Search results for "Calcein"

showing 10 items of 11 documents

Epimagnolin A, a tetrahydrofurofuranoid lignan from Magnolia fargesii, reverses ABCB1-mediated drug resistance.

2018

Abstract Background Epimagnolin A is an ingredient of the Chinese crude drug Shin-i, derived from the dried flower buds of Magnolia fargesii and Magnolia flos, which has been traditionally used for the treatment of allergic rhinitis and nasal congestion, empyema, and sinusitis. The pharmacokinetic activity of epimagnolin A remains to be evaluated. Purpose In this study, we examined the possible interactions of epimagnolin A with human ATP-binding cassette (ABC) transporter ABCB1, a membrane protein vital in regulating the pharmacokinetics of drugs and xenobiotics. Study design/methods The interaction of epimagnolin A with ABCB1 was evaluated in calcein, ATPase, and MTT assays by using Flp-I…

0301 basic medicineATP Binding Cassette Transporter Subfamily BATPasePharmaceutical ScienceATP-binding cassette transporterPharmacologyCrude drugLignans03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePharmacokineticsCell Line TumorDrug DiscoverymedicineHumansEnzyme kineticsP-glycoproteinPharmacologyAdenosine TriphosphatasesbiologyAntineoplastic Agents PhytogenicDrug Resistance MultipleCalceinMolecular Docking Simulation030104 developmental biologyComplementary and alternative medicinechemistryVerapamilDrug Resistance NeoplasmMagnolia030220 oncology & carcinogenesisbiology.proteinMolecular MedicineVerapamilmedicine.drugPhytomedicine : international journal of phytotherapy and phytopharmacology
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Alkamides from Echinacea angustifolia Interact with P-Glycoprotein of Primary Brain Capillary Endothelial Cells Isolated from Porcine Brain Blood Ves…

2013

The blood-brain barrier prevents the passage of toxic compounds from blood circulation into brain tissue. Unfortunately, drugs for the treatment of neurodegenerative diseases, brain tumors, and other diseases also do not cross the blood-brain barrier. In the present investigation, we used isolated porcine brain capillary endothelial cells and a flow cytometric calcein-AM assay to analyze inhibition of P-glycoprotein, a major constituent of the blood-brain barrier. We tested 8 alkamides isolated from Echinacea angustifolia and found that four of them inhibited P-glycoprotein-mediated calcein transport in porcine brain capillary endothelial cells.

ATP Binding Cassette Transporter Subfamily BPolyunsaturated AlkamidesSwinePharmaceutical ScienceATP-binding cassette transporterCapillary endothelial cellsPharmacologyBlood–brain barrierEchinaceaAnalytical Chemistrychemistry.chemical_compoundDrug DiscoverymedicineAnimalsCells CulturedP-glycoproteinPharmacologyDose-Response Relationship DrugMolecular StructurebiologyEchinacea angustifoliaOrganic ChemistryBrainEndothelial CellsBiological TransportFlow CytometryFluoresceinsbiology.organism_classificationCalceinmedicine.anatomical_structureComplementary and alternative medicinechemistryBlood-Brain BarrierBlood circulationbiology.proteinMolecular MedicinePorcine brainPlanta Medica
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Zur direkten komplexometrischen Calciumbestimmung im Serum mit Calcein als Indicator

1958

Es wird eine einfache Methode zur direkten komplexometrischen Ca-Bestimmung im Serum ohne Fallung und Enteiweisung mit Calcein als Indicator angegeben. Nach ausreichender Verdunnung wird die Titration bei pH>13 ausgefuhrt, wobei Mg quantitativ als Hydroxyd ausfallt. Bei der Standardmethode wird 1 ml Serum mit 0,002 m Komplexon titriert, gegebenenfalls konnen auch 0,5 ml Serum mit 0,0005 m Komplexon titriert werden. Eine Doppelbestimmung nimmt kaum mehr als 2 min in Anspruch.

Calceinchemistry.chemical_compoundChromatographyChemistryDrug DiscoveryMolecular Medicinechemistry.chemical_elementGeneral MedicineCalciumGenetics (clinical)Klinische Wochenschrift
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Fluorescent Nanowires Self-Assembled through Host-Guest Interactions in Modified Calcein

2011

Calceinchemistry.chemical_compoundNanostructureChemistryNanowireNanotechnologyGeneral ChemistrySelf-assemblyGeneral MedicineHost (network)FluorescenceCatalysisSelf assembledAngewandte Chemie
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Innentitelbild: Fluorescent Nanowires Self-Assembled through Host-Guest Interactions in Modified Calcein (Angew. Chem. 32/2011)

2011

Calceinchemistry.chemical_compoundchemistryNanowireNanotechnologyGeneral MedicineFluorescenceSelf assembledAngewandte Chemie
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Inside Cover: Fluorescent Nanowires Self-Assembled through Host-Guest Interactions in Modified Calcein (Angew. Chem. Int. Ed. 32/2011)

2011

Calceinchemistry.chemical_compoundchemistryPolymer chemistryNanowireGeneral ChemistrySelf-assemblyPhotochemistryFluorescenceCatalysisSelf assembledAngewandte Chemie International Edition
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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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Functional evidence of multidrug resistance transporters (MDR) in rodent olfactory epithelium.

