Search results for "Interactions"

showing 10 items of 1963 documents

Automated Determination of Paroxetine and Its Main Metabolite by Column Switching and On-Line High-Performance Liquid Chromatography

1994

An automated column-switching method coupled to isocratic high-performance liquid chromatography has been developed for simultaneous determination of blood levels of paroxetine and its nonconjugated main metabolite BRL 36610. The lower limits of detection were 9-15 nmol/L (3-5 ng/ml) and linearity between drug concentration and detector response was found for 0-1,500 nmol/L (0-500 ng/ml). The method could be applied to the analysis of serum samples obtained from depressed patients who were treated with daily oral doses of 20 or 40 mg of paroxetine. After the 20-mg dose, the mean blood level of paroxetine was 69 nM (23 ng/ml), whereas the metabolite BRL 36610 was detectable in only one of 5 …

ImipramineMetaboliteSensitivity and SpecificityHigh-performance liquid chromatographyImipramineMixed Function Oxygenaseschemistry.chemical_compoundCytochrome P-450 Enzyme SystemPiperidinesOral administrationDesipraminemedicineHumansDrug InteractionsPharmacology (medical)Chromatography High Pressure LiquidPharmacologyDetection limitChromatographyParoxetineParoxetineCytochrome P-450 CYP2D6chemistryFemaleQuantitative analysis (chemistry)medicine.drugTherapeutic Drug Monitoring
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Improved antifouling properties and selective biofunctionalization of stainless steel by employing heterobifunctional silane-polyethylene glycol over…

2016

AbstractA straightforward solution-based method to modify the biofunctionality of stainless steel (SS) using heterobifunctional silane-polyethylene glycol (silane-PEG) overlayers is reported. Reduced nonspecific biofouling of both proteins and bacteria onto SS and further selective biofunctionalization of the modified surface were achieved. According to photoelectron spectroscopy analyses, the silane-PEGs formed less than 10 Å thick overlayers with close to 90% surface coverage and reproducible chemical compositions. Consequently, the surfaces also became more hydrophilic, and the observed non-specific biofouling of proteins was reduced by approximately 70%. In addition, the attachment of E…

Immobilized enzymeBiofoulingSurface PropertiesBiotin02 engineering and technologyPolyethylene glycol010402 general chemistry01 natural sciencesBacterial AdhesionArticleOverlayerPolyethylene GlycolsBiofoulingchemistry.chemical_compoundLääketieteen bioteknologia - Medical biotechnologybiofunctionalitystainless steelMultidisciplinarySilanesbiologyta114Fysiikka - Physical sciences221 Nanotechnologytechnology industry and agriculture217 Medical engineeringSilanes021001 nanoscience & nanotechnologyAvidinSilane0104 chemical scienceschemistryChemical engineering216 Materials engineeringBiotinylationbiology.proteinruostumaton teräs3111 Biomedicine0210 nano-technologyHydrophobic and Hydrophilic InteractionsAvidinProtein BindingScientific Reports
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On the Age of Leprosy

2014

Leprosy is a chronic infection of the skin and nerves caused by Mycobacterium leprae and the newly discovered Mycobacterium lepromatosis. Human leprosy has been documented for millennia in ancient cultures. Recent genomic studies of worldwide M. leprae strains have further traced it along global human dispersals during the past ∼ 100,000 years. Because leprosy bacilli are strictly intracellular, we wonder how long humans have been affected by this disease-causing parasite. Based on recently published data on M. leprae genomes, M. lepromatosis discovery, leprosy bacilli evolution, and human evolution, it is most likely that the leprosy bacilli started parasitic evolution in humans or early h…

Immune defenselcsh:Arctic medicine. Tropical medicinelcsh:RC955-962EpidemiologyImmunologyReviewDermatologymedicine.disease_causeMicrobiologyMycobacteriumLeprosymedicineHumansMycobacterium lepraeBiologyPhylogenyMycobacterium lepromatosisClinical GeneticsbiologyHuman evolutionary geneticslcsh:Public aspects of medicinePublic Health Environmental and Occupational Healthlcsh:RA1-1270Genomicsbiology.organism_classificationmedicine.diseaseBiological EvolutionMycobacterium lepraeChronic infectionInfectious DiseasesHuman evolutionImmunologyHost-Pathogen InteractionsMedicineClinical ImmunologyLeprosyPublic HealthMycobacteriumPLoS Neglected Tropical Diseases
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Toll-like receptors – sentries in the B-cell response

