Search results for "erythrocyte"

showing 10 items of 370 documents

Binding of Escherichia coli hemolysin and activation of the target cells is not receptor-dependent.

2005

Abstract Production of a single cysteine substitution mutant, S177C, allowed Escherichia coli hemolysin (HlyA) to be radioactively labeled with tritiated N-ethylmaleimide without affecting biological activity. It thus became possible to study the binding characteristics of HlyA as well as of toxin mutants in which one or both acylation sites were deleted. All toxins bound to erythrocytes and granulocytes in a nonsaturable manner. Only wild-type toxin and the lytic monoacylated mutant stimulated production of superoxide anions in granulocytes. An oxidative burst coincided with elevation of intracellular Ca2+, which was likely because of passive influx of Ca2+ through the toxin pores. Competi…

ErythrocytesAcylationMutantBacterial ToxinsBiologymedicine.disease_causeBiochemistryHemolysin ProteinsSuperoxidesmedicineEscherichia coliHumansReceptorMolecular BiologyEscherichia coliRespiratory BurstSequence DeletionBinding SitesToxinHemolysinBiological activityCell BiologyMolecular biologyLymphocyte Function-Associated Antigen-1Respiratory burstBiochemistryAmino Acid SubstitutionMutationMutagenesis Site-DirectedbacteriaCalciumK562 CellsIntracellularGranulocytesThe Journal of biological chemistry
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On the activity of trifluoperazine and palmitoylcarnitine in mice: Delayed hypersensitivity models

2001

Abstract The effect of pre- and post-challenge treatments with trifluoperazine and palmitoylcarnitine, two protein kinase C (PKC) inhibitors characterised by their interaction with the phospholipid enzyme cofactor, on the inflammation caused by delayed hypersensitivity (DTH) to dinitrofluorobenzene (DNFB) and sheep red blood cells (SRBC) in mice is reported. The activity of dexamethasone and two immunosupressors, azathioprine and methotrexate, is also evaluated. The effectiveness of pre-treatment with each of the test drugs diminished when the DNFB challenge dose increased, whereas trifluoperazine and azathioprine were more active when administered after the challenge at the high DNFB dose.…

ErythrocytesAnti-Inflammatory Agentschemical and pharmacologic phenomenaInflammationTrifluoperazinePharmacologyDexamethasoneGeneral Biochemistry Genetics and Molecular BiologyMicechemistry.chemical_compoundAzathioprinemedicineAnimalsHypersensitivity DelayedEnzyme InhibitorsGeneral Pharmacology Toxicology and PharmaceuticsProtein Kinase CPalmitoylcarnitineProtein kinase CDexamethasoneSheepbusiness.industryPalmitoylcarnitineGeneral MedicineTrifluoperazineMethotrexatechemistryDelayed hypersensitivityDinitrofluorobenzeneFemaleMethotrexatemedicine.symptombusinessHaptenImmunosuppressive Agentsmedicine.drugLife Sciences
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Hypercholesterolemic patients have higher eryptosis and erythrocyte adhesion to human endothelium independently of statin therapy

2021

BACKGROUND Phosphatidylserine (PS) externalization out of the membrane facilitates the eryptotic erythrocytes (EE) binding to endothelial cells (EC), potentially leading to atherosclerosis. Thus, the levels of eryptosis and interactions of EE-EC in hypercholesterolemic patients, either non-medicated or medicated, compared with healthy subjects were studied. METHODS A total of 56 subjects clustered into three groups: (control (n = 20), hypercholesterolemic non-treated (HCNT) (n = 15), and statin-treated (HCT) (n = 21)) were enrolled in this cross-sectional study. Biochemical parameters were determined with validated and standard methods. PS exposure was estimated from annexin-V-binding, cell…

ErythrocytesApolipoprotein BEndotheliumEryptosisPharmacologymedicine.disease_causeMicrocirculationFlow cytometrychemistry.chemical_compoundmedicineHumansEndotheliumbiologymedicine.diagnostic_testbusiness.industryEndothelial CellsGeneral MedicineGlutathionePhosphatidylserineAdhesionCross-Sectional Studiesmedicine.anatomical_structurechemistrybiology.proteinCalciumHydroxymethylglutaryl-CoA Reductase InhibitorsbusinessOxidative stressInternational Journal of Clinical Practice
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Cell-mediated lipoprotein transport: A novel anti-atherogenic concept

2010

Lipoprotein transport is thought to occur in the plasma compartment of the blood, where lipoproteins are modulated by various enzymatic reactions. Subsequently, lipoproteins can migrate through the endothelial barrier to the subendothelial space or are taken up by the liver. The interaction between pro-atherogenic (apoB-containing) lipoproteins and blood cells (especially monocytes and macrophages) in the subendothelial space is well known. This lipoprotein-inflammatory cell interplay is central in the development of the atherosclerotic plaque. In this review, a novel interaction is described between lipoproteins and both leukocytes and erythrocytes in the blood compartment. This lipoprotei…

