Search results for "cytochrome c"

showing 10 items of 129 documents

Cajanol, a novel anticancer agent from Pigeonpea [Cajanus cajan (L.) Millsp.] roots, induces apoptosis in human breast cancer cells through a ROS-med…

2010

Cajanol (5-hydroxy-3-(4-hydroxy-2-methoxyphenyl)-7-methoxychroman-4-one) is an isoflavanone from Pigeonpea [Cajanus cajan (L.) Millsp.] roots. As the most effective phytoalexin in pigeonpea, the cytotoxic activity of cajanol towards cancer cells has not been report as yet. In the present study, the anticancer activity of cajanol towards MCF-7 human breast cancer cells was investigated. In order to explore the underlying mechanism of cell growth inhibition of cajanol, cell cycle distribution, DNA fragmentation assay and morphological assessment of nuclear change, ROS generation, mitochondrial membrane potential (DeltaPsim) disruption, and expression of caspase-3 and caspase-9, Bax, Bcl-2, PA…

Cell growthCytochrome cApoptosisBreast NeoplasmsGeneral MedicineMitochondrionCell cycleBiologyToxicologyFlow CytometryMolecular biologyAntineoplastic Agents PhytogenicIsoflavonesPlant RootsMitochondriaCajanusCell cultureApoptosisCell Line TumorCancer cellbiology.proteinCytotoxic T cellHumansFemaleReactive Oxygen SpeciesChemico-biological interactions
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U937 variant cells as a model of apoptosis without cell disintegration

2012

AbstractThe variant cell line U937V was originally identified by a higher sensitivity to the cytocidal action of tumor necrosis factor alpha (TNFα) than that of its reference cell line, U937. We noticed that a typical morphological feature of dying U937V cells was the lack of cellular disintegration, which contrasts to the formation of apoptotic bodies seen with dying U937 cells. We found that both TNFα, which induces the extrinsic apoptotic pathway, and etoposide (VP-16), which induces the intrinsic apoptotic pathway, stimulated U937V cell death without cell disintegration. In spite of the distinct morphological differences between the U937 and U937V cells, the basic molecular events of ap…

Cell typeProgrammed cell deathBlotting WesternCellApoptosisU937 cellsDNA FragmentationBiologyModels BiologicalBiochemistrymedicineHumansCell ShapeMolecular BiologyU937 cellCytochrome cCytochromes chemic and immune systemsCell BiologyApoptotic bodyCaspase 9MitochondriaCell biologyEnzyme Activationmedicine.anatomical_structureApoptosisCell culturebiology.proteinApoptotic bodiesLymphoma Large B-Cell DiffuseCell disintegrationSignal TransductionResearch ArticleCellular and Molecular Biology Letters
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Comparative study of capillary electroendosmotic chromatography and electrically assisted gradient nano-liquid chromatography for the separation of p…

2000

Capillary electroendoendosmotic chromatography (CEC), being a hybrid of high-performance liquid chromatography (HPLC) and capillary electrophoresis, offers considerable changes to enhance column efficiency, speed of analysis and additional selectivity as compared to the parent methods. The analytes are driven by the electroendosmotic flow (EOF) and separated by surface-solute interactions as well as by differences in electromigration. In this paper on the separation of peptides on C18 reversed-phase and mixed-mode (sulphonic acid-n-alkyl) packings in CEC and electrically assisted reversed-phase gradient nano-LC are investigated. It is shown that mixed mode packings generate a higher EOF tha…

ChromatographyElutionChemistryOrganic ChemistryAnalytical chemistryElectrophoresis CapillaryCytochrome c GroupGeneral MedicineReversed-phase chromatographyHydrogen-Ion ConcentrationBiochemistryHigh-performance liquid chromatographyAngiotensin IIAnalytical ChemistryCapillary electrophoresisColumn chromatographyMixed-mode chromatographyElectrochromatographyPeptidesChromatography High Pressure LiquidJournal of chromatography. A
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Staining mitochondria in Saccharomyces cerevisiae.

