Search results for "erythrocyte"

showing 10 items of 370 documents

Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gra…

1998

Streptolysin O (SLO) is a bacterial exotoxin that binds to cell membranes containing cholesterol and then oligomerizes to form large pores. Along with rings, arc-shaped oligomers form on membranes. It has been suggested that each arc represents an incompletely assembled oligomer and constitutes a functional pore, faced on the opposite side by a free edge of the lipid membrane. We sought functional evidence in support of this idea by using an oligomerization-deficient, non-lytic mutant of SLO. This protein, which was created by chemical modification of a single mutant cysteine (T250C) with N-(iodoacetaminoethyl)-1-naphthylamine-5-sulfonic acid, formed hybrid oligomers with active SLO on memb…

Cell Membrane PermeabilityProtein ConformationMembrane lipidsBiologyCholesterol-dependent cytolysinComplement Hemolytic Activity AssayOligomerGeneral Biochemistry Genetics and Molecular BiologyMembrane Lipidschemistry.chemical_compoundBacterial ProteinsNaphthalenesulfonatesAnimalsProtein oligomerizationCysteineLipid bilayerMolecular BiologyGeneral Immunology and MicrobiologyGeneral NeuroscienceErythrocyte MembraneCalceinMembranechemistryBiochemistryMutationStreptolysinsBiophysicsStreptolysinRabbitsResearch ArticleThe EMBO Journal
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Gas chromatographic analysis of resveratrol in plasma, lipoproteins and cells after in vitro incubations

1998

Resveratrol is a trihydroxystilbene present in certain red wines. It may play a role in the inhibition of lipoprotein oxidation and platelet activity. We have developed the first method to measure resveratrol in animal and human samples and to study its incorporation in vitro. After adding epicoprostanol as an internal standard, samples are subjected to lipid extraction in the presence of antioxidant and under dim light to minimize both denaturation and isomerization of the trans-resveratrol to the cis-form. Extracts were purified by cold acetone precipitation and the resveratrol-containing acetone phase was evaporated under nitrogen. The resveratrol was analyzed as a trimethylsilyl derivat…

Chromatography GasErythrocytesAntioxidantendocrine system diseasesmedicine.medical_treatmentResveratrolSensitivity and Specificitychemistry.chemical_compoundStilbenesAcetonemedicineAnimalsHumansPlatelet activationLipoprotein oxidationDetection limitChromatographyorganic chemicalsReproducibility of Resultsfood and beveragesStereoisomerismGeneral ChemistryRatsLipoproteins LDLchemistryResveratrolCalibrationLinear ModelsGas chromatographyQuantitative analysis (chemistry)Platelet Aggregation InhibitorsJournal of Chromatography B: Biomedical Sciences and Applications
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Core Histones Are Glutaminyl Substrates for Tissue Transglutaminase

1996

Chicken erythrocyte core histones are glutaminyl substrates in the transglutaminase (TGase) reaction with monodansylcadaverine (DNC) as donor amine. The modification is very fast when compared with that of many native substrates of TGase. Out of the 18 glutamines of the four histones, nine (namely glutamine 95 of H2B; glutamines 5, 19, and 125 of H3; glutamines 27 and 93 of H4; and glutamines 24, 104, and 112 of H2A) are the amine acceptors in free histones. The use of Gln112 of H2A requires a temperature-dependent partial unfolding of the histone, showing that structural determinants are decisive for the glutamine specificity. The structures of H2A and H2B do not appreciably change upon mo…

Circular dichroismErythrocytesTissue transglutaminaseGlutamineGuinea PigsMolecular Sequence DataIn Vitro TechniquesBiochemistrySubstrate SpecificityHistoneschemistry.chemical_compoundCadaverineAnimalsNucleosomeAmino Acid SequenceMolecular BiologyPeptide sequenceTransglutaminasesMolecular StructurebiologyMethylamineCell BiologyNucleosomesChromatinGlutamineKineticsHistonechemistryBiochemistrybiology.proteinJournal of Biological Chemistry
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Intraoperative transfusion practices and perioperative outcome in the European elderly: A secondary analysis of the observational ETPOS study