2009

Summary Toll-like receptors (TLR) play a central role in the initiation of the innate immune response to pathogens. Upon recognition of molecular motifs specific for microbial molecules TLR mediate pro-inflammatory cytokine secretion and enhance antigen presentation; in B cells they further promote expansion, class switch recombination and immunoglobulin secretion. As a result of their adjuvant properties, TLR ligands have become an integral component of antimicrobial vaccines. In spite of this, little is known of the direct effects of TLR engagement on B-lymphocyte function. The scope of this review is to outline the differences in TLR expression and reactivity in murine and human B-cell s…

ImmunologyAntigen presentationReview ArticleBiologyImmunoglobulin secretionImmunomodulationMicemedicineImmunology and AllergyAnimalsHumansReceptorB cellB-LymphocytesInnate immune systemToll-Like ReceptorsImmunoglobulin Class SwitchingImmunity InnateCell biologymedicine.anatomical_structureImmunoglobulin class switchingImmunologyAntibody FormationHost-Pathogen InteractionsCytokine secretionFunction (biology)
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Novel Paraoxonase 2-Dependent Mechanism Mediating the Biological Effects of the Pseudomonas aeruginosa Quorum-Sensing Molecule N-(3-Oxo-Dodecanoyl)-l…

2015

ABSTRACT Pseudomonas aeruginosa produces N -(3-oxo-dodecanoyl)- l -homoserine lactone (3OC12), a crucial signaling molecule that elicits diverse biological responses in host cells thought to subvert immune defenses. The mechanism mediating many of these responses remains unknown. The intracellular lactonase paraoxonase 2 (PON2) hydrolyzes and inactivates 3OC12 and is therefore considered a component of host cells that attenuates 3OC12-mediated responses. Here, we demonstrate in cell lines and in primary human bronchial epithelial cells that 3OC12 is rapidly hydrolyzed intracellularly by PON2 to 3OC12 acid, which becomes trapped and accumulates within the cells. Subcellularly, 3OC12 acid acc…

ImmunologyBlotting WesternHomoserineMitochondrionMicrobiologyCell LineHost-Parasite Interactionschemistry.chemical_compoundLactonesLactonaseHomoserineHumansImmunoprecipitationPseudomonas InfectionsChromatography High Pressure LiquidCellular Microbiology: Pathogen-Host Cell Molecular InteractionsMicroscopy ConfocalbiologyKinaseAryldialkylphosphataseQuorum SensingQuorum sensingCytosolInfectious DiseasesBiochemistrychemistryPseudomonas aeruginosabiology.proteinPhosphorylationParasitologyRNA InterferenceIntracellular
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Inhibition of Transfer to Secondary Receptors by Heparan Sulfate-Binding Drug or Antibody Induces Noninfectious Uptake of Human Papillomavirus

2007

ABSTRACT Infection with various human papillomaviruses (HPVs) induces cervical cancers. Cell surface heparan sulfates (HS) have been shown to serve as primary attachment receptors, and molecules with structural similarity to cell surface HS, like heparin, function as competitive inhibitors of HPV infection. Here we demonstrate that the N , N ′-bisheteryl derivative of dispirotripiperazine, DSTP27, efficiently blocks papillomavirus infection by binding to HS moieties, with 50% inhibitory doses of up to 0.4 μg/ml. In contrast to short-term inhibitory effects of heparin, pretreatment of cells with DSTP27 significantly reduced HPV infection for more than 30 h. Using DSTP27 and heparinase, we fu…

ImmunologyEndocytosisBinding CompetitiveMicrobiologyAntibodiesCell LineExtracellular matrixLamininVirologyHumansReceptorPapillomaviridaeOxadiazolesHeparinasebiologyMolecular biologyEndocytosisVirus-Cell InteractionsPyrimidinesEndocytic vesicleCell cultureInsect Sciencebiology.proteinReceptors VirusHeparan sulfate bindingHeparitin SulfateHeparan Sulfate ProteoglycansJournal of Virology
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Complex Cellular Responses of Helicobacter pylori-Colonized Gastric Adenocarcinoma Cells ▿

2011

ABSTRACT Helicobacter pylori is an important class I carcinogen that persistently infects the human gastric mucosa to induce gastritis, gastric ulceration, and gastric cancer. H. pylori pathogenesis strongly depends on pathogenic factors, such as VacA (vacuolating cytotoxin A) or a specialized type IV secretion system (T4SS), which injects the oncoprotein CagA (cytotoxin-associated gene A product) into the host cell. Since access to primary gastric epithelial cells is limited, many studies on the complex cellular and molecular mechanisms of H. pylori were performed in immortalized epithelial cells originating from individual human adenocarcinomas. The aim of our study was a comparative anal…

ImmunologyImmunoblottingAdenocarcinomaMicrobiologyHelicobacter InfectionsStomach NeoplasmsCell Line TumormedicineGastric mucosaCell AdhesionCagAHumansImmunoprecipitationSecretionInterleukin 8Cell adhesionAuthor CorrectionbiologyHelicobacter pyloriReverse Transcriptase Polymerase Chain ReactionInterleukin-8Bacterial InfectionsHelicobacter pylorimedicine.diseasebiology.organism_classificationbacterial infections and mycosesdigestive system diseasesInfectious Diseasesmedicine.anatomical_structureCell cultureBacterial TranslocationImmunologyHost-Pathogen InteractionsCancer researchAdenocarcinomaParasitology
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Human papillomavirus infection requires cell surface heparan sulfate.

