Search results for "Hemolysis"

showing 10 items of 89 documents

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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Polymer-doxycycline conjugates as fibril disrupters: an approach towards the treatment of a rare amyloidotic disease.

2014

The term amyloidosis describes neurological diseases where an abnormal protein is misfolded and accumulated as deposits in organs and tissues, known as amyloid, disrupting their normal function. In the most common familial amyloid polyneuropathy (FAP), transthyretin (TTR) displays this role primarily affecting the peripheral nervous system (PNS). Advanced stages of this inherited rare amyloidosis, present as fibril deposits that are responsible for disease progression. In order to stop disease progression, herein we designed an efficient family of nanoconjugates as fibril disrupters. These polymer conjugates are based on doxycycline (doxy), already in phase II trials for Alzheimer's disease…

DrugAmyloidErythrocytesAmyloidmedia_common.quotation_subjectPharmaceutical ScienceMice TransgenicFibrilHemolysisPlasmaIn vivomedicinePolymeric drugAnimalsTissue DistributionAmyloid disruptersmedia_commonDoxycyclineAmyloid Neuropathies FamilialMice Inbred BALB CbiologyChemistryAmyloidosismedicine.diseaseRare diseasesRatsTransthyretinPolymer-drug conjugateDisease Models AnimalDrug LiberationBiochemistryPolyglutamic AcidDoxycyclineDrug deliveryDrug deliverybiology.proteinCancer researchPolymer therapeuticsmedicine.drugJournal of controlled release : official journal of the Controlled Release Society
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An allergen-polymeric nanoaggregate as a new tool for allergy vaccination.

2014

Parietaria pollen is one of the major causes of allergic reaction in southern Europe, affecting about 30% of all allergic patients in this area. Specifi immunotherapy is the only treatment able to modify the natural outcome of the disease by restoring a normal immunity against allergens. The preparation of allergen-solid lipid nanoparticles as delivery vehicles for therapeutic proteins, P. judaica major allergen Par j 2, was investigated. The Par j 2 allergen was expressed in a large amount in Escherichia coli and purifid to homogeneity. Its immunological properties were studied by western blotting and enzyme-linked immunosorbent assay inhibition. Solid lipid nanoparticles were obtained by …

ElectrophoresisLightCell SurvivalChemistry PharmaceuticalPharmaceutical ScienceImmunoglobulin Emedicine.disease_causeMicroscopy Atomic ForceHemolysislaw.inventionCell LineMiceAllergenDrug StabilitylawZeta potentialmedicineSide chainHypersensitivityAnimalsHumansNanotechnologyScattering RadiationTechnology PharmaceuticalPlant ProteinsDrug CarriersVaccines SyntheticbiologyChemistryMacrophagesVaccinationBiological activityAllergensAntigens PlantImmunoglobulin EIn vitroBasophilsElectrophoresisAllergyParietaria pollenRecombinant allergens PHEAPolymeric nanoaggregatesBiochemistryImmunologybiology.proteinRecombinant DNANanoparticlesPeptides
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Microwave-assisted synthesis of PHEA-oligoamine copolymers as potential gene delivery systems

2009

Aims - Copolymers bearing oligoamines and having buffering capacity in the endosomal pH range seems very promising as non viral vectors in gene delivery, due to the great importance of endosomal escaping for an efficient endocellular DNA release. Aim of this paper was to prepare new copolymers based on α,β-poly-(N-2-hydroxyethyl)-D,L-aspartamide (PHEA) as polymeric backbone and bearing an oligoamine, such as diethylentriamine (DETA) in the side chain and useful for gene delivery. Moreover in order to reduce solvent volume and to make faster the reaction, microwave-assisted has been used. Materials and methods - PHEA copolymers bearing different amount of DETA were prepared by using bis(4-ni…

Erythrocyte AggregationMaterials scienceCell SurvivalPolymersBiomedical EngineeringMedicine (miscellaneous)Bioengineeringmicrowave-assisted synthesis PHEA polycationDevelopmentGene deliveryHemolysisMicrowave assistedpolyhydroxyethylaspartamideNitrophenolsMicechemistry.chemical_compoundPlasmid dnaCell Line TumorPolymer chemistryPolyaminesSide chainCopolymerAnimalsHumansGeneral Materials Sciencegene deliveryMicrowavesDerivatizationPolyhydroxyethyl MethacrylateDETA diethyltriamineGene Transfer TechniquesDNACombinatorial chemistrySolventchemistryDiethylenetriamine
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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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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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The molecular basis of the low hemolytic activity of C4 molecules from low-C4 mice with IgM-coated erythrocytes.

