Search results for "Cytochrome c Group"

showing 3 items of 13 documents

The apoptotic effects and synergistic interaction of sodium butyrate and MG132 in human retinoblastoma Y79 cells

1999

This study deals with the apoptotic effect exerted on human retinoblastoma Y79 cells by both sodium butyrate and an inhibitor of 26S proteasome [z-Leu-Leu-Leu-CHO (MG132)] and their synergistic effect. Exposure to sodium butyrate (1-4 mM) induced an accumulation of cells in the G2-M phase that was already visible after 24 h of treatment, when morphological and biochemical signs of apoptosis appeared only in a small number of cells (5-10%). Thereafter, the apoptotic effects increased progressively with slow kinetics, reaching a maximum after 72 h of exposure, when they concerned a large fraction of cells (>75% with 4 mM sodium butyrate). Sodium butyrate stimulated the conversion of procaspas…

Proteasome Endopeptidase ComplexTime FactorsLeupeptinsApoptosisCytochrome c GroupCysteine Proteinase InhibitorsProto-Oncogene Proteins c-mycTumor Cells CulturedHumanssodium butyrateLamin Type BCaspase 3Cell CycleNF-kappa BRetinoblastomaNuclear ProteinsFlow CytometryLaminsMitochondriaButyratesKineticsCaspasesI-kappa B ProteinsPoly(ADP-ribose) PolymerasesTumor Suppressor Protein p53Peptide Hydrolases
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Ferricytochrome c encapsulated in silica hydrogels: correlation between active site dynamics and solvent structure.

2003

Ferricytochrome c encapsulated in silica hydrogels has been prepared by the sol-gel technique following, with some modifications, the procedure originally developed by Ellerby et al. (Science 255 1113 (1992)). A suitable preparation of hydrogels enables having both 'wet' and 'dry' samples. Wet samples have a high water content: as the temperature is lowered below approximately 260 K, water freezes and the samples crack. On the contrary, dry samples have a low water content (hydration h approximately equal 0.35): in these conditions water does not freeze even at cryogenic temperatures and the samples remain transparent and non-cracking. The dynamics of ferricytochrome c and its dependence on…

Time FactorsAbsorption spectroscopySilicon dioxideDrug CompoundingAnalytical chemistryBiophysicsSilica GelCapsulesCytochrome c GroupSpectrum Analysis RamanBiochemistrychemistry.chemical_compoundDrug StabilityFreezingAnimalsHorsesWater contentBinding SitesbiologySilica gelSpectrum AnalysisOrganic ChemistryTemperatureActive siteWaterHydrogelsAtmospheric temperature rangeSilicon DioxideSolventKineticschemistrySelf-healing hydrogelsbiology.proteinSolventsBiophysical chemistry
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Effects of vitamin A deficiency on mitochondrial function in rat liver and heart.

2000

The aim of this study was to investigate comparative effects of vitamin A deficiency on respiratory activity and structural integrity in liver and heart mitochondria. Male rats were fed a liquid control diet (control rats) or a liquid vitamin A-deficient diet (vitamin A-deficient rats) for 50 days. One group of vitamin-A deficient rats was refed a control diet for 15 days (vitamin A-recovered rats). To assess the respiratory function of mitochondria the contents of coenzyme Q (ubiquinone, CoQ), cytochrome c and the activities of the whole electron transport chain and of each of its respiratory complexes were evaluated. Chronic vitamin A deficiency promoted a significant increase in the endo…

VitaminMalemedicine.medical_specialtyUbiquinoneRespiratory chainMedicine (miscellaneous)Cytochrome c GroupMitochondria LiverMitochondria HeartElectron Transportchemistry.chemical_compoundRetinoidsInternal medicinemedicineAnimalsVitamin ERespiratory functionNutrition and DieteticsbiologyVitamin A DeficiencyCytochrome cRetinolmedicine.diseaseRatsVitamin A deficiencyEndocrinologyMitochondrial respiratory chainchemistryCoenzyme Q – cytochrome c reductasebiology.proteinThe British journal of nutrition
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