureIndolesBSALightChlorpromazineLipid BilayersBiophysicsPhospholipidNeuraminidaseQuantum yieldPyrimidinonesBiochemistryCell membranechemistry.chemical_compoundt-BuOOHOrganometallic CompoundsTumor Cells CulturedmedicineMerocyanine 540HumansPBSCell MembraneErythrocyte MembraneMembrane structureCell Biologymedicine.diseasePEGFluorescenceDIDSLeukemiaLeukemia cellAlPcS4CholesterolSpectrometry FluorescenceMembranemedicine.anatomical_structureBNML cellsBiochemistrychemistryLeukemia MyeloidCovalent bondBiophysicsMC540Biochimica et Biophysica Acta (BBA) - Biomembranes
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Kinetics of streptolysin O self-assembly.

1995

Streptolysin O is a member of a family of membrane-damaging toxins that bind to cell membranes containing cholesterol and then polymerize to form large pores. We have examined the kinetics of toxin action using 125I-labelled streptolysin O. Binding of toxin monomers to membranes displays first-order kinetics and is reversible; the rate of desorption from red cells shows a marked dependence on temperature. To study oligomerization, toxin was bound to erythrocytes at 0 degrees C. Oligomer formation was then triggered by a sudden temperature shift and stopped by solubilization of membranes with deoxycholate. While at moderately high streptolysin O concentrations oligomerization behaves as a re…

Reaction mechanismErythrocytesToxinMacromolecular SubstancesKineticsErythrocyte MembraneDithionitrobenzoic Acidmedicine.disease_causeOligomerBiochemistrychemistry.chemical_compoundCrystallographyKineticsMembraneMonomerchemistryPolymerizationBacterial ProteinsStreptolysinsmedicineBiophysicsCentrifugation Density GradientAnimalsStreptolysinRabbitsEuropean journal of biochemistry
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Vascular atherosclerotic disease: Behaviour of the red cell phospholipids and their relationships with the erythrocyte membrane fluidity. Preliminary…

2016

Red CellPhysiologyPhospholipidAtherosclerotic diseaseHematologyBiologychemistry.chemical_compoundRed blood cellErythrocyte membranemedicine.anatomical_structureBiochemistrychemistryPreliminary reportPhysiology (medical)medicineCardiology and Cardiovascular Medicine
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