ErythrocytesApolipoprotein BLipoproteinsComplement receptor 1Blood lipidsLeukocytesInternal MedicinemedicineAnimalsHumansEndothelial dysfunctionComplement ActivationApolipoproteins BbiologyBiological TransportGeneral MedicineLipoprotein(a)Atherosclerosismedicine.diseaseComplement systemCell biologyLiverBiochemistryLipoprotein transportbiology.proteinlipids (amino acids peptides and proteins)Inflammation Mediatorsbiology.geneCardiology and Cardiovascular MedicineLipoproteinAtherosclerosis Supplements
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Crucial role of aspartic acid at position 265 in the CH2 domain for murine IgG2a and IgG2b Fc-associated effector functions.

2008

Abstract Replacement of aspartic acid by alanine at position 265 (D265A) in mouse IgG1 results in a complete loss of interaction between this isotype and low-affinity IgG Fc receptors (FcγRIIB and FcγRIII). However, it has not yet been defined whether the D265A substitution could exhibit similar effects on the interaction with two other FcγR (FcγRI and FcγRIV) and on the activation of complement. To address this question, 34-3C anti-RBC IgG2a and IgG2b switch variants bearing the D265A mutation were generated, and their effector functions and in vivo pathogenicity were compared with those of the respective wild-type Abs. The introduction of the D265A mutation almost completely abolished the…

ErythrocytesAspartic Acid/genetics/physiologyAntibodies Monoclonal/toxicityImmunologyMutantReceptors Fcddc:616.07Complement Activation/genetics/immunologyAlanine/geneticsMiceStructure-Activity RelationshipProtein structureImmunoglobulin G/chemistry/metabolismProtein Isoforms/chemistry/deficiency/genetics/physiologyAspartic acidImmunology and AllergyAnimalsProtein IsoformsErythrocytes/immunologyReceptorComplement ActivationAutoantibodiesAlanineMice KnockoutAspartic AcidMice Inbred BALB CAlaninebiologyAnemia Hemolytic Autoimmune/genetics/immunologyAntibodies MonoclonalReceptors Fc/chemistry/deficiency/genetics/physiologyFragment crystallizable regionIsotypeAmino Acid Substitution/genetics/physiologySialic Acids/geneticsProtein Structure TertiaryMice Inbred C57BLBiochemistryAmino Acid SubstitutionImmunoglobulin Gbiology.proteinSialic AcidsAutoantibodies/toxicityAnemia Hemolytic AutoimmuneAntibodyProtein Structure Tertiary/genetics/physiologyJournal of immunology (Baltimore, Md. : 1950)
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Phobalysin, a Small β-Pore-Forming Toxin of Photobacterium damselae subsp. damselae

2015

ABSTRACT Photobacterium damselae subsp. damselae , an important pathogen of marine animals, may also cause septicemia or hyperaggressive necrotizing fasciitis in humans. We previously showed that hemolysin genes are critical for virulence of this organism in mice and fish. In the present study, we characterized the hlyA gene product, a putative small β-pore-forming toxin, and termed it phobalysin P (PhlyP), for “photobacterial lysin encoded on a plasmid.” PhlyP formed stable oligomers and small membrane pores, causing efflux of K + , with no significant leakage of lactate dehydrogenase but entry of vital dyes. The latter feature distinguished PhlyP from the related Vibrio cholerae cytolysin…

ErythrocytesBacterial ToxinsMolecular Sequence DataImmunologyVirulencemedicine.disease_causeHemolysin ProteinsHemolysisMicrobiologyBacterial AdhesionMicrobiologyHemolysin ProteinsmedicineAnimalsHumansAmino Acid SequencePore-forming toxinbiologyPhotobacteriumEpithelial CellsHemolysinPhotobacteriumbiology.organism_classificationMolecular PathogenesisInfectious DiseasesPhotobacterium damselaeVibrio choleraeParasitologyRabbitsCytolysinSequence AlignmentInfection and Immunity
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Phospholipid-polyaspartamide micelles for pulmonary delivery of corticosteroids

2011

A novel drug delivery system for beclomethasone dipropionate (BDP) has been constructed through self-assembly of a pegylated phospholipid-polyaminoacid conjugate. This copolymer was obtained by chemical reaction of α,β-poly(N-2-hydroxyethyl)-DL-aspartamide (PHEA) with 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-[amino(polyethyleneglycol)2000] (DSPE-PEG(2000)-NH(2)). Benefiting from the amphiphilic structure with the hydrophilic shell based on both PHEA and PEG and many hydrophobic stearoyl tails, PHEA-PEG(2000)-DSPE copolymer was able to self assemble into micelles in aqueous media above a concentration of 1.23 × 10(-7)M, determined by fluorescence studies. During the self-assembling …

