Search results for "Subcellular Fraction"

showing 10 items of 58 documents

Characterization of the cleavage site and function of resulting cleavage fragments after limited proteolysis of Clostridium difficile toxin B (TcdB) …

2005

Clostridium difficiletoxin B (TcdB) is a single-stranded protein consisting of a C-terminal domain responsible for binding to the host cell membrane, a middle part involved in internalization, and the N-terminal catalytic (toxic) part. This study shows that TcdB is processed by a single proteolytic step which cleaves TcdB10463between Leu543and Gly544and the naturally occurring variant TcdB8864between Leu544and Gly545. The cleavage occurs at neutral pH and is catalysed by a pepstatin-sensitive protease localized in the cytoplasm and on the cytoplasmic face of intracellular membranes. The smaller N-terminal cleavage products [63 121 Da (TcdB10463) and 62 761 Da (TcdB8864)] harbour the cytotox…

Endosomemedia_common.quotation_subjectBacterial ToxinsMolecular Sequence DataClostridium difficile toxin BCleavage (embryo)MicrobiologyCricetulusBacterial ProteinsCricetinaeChlorocebus aethiopsAnimalsAmino Acid SequenceInternalizationLungVero CellsCells Culturedmedia_commonHost cell membraneClostridioides difficileChemistryFibroblastsMolecular biologyCytosolBiochemistryGlucosyltransferasesCytoplasmIntracellularPeptide HydrolasesSubcellular FractionsMicrobiology
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Differential subcellular localization of endogenous and transfected soluble epoxide hydrolase in mammalian cells: evidence for isozyme variants

1999

AbstractEndogenous, constitutive soluble epoxide hydrolase in mice 3T3 cells was localized via immunofluorescence microscopy exclusively in peroxisomes, whereas transiently expressed mouse soluble epoxide hydrolase (from clofibrate-treated liver) accumulated only in the cytosol of 3T3 and HeLa cells. When the C-terminal Ile of mouse soluble epoxide hydrolase was mutated to generate a prototypic putative type 1 PTS (-SKI to -SKL), the enzyme targeted to peroxisomes. The possibility that soluble epoxide hydrolase-SKI was sorted slowly to peroxiosmes from the cytosol was examined by stably expressing rat soluble epoxide hydrolase-SKI appended to the green fluorescent protein. Green fluorescent…

Epoxide hydrolase 2animal structuresRecombinant Fusion ProteinsBiophysicsBiologyEpoxide hydrolasePeroxisomeTransfectionBiochemistryIsozymeMicrobodies3T3 cellsGreen fluorescent protein03 medical and health sciencesMiceStructural BiologyGeneticsmedicineAnimalsHumansClofibrateEpoxide hydrolaseMolecular Biology030304 developmental biologyEpoxide HydrolasesMammals0303 health sciences030302 biochemistry & molecular biologyPeroxisome targeting signalCell Biology3T3 CellsPeroxisomeSubcellular localizationMolecular biologyRatsIsoenzymesCytosolmedicine.anatomical_structureBiochemistrySolubilityhuman activitiesHeLa CellsSubcellular FractionsFEBS Letters
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Differential Distribution of Harmonin Isoforms and Their Possible Role in Usher-1 Protein Complexes in Mammalian Photoreceptor Cells

2003

PURPOSE. Human Usher syndrome is the most common form of combined deafness and blindness. Usher type I (USH1), the most severe form, is characterized by profound congenital deafness, constant vestibular dysfunction, and prepubertal onset retinitis pigmentosa. Previous studies have shown that the USH1-proteins myosin VIIa, harmonin, and cadherin 23 interact and form a functional network during hair cell differentiation in the inner ear. The purpose of the present study was to analyze the molecular and cellular functions of these USH1 proteins in the mammalian retina. METHODS. Antibodies to USH1 proteins were generated and used in Western blot analysis of subcellular photoreceptor fractions a…

Gene isoformUsher syndromeBlotting WesternSynaptophysinCell Cycle ProteinsMyosinsBiologyPhotoreceptor cellMiceRetinitis pigmentosaotorhinolaryngologic diseasesmedicineAnimalsProtein IsoformsRats WistarFluorescent Antibody Technique IndirectMicroscopy ImmunoelectronCytoskeletonGeneticsRetinaHair cell differentiationReverse Transcriptase Polymerase Chain ReactionCadherinDyneinsCadherinsmedicine.diseaseeye diseasesRatsCell biologyMice Inbred C57BLCytoskeletal Proteinsmedicine.anatomical_structureMicroscopy FluorescenceMyosin VIIasense organsCarrier ProteinsPhotoreceptor Cells VertebrateSubcellular FractionsInvestigative Opthalmology & Visual Science
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Persistent and Transient Replication of Full-Length Hepatitis C Virus Genomes in Cell Culture