2001

ABSTRACT Using pseudoinfection of cell lines, we demonstrate that cell surface heparan sulfate is required for infection by human papillomavirus type 16 (HPV-16) and HPV-33 pseudovirions. Pseudoinfection was inhibited by heparin but not dermatan or chondroitin sulfate, reduced by reducing the level of surface sulfation, and abolished by heparinase treatment. Carboxy-terminally deleted HPV-33 virus-like particles still bound efficiently to heparin. The kinetics of postattachment neutralization by antiserum or heparin indicated that pseudovirions were shifted on the cell surface from a heparin-sensitive into a heparin-resistant mode of binding, possibly involving a secondary receptor. Alpha-6…

ImmunologyIntegrinIntegrin alpha6Microbiologychemistry.chemical_compoundSulfationAntigens CDVirologymedicineAnimalsHumansChondroitin sulfateReceptorNeural Cell Adhesion MoleculesPapillomaviridaeAntiserumHeparinaseMembrane GlycoproteinsbiologyHeparinVirionHeparan sulfateHeparinMolecular biologyVirus-Cell InteractionschemistryInsect ScienceCOS Cellsbiology.proteinHeparitin SulfateLeukocyte L1 Antigen Complexmedicine.drugJournal of virology
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Plant virus cell-to-cell movement is not dependent on the transmembrane disposition of its movement protein

2009

ABSTRACT The cell-to-cell transport of plant viruses depends on one or more virus-encoded movement proteins (MPs). Some MPs are integral membrane proteins that interact with the membrane of the endoplasmic reticulum, but a detailed understanding of the interaction between MPs and biological membranes has been lacking. The cell-to-cell movement of the Prunus necrotic ringspot virus (PNRSV) is facilitated by a single MP of the 30K superfamily. Here, using a myriad of biochemical and biophysical approaches, we show that the PNRSV MP contains only one hydrophobic region (HR) that interacts with the membrane interface, as opposed to being a transmembrane protein. We also show that a proline resi…

ImmunologyMolecular Sequence DataMicrobiologiaBiologyIlarvirusMicrobiologyCell membraneSequence Analysis ProteinVirologymedicineAmino Acid SequenceMovement proteinPeptide sequenceIntegral membrane proteinPhospholipidsEndoplasmic reticulumCircular DichroismCell MembraneProteïnes de membranaBiological membraneVirus InternalizationTransmembrane proteinCell biologyVirus-Cell InteractionsVirusPlant Viral Movement ProteinsMembranemedicine.anatomical_structureBiochemistryInsect ScienceMutationPrunusHydrophobic and Hydrophilic InteractionsSequence Alignment
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Identification of a Dynein Interacting Domain in the Papillomavirus Minor Capsid Protein L2

2006

ABSTRACT Papillomaviruses enter cells via endocytosis (H. C. Selinka et al., Virology 299:279-287, 2002). After egress from endosomes, the minor capsid protein L2 accompanies the viral DNA to the nucleus and subsequently to the subnuclear promyelocytic leukemia protein bodies (P. M. Day et al., Proc. Natl. Acad. Sci. USA 101:14252-14257, 2004), suggesting that this protein may be involved in the intracytoplasmic transport of the viral genome. We now demonstrate that the L2 protein is able to interact with the microtubule network via the motor protein dynein. L2 protein was found attached to microtubules after uncoating of incoming human papillomavirus pseudovirions. Based on immunofluoresce…

ImmunoprecipitationImmunologyDyneinActive Transport Cell NucleusGenome ViralMicrotubulesMicrobiologyMotor proteinPromyelocytic leukemia proteinMicrotubuleDynein ATPaseVirologyHumansPapillomaviridaebiologyPapillomavirus InfectionsDyneinsOncogene Proteins ViralMolecular biologyEndocytosisVirus-Cell InteractionsMicroscopy FluorescenceCapsidInsect ScienceDNA Viralbiology.proteinDynactinCapsid ProteinsIntranuclear SpaceHeLa CellsProtein BindingJournal of Virology
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