ErythrocytesBiocompatibilityCell SurvivalDrug CompoundingDrug StorageALPHABETA-Poly(N-2-hydroxyethyl)-dl- aspartamide (PHEA) 12-distearoyl-sn-glycero-3-phosphoethanolamine-N-[amino(polyethyleneglycol)2000](DSPE-PEG2000-NH2) Polymeric micelles Drug delivery Beclomethasone dipropionate (BDP) Pulmonary diseasesPhospholipidPharmaceutical Science[object Object]HemolysisMicelleCell LinePolyethylene Glycolschemistry.chemical_compoundDrug StabilityAmphiphilePEG ratioPulmonary diseasesHumans?Beclomethasone dipropionate (BDP)Particle SizeLungMicellesDrug CarriersChromatographyAqueous solutionMolecular StructureChemistryPhosphatidylethanolaminesBeclomethasonetechnology industry and agriculture?-Poly(N-2-hydroxyethyl)-dl-aspartamide (PHEA)Spectrometry FluorescenceSolubilitySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoDrug deliveryDrug deliveryPolymeric micellesNanocarriersPeptidesHydrophobic and Hydrophilic InteractionsNuclear chemistry
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Interaction between N-terminal domain of H4 and DNA is regulated by the acetylation degree.

1998

Abstract To study whether the acetylation of one or more of the four acetylatable lysines of histone H4 affects its binding to DNA, we have designed a protection experiment with a model system consisting in phage lambda DNA as substrate, Stu I as restriction endonuclease and histone H4 with different degrees of acetylation as the protective agent. It can be deduced from the experimental data that the protection afforded by the histone is not dependent on the number of positive charges lost by acetylation. Thus, non-acetylated H4 and mono-acetylated H4 cause similar protection, while di-acetylation of the histone seems to be the crucial step in significantly weakening the interaction between…

ErythrocytesBiophysicsAcetylationDNABiologySAP30Chemical FractionationChromatography Ion ExchangeBiochemistryPeptide FragmentsHistone H4HistonesBiochemistryHistone H1Structural BiologyHistone H2AGeneticsHistone codeNucleosomeAnimalsHistone octamerHistone deacetylaseChickens
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Construction of an agglutination tool: recombinant Fab fragments biotinylated in vitro.

2009

The pComb3H vector system is used for constructing and panning recombinant antibody libraries. It allows for expression of monovalent Fab fragments, either on the surface of M13 phage, or in the form of soluble proteins secreted into the periplasmic space of bacteria. We constructed a modified pComb3H vector containing cDNA encoding for a 23-amino acid fragment of the Escherichia coli biotin carboxy carrier protein (BCCP), which is an acceptor sequence for biotinylation. The vector was used to express the Fab fragment recognizing human glycophorin A. The purified Fab fragment containing this biotin acceptor sequence was effectively biotinylated in vitro using biotin ligase (BirA). The speci…

ErythrocytesBlotting WesternBioengineeringlaw.inventionchemistry.chemical_compoundImmunoglobulin Fab FragmentsBiotinlawAgglutination TestsGlycophorinHumansBiotinylationGlycophorinsMolecular BiologybiologyChemistryHemagglutinationGeneral MedicinePeriplasmic spaceAvidinMolecular biologyPrimary and secondary antibodiesRecombinant ProteinsAgglutination (biology)BiochemistryBiotinylationbiology.proteinRecombinant DNAChromatography GelElectrophoresis Polyacrylamide GelBiotechnologyAvidinProtein BindingNew biotechnology
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Naturally occurring hemolysins in the coelomic fluid of Holothuria polii delle chiaie (Echinodermata).

1979

Abstract The coelomic fluid of Holothuria polii D.Ch contains hemolytic activity against erythrocytes of several vertebrate species. The hemolytic potency depends upon calcium ion concentration and varies according to erythrocyte source and cell number in the reaction mixture. Absorption experiments with formalinized rabbit erythrocytes suggest that hemolytic activity is not specific. Its heat lability, water insolubility at low pH values, and sensitivity to proteolytic enzymes suggest that hemolytic activity resides in protein molecules. The activity, maximal in alkaline media, appears to depend up time and temperature.

ErythrocytesCations DivalentSea CucumbersImmunologyDose-Response Relationship Immunologicchemistry.chemical_elementCalciumHemolysisHemolysin ProteinsPotencyAnimalsbiologyLabilityProteolytic enzymesTemperatureHemolysinExudates and TransudatesHydrogen-Ion Concentrationbiology.organism_classificationKineticschemistryBiochemistryCoelomAbsorption (chemistry)HolothuriaDevelopmental BiologyEchinodermataDevelopmental and comparative immunology
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