1969

After testing various procedures (amidoblack 10B, acid fuchsin-methyl blue, Luxol fast blue MBS-phloxine, toluidine blue O, Jams green B and pinacyanol), three stains can be recommended for staining both types of mitochondria (globose and threadlike) in the cells of Saccharomyces cerevisiae: (1) 0.1% solution of amidoblack 10B in citrate buffer (pH 3.0) for 10 min; (2) 0.01% solution of toluidine blue O in phosphate buffer (pH 6.0) for 30 min; (3) 0.01% solution of Janus green B in distilled water (pH 5.6) for 30 min. The latter stain is most specific because its staining reaction depends upon the action of the mitochondrial enzyme cytochrome c oxidase. Yet, low concentrations and short inc…

ChromatographyTime FactorsStaining and LabelingJanus Green BSaccharomyces cerevisiaeBiologyBuffersHydrogen-Ion Concentrationbiology.organism_classificationStainLuxol fast blue stainStainingMitochondriaElectron Transport Complex IVchemistry.chemical_compoundSaccharomyceschemistryBiochemistryDistilled waterbiology.proteinMethodsCytochrome c oxidaseAnatomyColoring AgentsIncubationStain technology
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FERULIC ACID INHIBITS OXIDATE STRESS AND CELL DEATH INDUCED BY Ab OLIGOMERS: IMPROVED DELIVERY BY SOLID LIPID NANOPARTICLES.

2009

Oxidative stress and dysfunctional mitochondria are among the earliest events in AD, triggering neurodegeneration. The use of natural antioxidants could be a neuroprotective strategy for blocking cell death. Here, the antioxidant action of ferulic acid (FA) on different paths leading to degeneration of recombinant beta-amyloid peptide (rAbeta42) treated cells was investigated. Further, to improve its delivery, a novel drug delivery system (DDS) was used. Solid lipid nanoparticles (SLNs), empty or containing ferulic acid (FA-SNL), were developed as DDS. The resulting particles had small colloidal size and highly negative surface charge in water. Using neuroblastoma cells and rAbeta42 oligome…

Coumaric AcidsMitochondrionmedicine.disease_causeBiochemistryAntioxidantsFerulic acidchemistry.chemical_compoundAlzheimer DiseaseCell Line TumorSolid lipid nanoparticlemedicineHumansViability assayMembrane Potential MitochondrialNeuronsAmyloid beta-PeptidesCell DeathbiologyCytochrome cCytochromes cFERULIC ACID Ab OLIGOMERS LIPID NANOPARTICLES DELIVERY SYSTEM.General MedicineLipidsPeptide FragmentsRecombinant ProteinsMitochondriaOxidative StressBiochemistrychemistrySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoDrug deliveryBiophysicsbiology.proteinNanoparticlesPeroxiredoxinOxidative stress
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Data from: Cuticular hydrocarbons as potential mediators of cryptic species divergence in a mutualistic ant association

2019

Upon advances in sequencing techniques, more and more morphologically identical organisms are identified as cryptic species. Often, mutualistic interactions are proposed as drivers of diversification. Species of the Neotropical parabiotic ant association between Crematogaster levior and Camponotus femoratus are known for highly diverse cuticular hydrocarbon (CHC) profiles, which in insects serve as desiccation barrier but also as communication cues. In the present study we investigated the association of the ants’ CHC profiles to genotypes and morphological traits, and discovered cryptic species pairs in both genera. To assess putative niche differentiation between the cryptic species, we c…

Crematogaster leviorcytochrome c oxidase subunit ICamponotus femoratusBarcoding
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Evidence for the operation of a cyanide-sensitive oxidase in chlororespiration in the thylakoids of the chlorophyll c-containing alga Pleurochloris m…

1995

For characterisation of chlororespiration in the chlorophyll c-containing alga Pleurochloris meiringensis, we measured the flash-induced electrochromic absorbance changes between 470 and 545 nm and the redox changes of cytochrome f and cytochrome c553. Cytochrome c553 was shown to be present in high amounts (1 mol cytochrome c553 per 300 mol chlorophyll) in this alga and to function as the obligate electron donor for photosystem I instead of plastocyanin. Whereas salicylhydroxamic acid had no effect on the flash-induced absorbance transients, cyanide enhanced the slow-rising (t1/2≈10 ms) kinetic component of the electrochromic absorbance change. Cyanide also accelerated the re-reduction of …