2022

PLOS ONE 17(1), e0262110 (2022). doi:10.1371/journal.pone.0262110

Clinical OncologyMaleScienceClinical Decision-MakingCancer TreatmentSurgical and Invasive Medical ProceduresGeographical LocationsDiagnostic MedicineOutcome Assessment Health CareMedicine and Health SciencesHumansBlood TransfusionProspective StudiesAgedAged 80 and overIntraoperative CareMultidisciplinaryTransfusion MedicineQRAnemiaHematologyClinical Laboratory SciencesHealth CareEuropeSurgical OncologyOncologyAge GroupsElective Surgical ProceduresPeople and PlacesMedicinePopulation GroupingsFemaleGeriatric CareClinical MedicineErythrocyte TransfusionResearch ArticlePLOS ONE
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The Mucus of Actinia equina (Anthozoa, Cnidaria): An Unexplored Resource for Potential Applicative Purposes

2015

The mucus produced by many marine organisms is a complex mixture of proteins and polysaccharides forming a weak watery gel. It is essential for vital processes including locomotion, navigation, structural support, heterotrophic feeding and defence against a multitude of environmental stresses, predators, parasites, and pathogens. In the present study we focused on mucus produced by a benthic cnidarian, the sea anemone Actinia equina (Linnaeus, 1758) for preventing burial by excess sedimentation and for protection. We investigated some of the physico-chemical properties of this matrix such as viscosity, osmolarity, electrical conductivity, protein, carbohydrate, and total lipid contents. Som…

CnidariaErythrocytesCarbohydratesPharmaceutical ScienceSea anemonePolysaccharideActinia equina; Antibacterial activity; Cytotoxicity; Hemolytic activity; Mucus; Tumor cell line K562; Drug Discovery3003 Pharmaceutical ScienceArticleActinia equinaBiological FactorsCnidarian Venomsantibacterial activityDry weightCell Line TumorAnthozoaDrug DiscoveryAnimalsHumanshemolytic activitylcsh:QH301-705.5Pharmacology Toxicology and Pharmaceutics (miscellaneous)chemistry.chemical_classification<i>Actinia equina</i>tumor cell line K562biologyCytotoxinsHemolytic AgentsEcologyDrug Discovery3003 Pharmaceutical SciencemucuAnthozoabiology.organism_classificationInvertebratesMucusAnti-Bacterial AgentsMucusSea Anemoneslcsh:Biology (General)chemistryBiochemistryMucucytotoxicityRabbitsK562 CellsAntibacterial activityActiniaMarine Drugs
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Complement receptors on lymphocytes

1981

Complement component 5Cancer ResearchErythrocytesRosette FormationSheepComplement component 2CD46ChemistryComplement C3General MedicineComplement receptorImmune receptorBurkitt LymphomaComplement factor BCell LineReceptors ComplementClassical complement pathwayOncologyImmunologyAnimalsHumansLymphocytesCFHR5Journal of Cancer Research and Clinical Oncology
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Interaction ofEscherichia colihemolysin with biological membranes

2001

Escherichia coli hemolysin (HlyA) is a membrane-permeabilizing protein belonging to the family of RTX-toxins. Lytic activity depends on binding of Ca2(+) to the C-terminus of the molecule. The N-terminus of HlyA harbors hydrophobic sequences that are believed to constitute the membrane-inserting domain. In this study, 13 HlyA cysteine-replacement mutants were constructed and labeled with the polarity-sensitive fluorescent probe 6-bromoacetyl-2-dimethylaminonaphthalene (badan). The fluorescence emission of the label was examined in soluble and membrane-bound toxin. Binding effected a major blue shift in the emission of six residues within the N-terminal hydrophobic domain, indicating inserti…

Conformational changeProtein ConformationPlasma protein bindingBiologymedicine.disease_causeHemolysisBiochemistryHemolysin ProteinsProtein structureBacterial Proteins2-NaphthylamineEscherichia colimedicineCysteineCloning MolecularLipid bilayerEscherichia coliFluorescent DyesEscherichia coli ProteinsCell MembraneErythrocyte MembraneBiological membraneProtein Structure TertiarySpectrometry FluorescenceMembraneBiochemistryMutagenesisLiposomesChromatography GelCalciumElectrophoresis Polyacrylamide GelProtein BindingBinding domainEuropean Journal of Biochemistry
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A versatile model of steady state O2 supply to tissue. Application to skeletal muscle