2002

ABSTRACT The recently developed subgenomic hepatitis C virus (HCV) replicons were limited by the fact that the sequence encoding the structural proteins was missing. Therefore, important information about a possible influence of these proteins on replication and pathogenesis and about the mechanism of virus formation could not be obtained. Taking advantage of three cell culture-adaptive mutations that enhance RNA replication synergistically, we generated selectable full-length HCV genomes that amplify to high levels in the human hepatoma cell line Huh-7 and can be stably propagated for more than 6 months. The structural proteins are efficiently expressed, with the viral glycoproteins E1 and…

ImmunologyReplicationGenome ViralHepacivirusBiologyVirus ReplicationMicrobiologyVirusViral ProteinsGene FrequencyVirologyTumor Cells CulturedHumansSubgenomic mRNAchemistry.chemical_classificationEndoplasmic reticulumRNAHepatitis CMolecular biologyNS2-3 proteasechemistryViral replicationCell cultureCulture Media ConditionedInsect ScienceRNA ViralGlycoproteinSubcellular FractionsJournal of Virology
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Structural analysis of Cryptosporidium parvum.

2004

Cryptosporidium parvum(Apicomplexa, formerly Sporozoa) is the causative agent of cryptosporidiosis, an enteric disease of substantial medical and veterinary importance.C. parvumshows a number of unique features that differ from the rest of the class of coccidea in which it is currently grouped taxonomically. Differences occur in the overall structure of the transmission form and the invasive stages of the parasite, its intracellular location, the presence of recently described additional extracellular stages, the host range and target cell tropism, the ability to autoinfection, the nonresponsiveness to anticoccidial drugs, the immune response of the host, and immunochemical and genetic char…

InfectivityCryptosporidium parvumbiologyCryptosporidiumbiology.organism_classificationVirologyImmunohistochemistryApicomplexaCryptosporidium parvumImmune systemMicroscopy Electron TransmissionCell Line Tumorparasitic diseasesIntestine Smallbiology.proteinParasite hostingAnimalsHumansAntibodyInstrumentationTropismSubcellular FractionsMicroscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada
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Reductive and oxidative metabolism of nitrofurantoin in rat liver.

1980

The elimination of nitrofurantoin was studied in the isolated rat liver using a recirculating hemoglobin-free perfusion system. The most rapid clearance of nitrofurantoin (0.1 mM) was found under hypoxia (8 ml/min) or anoxia (11 ml/min) indicating a fast and oxygen-sensitive reductive metabolism. The hepatic elimination of nitrofurantoin under anaerobic conditions apparently is not catalyzed by xanthine oxidase, aldehyde oxidase or cytochrome P-450 as judged from the lack of influence of the inhibitors (0.1 mM) allopurinol, menadione, metyrapone, α-naphthoflavone or of carbon monoxide (50%; v/v). Under aerobic conditions the hepatic clearance of nitrofurantoin is rather low (1 ml/min) indic…

MaleAllopurinolPharmacologyIn Vitro Techniquesurologic and male genital diseasesHydroxylationchemistry.chemical_compoundOxygen ConsumptionMenadionemedicineAnimalsXanthine oxidaseAldehyde oxidaseBiotransformationPharmacologyChemistryGeneral MedicineMetabolismfemale genital diseases and pregnancy complicationsRatsBiochemistryLiverNitrofurantoinNitrofurantoinMicrosomeOxidation-Reductionmedicine.drugSubcellular FractionsNaunyn-Schmiedeberg's archives of pharmacology
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Expression and developmental regulation of the cystine/glutamate exchanger (xc-) in the rat.

2007

The cystine/glutamate exchanger (antiporter x c − ) is a membrane transporter involved in the uptake of cystine, the rate-limiting amino acid in the synthesis of glutathione. Recent studies suggest that the antiporter plays a role in the slow oxidative excitotoxity and in the pathological effects of β-N-oxalylamino-l-alanine, the molecule responsible for neurolathyrism, a neurotoxic upper motor neuron disease. The mouse cystine/glutamate exchanger has been cloned and showed to be composed of two distinct proteins, one of which being a novel protein, named xCT, of 502 amino acids and 12 putative trans-membrane domains. We have generated and purified a polyclonal antibody to mouse xCT and stu…

MaleAmino Acid Transport SystemsAntiporterProtein subunitBlotting WesternImmunoblottingCystineGlutamic AcidBiologyBiochemistryRats Sprague-DawleyCellular and Molecular Neurosciencechemistry.chemical_compoundMiceWestern blotChlorocebus aethiopsmedicineAnimalsHumansCystine/glutamate exchanger Protein expression Cell cultures Developmenchemistry.chemical_classificationCerebral CortexNeuronsmedicine.diagnostic_testGlutamate receptorGene Expression Regulation DevelopmentalGeneral MedicineGlutathioneFibroblastsImmunohistochemistryAmino acidRatsBiochemistrychemistryAstrocytesCOS CellsCystineSettore MED/26 - NeurologiaElectrophoresis Polyacrylamide GelCell fractionationSubcellular FractionsNeurochemical research
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Synaptosomes: new vesicles for neuronal mitochondrial transplantation