Cytochrome fOxidase testbiologyCytochromeCytochrome b6f complexCytochrome cCyanidePlant ScienceChlororespirationPhotochemistrychemistry.chemical_compoundchemistryGeneticsbiology.proteinPlastocyaninPlanta
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NADPH-cytochrome P-450 reductase: Preferential inhibition by ellipticine and other type II compounds having little effect on NADPH-cytochrome c reduc…

1980

Abstract Ellipticine (5,11-dimethyl-[6H]-pyrido[4,3b]carbazole) binds with an affinity greater than most other compounds known to interact with P-450. Control and 3-methylcholanthrene-induced aryl hydrocarbon (benzo[ a ]pyrene) hydroxylase (EC 1.14.14.2) and acetanilide 4-hydroxylase and control and phenobarbital-induced ethylmorphine N -demethylase activities are all markedly inhibited by ellipticine to about the same extent. Ellipticine and other Type II compounds (metyrapone, octylamine-1, pyridine and aniline) preferentially inhibit NADPH-cytochrome P-450 reductase activity, while affecting NADPH-cytochrome c reductase activity very little. Butanol-1, a compound having pure Reverse Type…

CytochromeStereochemistryIn Vitro TechniquesReductaseBiochemistryMixed Function OxygenasesMicechemistry.chemical_compoundAlkaloidsCytochrome P-450 Enzyme SystemAnimalsEllipticinesBenzopyrenesBinding siteAcetanilideNADPH-Ferrihemoprotein ReductasePharmacologychemistry.chemical_classificationbiologyCytochrome cDNAElectron acceptorchemistryMicrosomes Liverbiology.proteinMicrosomePyreneBiochemical Pharmacology
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Cytochrome c is released in a single step during apoptosis

2005

Release of cytochrome c from mitochondria is a central event in apoptotic signaling. In this study, we utilized a cytochrome c fusion that binds fluorescent biarsenical ligands (cytochrome c-4CYS (cyt. c-4CYS)) as well as cytochrome c-green fluorescent protein (cyt. c-GFP) to measure its release from mitochondria in different cell types during apoptosis. In single cells, the kinetics of cyt. c-4CYS release was indistinguishable from that of cyt. c-GFP in apoptotic cells expressing both molecules. Lowering the temperature by 7 degrees C did not affect this corelease, but further separated cytochrome c release from the subsequent decrease in mitochondrial membrane potential (DeltaPsi(m)). Cyt…

CytochromeUltraviolet RaysGreen Fluorescent ProteinsApoptosisLigandsMembrane PotentialsJurkat CellsCytochrome C1HumansCytochrome c oxidaseEnzyme InhibitorsMolecular BiologyProtein Synthesis InhibitorsMicroscopy VideobiologyTumor Necrosis Factor-alphaCytochrome bCytochrome cTemperatureCytochromes cCytochrome P450 reductaseCell BiologyStaurosporineMitochondriaCell biologyKineticsenzymes and coenzymes (carbohydrates)Coenzyme Q – cytochrome c reductaseDactinomycinbiology.proteinApoptosomeBiomarkersHeLa CellsCell Death & Differentiation
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Analysis of cytochrome C oxidase subunits III and IV expression in developing rat brain

2004

Abstract Cytochrome c oxidase (COX) complex is built up with both nucleus- and mitochondrion-encoded subunits. Biogenesis and assembly of the complex thus requires fine cross-talk between the two compartments. In order to shed light on the regulation of nuclear–mitochondrial interactions, we studied the expression of COXIII (mitochondrion-encoded) and COXIV (nucleus-encoded) in adult rat tissues and rat developing brain. We found that the levels of COXIV protein and mRNA are not linearly related, thus suggesting a post-transcriptional mode of regulation. In agreement with this observation, we report the presence of a protein that specifically binds to the 3′-untranslated region of COXIV mRN…

CytoplasmRNA-binding proteinProtein subunitBlotting WesternCOX IVRNA-binding proteinMitochondrionBiologyGene Expression Regulation EnzymologicElectron Transport Complex IVAnimalsCytochrome c oxidaseElectrophoresis Gel Two-DimensionalCOX III.RNA MessengerRNA Processing Post-TranscriptionalMessenger RNAGeneral NeuroscienceBrainProteinsRNABlotting NorthernMitochondriaRatsProtein TransportCytosolnucleus-mitochondrion cross-talkBiochemistryCytoplasmbiology.proteinNeuroscience
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