2012

WOS: 000305340700029; International audience; BACKGROUND: P-glycoprotein (Pgp) and multidrug resistance-associated protein (MRP1) are membrane transporter proteins which function as efflux pumps at cell membranes and are considered to exert a protective function against the entry of xenobiotics. While evidence for Pgp and MRP transporter activity is reported for olfactory tissue, their possible interaction and participation in the olfactory response has not been investigated. PRINCIPAL FINDINGS: Functional activity of putative MDR transporters was assessed by means of the fluorometric calcein acetoxymethyl ester (calcein-AM) accumulation assay on acute rat and mouse olfactory tissue slices.…

MaleAnatomy and Physiology[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionGene Expressionlcsh:MedicineATP-binding cassette transporterPharmacologyMicechemistry.chemical_compoundMolecular Cell Biologypolycyclic compoundslcsh:ScienceMice Inbred BALB CMultidisciplinaryNeuromodulationProbenecidReverse Transcriptase Polymerase Chain ReactionNeurochemistryFluoresceinsSensory SystemsCell biologyElectrophysiologymedicine.anatomical_structureAlimentation et NutritionCyclosporineQuinolinesMedicineFemaleEffluxCellular TypesMultidrug Resistance-Associated Proteinsproduct p-glycoprotein;blood-brain-barrier;receptor neurons;cyclic-nucleotides;tumor-cells;expression;localization;protein;gene;tissuesMultidrug Resistance-Associated ProteinsResearch ArticleATP Binding Cassette Transporter Subfamily BNeurophysiologyBiologyOlfactory Receptor NeuronsOlfactory mucosaPsychologie (Sciences cognitives)Olfactory MucosaPeripheral Nervous SystemmedicineAnimalsFood and NutritionRats WistarBiologyOlfactory SystemOlfactory receptorlcsh:RNeurosciencesEpithelial CellsBiological TransportTransporterRatsCalceinMicroscopy FluorescenceVerapamilchemistryNeurons and Cognitionlcsh:QPropionates[SDV.AEN]Life Sciences [q-bio]/Food and NutritionOlfactory epitheliumNeuroscience
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Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins

2005

Bax and Bid are proapoptotic proteins of the Bcl-2 family that regulate the release of apoptogenic factors from mitochondria. Although they localize constitutively in the cytoplasm, their apoptotic function is exerted at the mitochondrial outer membrane, and is related to their ability to form transbilayer pores. Here we report the poration activity of fragments from these two proteins, containing the first alpha-helix of a colicinlike hydrophobic hairpin (alpha-helix 5 of Bax and alpha-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly alpha-helical structures and induce the release of entrapped calcein. In planar lipid membranes they fo…

Models MolecularMolecular Sequence DataBiophysicsApoptosisPeptideIn Vitro TechniquesBiophysical PhenomenaIon ChannelsPermeabilityProtein Structure Secondarychemistry.chemical_compoundBcl-2-associated X proteinSpectroscopy Fourier Transform InfraredHumansChannels Receptors and Electrical SignalingAmino Acid SequencePeptide sequenceIon channelbcl-2-Associated X Proteinchemistry.chemical_classificationbiologyChemistryCircular DichroismPeptide FragmentsCell biologyCalceinMembraneProto-Oncogene Proteins c-bcl-2CytoplasmMultiprotein ComplexesLiposomesbiology.proteinPèptidsCarrier ProteinsBacterial outer membraneProteïnesBH3 Interacting Domain Death Agonist ProteinBiophysical Journal
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Effect of Caseinophosphopeptides from αs- and β-Casein on Iron Bioavailability in HuH7 Cells

2015

International audience; Two pools of caseinophosphopeptides (CPPs) obtained from αs- and β-casein fractions (α-CPPs and β-CPPs) were characterized. A total of 16 CPPs were identified in the α-CPPs pool, 9 of them derived from αs1-casein and 7 from αs2-casein. A total of 18 CPPs were identified in the β-CPPs pool. Four of the identified CPPs contained the characteristic phosphoseryl-glutamic acid cluster SpSpSpEE. Calcein assay was used to compare the iron-binding capacity of the α- and β-CPPs pools. At the concentration of 12.5 μM CPPs used in the iron bioavailability assays, β-CPPs pools show greater iron-binding capacity than α-CPPs pools. HuH7 human hepatoma cells show many differentiate…

PhosphopeptidesIronBiological AvailabilitydigestionModels BiologicalMass Spectrometryproduit laitierchemistry.chemical_compoundcaséinophosphopeptideIn vivoCell Line TumorReceptors Transferrinferritine[SDV.IDA]Life Sciences [q-bio]/Food engineeringHumanscellule HuH7Chromatography High Pressure LiquidComputingMilieux_MISCELLANEOUSSoluble transferrin receptorbiologytransferrine solubleCaseinsGeneral ChemistryMolecular biologyBioavailabilityFerritinCalceinnutritionchemistryβ caseinBiochemistryFerritinsbiology.proteinGeneral Agricultural and Biological Sciences[SDV.AEN]Life Sciences [q-bio]/Food and NutritionJournal of Agricultural and Food Chemistry
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