2021

Abstract Background Mitochondrial dysfunction is a critical factor in the onset and progression of neurodegenerative diseases. Recently, mitochondrial transplantation has been advised as an innovative and attractive strategy to transfer and replace damaged mitochondria. Here we propose, for the first time, to use rat brain extracted synaptosomes, a subcellular fraction of isolated synaptic terminal that contains mitochondria, as mitochondrial delivery systems. Results Synaptosome preparation was validated by the presence of Synaptophysin and PSD95. Synaptosomes were characterized in terms of dimension, zeta potential, polydispersity index and number of particles/ml. Nile Red or CTX-FITCH la…

MaleFIS1Mitochondrial DNAlcsh:Medical technologylcsh:BiotechnologyBiomedical EngineeringPharmaceutical ScienceMedicine (miscellaneous)BioengineeringMitochondrionDNA MitochondrialApplied Microbiology and BiotechnologyMembrane Potentials03 medical and health sciencesDrug Delivery Systems0302 clinical medicinelcsh:TP248.13-248.65medicineAnimalsHomeostasisProtein Interaction Domains and MotifsNeurodegenerationDelivery system030304 developmental biologyMitochondrial transplantationSynaptosome0303 health sciencesbiologyChemistryResearchCytochrome cNeurodegenerationSynaptosomes Mitochondria Neurodegeneration Delivery system Mitochondrial transplantationCytochromes cmedicine.diseaseRatsCell biologyMitochondriaTransplantationlcsh:R855-855.5Cytoplasmbiology.proteinMolecular Medicine030217 neurology & neurosurgerySubcellular FractionsSynaptosomes
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Metabolism of apigenin by rat liver phase I and phase II enzymes and by isolated perfused rat liver

2004

The metabolism of apigenin, a low estrogenic flavonoid phytochemical, was investigated in rat using liver models both in vitro (subcellular fractions) and ex vivo (isolated perfused liver). In vitro, phase I metabolism led to the formation of three monohydroxylated derivatives: luteolin which was the major metabolite (K(m) = 22.5 +/- 1.5 microM; V(max) = 5.605 +/- 0.090 nmol/min/mg protein, means +/- S.E.M.), scutellarein, and iso-scutellarein. These oxidative pathways were mediated by cytochrome P450 monooxygenases (P450s). The use of P450 inhibitors and inducers showed that CYP1A1, CYP2B, and CYP2E1 are involved. In vitro studies of phase II metabolism indicated that apigenin underwent co…

MaleFMN ReductaseMetabolite[SDV]Life Sciences [q-bio]Pharmaceutical ScienceIn Vitro TechniquesMethylation030226 pharmacology & pharmacyMass Spectrometry03 medical and health scienceschemistry.chemical_compoundGlucuronides0302 clinical medicineCytochrome P-450 Enzyme SystemAnimalsApigeninEnzyme InhibitorsRats WistarLuteolinBiotransformationChromatography High Pressure LiquidComputingMilieux_MISCELLANEOUS030304 developmental biologyFlavonoidsPharmacologySex Characteristics0303 health sciencesbiologySulfatesScutellareinCytochrome P450MonooxygenaseDiosmetinRats3. Good health[SDV] Life Sciences [q-bio]KineticsLiverBiochemistrychemistryApigeninbiology.proteinRATFemaleSpectrophotometry UltravioletLuteolinNADPDrug metabolismSubcellular Fractions
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Regulation of glutathione metabolism in Ehrlich ascites tumour cells.

1992

Glutathione metabolism was studied in cancer cells during the growth of an Ehrlich ascites tumour. GSH, but not GSSG, content decreases when cell proliferation and the rate of protein synthesis in the tumour decrease. This change correlates with a decrease in the rate of GSH synthesis and an increase in glutathione peroxidase and glutathione S-transferase activities. Glutathione efflux from tumour cells seems to co-ordinate with the rate of GSH synthesis. Cysteine, and not methionine, promotes GSH synthesis in tumour cells. However, changes in the rate of GSH synthesis are not due to limitations in the supply of blood cysteine or to changes in the intracellular amino acid pool of the cancer…

MaleGPX1Glutathione reductaseProtein metabolismMice Inbred StrainsBiologyGlucosephosphate DehydrogenaseBiochemistrychemistry.chemical_compoundMiceMethionineReference ValuesAnimalsAmino AcidsCarcinoma Ehrlich TumorMolecular BiologyCells CulturedGlutathione Transferasechemistry.chemical_classificationGlutathione PeroxidaseGlutathione DisulfideGlutathione peroxidaseCell BiologyGlutathioneGlutathioneAcetylcysteineRatsKineticsGlutathione ReductasechemistryBiochemistryLiverCancer cellGlutathione disulfidesense organsCell DivisionCysteineSubcellular FractionsResearch ArticleThe Biochemical journal
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