1989

This study investigated the origin of the different hemolytic activity of two allotypes of murine C4, C4H (C4-high) and C4L (C4-low) in the presence of IgM-coated erythrocytes. C4H displayed a threefold higher hemolytic titer (expressed in hemolytic units/microgram protein) than C4L. No difference was found between c4H and C4L either in stability at 37 degrees C at different pH values and in the rate of C4H and C4L hydrolysis by activated Cl. The major functional difference was found in the covalent binding capacity to IgM-coated erythrocytes, with the amount of C4H bound being about threefold higher than that of C4L. A marked difference in the reactivity of the C4b fragment of C4H and C4L …

ErythrocytesImmunologyMice Inbred StrainsBiologyHemolysisMethylaminesMiceComplementary DNAImidoestersmedicineImmunology and AllergyAnimalsComplement ActivationAllelesSouthern blotMessenger RNAComplement C5Biological activityComplement C4Complement C3Hydrogen-Ion Concentrationmedicine.diseaseHemolysisRed blood cellBlotting Southernmedicine.anatomical_structureBiochemistryGenesGlycinebiology.proteinAntibodyProtein BindingEuropean journal of immunology
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Inhibitory activity of sphingomyelin on hemolytic activity of coelomic fluid of Holothuria polii (echinodermata)

1987

Abstract The hemolytic activity of coelomic fluid from Holothuria polii is specifically inhibited by sphingomyelin. This phospholipid is the constituent of the membrane which probably interacts with the hemolysin thereby leading to the lysis.

ErythrocytesLysisSea CucumbersImmunologyPhospholipidSettore BIO/05 - ZoologiaInhibitory postsynaptic potentialHemolysisMicrobiologychemistry.chemical_compoundmedicineAnimalsPhospholipidsComplement Inactivator ProteinsBacteriabiologyHemolysinbiology.organism_classificationBody FluidsSphingomyelinsRed blood cellCholesterolSphingomyelin Phosphodiesterasemedicine.anatomical_structurechemistryBiochemistryCoelomlipids (amino acids peptides and proteins)SphingomyelinHolothuriaEchinodermataDevelopmental Biology
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Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin

2013

Pyolysin (PLO) belongs to the homologous family of the cholesterol- dependent cytolysins (CDCs), which bind to cell membranes containing cholesterol to form oligomeric pores of large size. The CDC monomer structure consists of 4 domains. Among these, the C-terminal domain 4 has been implicated in membrane binding of the monomer, while the subsequent processes of oligomerization and membrane insertion have primarily been assigned to other domains of the molecule. Recombinantly expressed or proteolytic fragments that span domain 4 of the CDCs streptolysin O and perfringolysin O bind to membranes but fail to oligomerize, and they inhibit the activity of the respective wild-type toxins. We repo…

ErythrocytesMembrane bindingCellprotein bindingBiochemistryoligomerHemolysin Proteinschemistry.chemical_compoundReaction kineticsToxic materialsMonomersprotein domainRecombinant ProteinsHemolysisunclassified drugcytolysinmedicine.anatomical_structureMembraneBiochemistryStreptolysinsStreptolysinLarge sizeBacterial ToxinsBiologyCholesterol-dependent cytolysinHemolysisoligomerizationMembrane LipidsBacterial ProteinsProteolytic fragmentsEscherichia colimedicineAnimalsMonomer structuresMolecular BiologySheep Domesticcarboxy terminal sequenceC-terminal domainsCholesterolC-terminusCell MembraneHemolytic activitycholesterolCell Biologymedicine.diseaseProtein Structure TertiaryCell membranesKineticschemistryOligomersProtein MultimerizationPyolysinprotein pyolysinMembrane insertionCytology
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