1990

A model of combined convective and diffusive O2 transport to tissue is suggested which allows for the calculation of PO2 distributions in a cuboid tissue region with arbitrary microvascular geometries and blood flows. Carrier-facilitated O2 diffusion in the erythrocytes and in the tissue and red blood cell reaction kinetics are considered. The model is based on analytical descriptions of the PO2 fields of single erythrocytes surrounded by carrier-free layers in an infinite three-dimensional space containing an O2 carrier such as myoglobin. These PO2 fields are overlaid to obtain a solution of the differential equation of diffusion in respiring tissue. The model has been applied to a situati…

Convectioninorganic chemicalsErythrocytesDifferential equationPartial PressureBiophysicsHomogenization (chemistry)Models Biologicalchemistry.chemical_compoundOxygen ConsumptionmedicineAnimalsCuboidMusclesConductanceSkeletal muscleAnatomyOxygenRed blood cellmedicine.anatomical_structureMyoglobinchemistryRegional Blood FlowBiophysicsMathematicsResearch ArticleBiophysical Journal
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Cytotoxic activity of Ciona intestinalis (Tunicata) hemocytes: Properties of the in vitro reaction against erythrocyte targets

1993

Hemocytes (effectors) of Ciona intestinalis showed a natural cytotoxic capacity (HCA) when assayed in vitro against erythrocytes (targets). Cytotoxic cells lysed, to a variable extent, rabbit (RE), human (A, B, O), guinea pig, and sheep (SE) erythrocytes. Hemocyte cytotoxic activity (HCA) assayed against SE is a calcium-dependent reaction, occurs rapidly (15-30 min), at 25-37 degrees C over a wide range of pH (5.4-8.0). Assays were carried out using: 1) the medium in which hemocytes were maintained, 2) the soluble portion of hemocyte lysates, and 3) debris prepared from hemocyte lysates. Results suggest that HCA is a cell-mediated process that requires effector-target cell contacts. Anti-SE…

Cytotoxicity ImmunologicErythrocytesHemocytesLysisCiona intestinaliCytotoxicityHemolysinImmunologyCellHemocyteTunicateHemolymphmedicineAnimalsCytotoxic T cellCiona intestinalisInvertebrateCytotoxicitySheepbiologyHemolysinHemagglutination Testsbiology.organism_classificationMolecular biologyIn vitroCiona intestinalisRed blood cellmedicine.anatomical_structureImmunologySheep erythrocyteDevelopmental BiologyDevelopmental &amp; Comparative Immunology
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Expression of P, S, and F1C adhesins by cytotoxic necrotizing factor1-producing Escherichia coli from septicemic and diarrheic pigs

1997

Nineteen papC-positive cytotoxic necrotizing factor 1 (CNF1)-producing Escherichia coli isolates from pigs with septicemia or diarrhea were tested for the presence of pap-, sfa-, and afa-related sequences encoding P/Prs, S/F1C, and Dr/AFA adhesins respectively. Production of adhesins by isolates was tested by mannose-resistant hemagglutination (MRHA), sialidase treatment of erythrocytes and particle agglutination tests. Production of P, S, and F1C fimbriae by isolates was also examined by immunofluorescence. All isolates were pap+ by PCR. Eighteen isolates (95%) were MRHA for ovine and human A erythrocytes and exhibited GalNac-GalNac receptor specificity associated with class III P(Prs) adh…

DiarrheaSerotypeErythrocytesHemagglutinationSwine[SDV]Life Sciences [q-bio]Bacterial ToxinsFimbriaBiologyImmunofluorescencemedicine.disease_causeMicrobiologyMicrobiologyAgglutination TestsSepsisEscherichia coliGeneticsmedicineAnimalsHumansAdhesins BacterialMolecular BiologyEscherichia coliEscherichia coli InfectionsSwine DiseasesAntiserumSheepmedicine.diagnostic_testCytotoxinsEscherichia coli Proteinsbiochemical phenomena metabolism and nutritionBacterial adhesin[SDV] Life Sciences [q-bio]Agglutination (biology)Fimbriae BacterialCattle
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