Search results for "mito"

showing 10 items of 2513 documents

Involvement of nitric oxide in the mitochondrial action of efavirenz: a differential effect on neurons and glial cells

2014

Abstract The anti-human immunodeficiency virus (HIV) drug efavirenz (EFV) alters mitochondrial function in cultured neurons and glial cells. Nitric oxide (NO) is a mediator of mitochondrial dysfunction associated with HIV central nervous system symptoms. We show that EFV promotes inducible nitric oxide synthase (iNOS) expression in cultured glial cells and generated NO undermines their mitochondrial function, as inhibition of NOS partially reverses this effect. EFV inhibits mitochondrial Complex I in both neurons and glia; however, when the latter cells are treated for longer periods, other mitochondrial complexes are also affected in accordance with the increased NO production. These findi…

CyclopropanesNNRTIEfavirenzAnti-HIV AgentsCentral nervous systemNitric Oxide Synthase Type IIMitochondrionBiologyNitric OxideNitric oxideCell Linechemistry.chemical_compoundMediatornitric oxidemedicineImmunology and AllergyHumansNeuronsNeurotoxicityelectron transport chainHIVefavirenzmedicine.diseasecentral nervous systemCell biologyBenzoxazinesMitochondriaNitric oxide synthasemitochondriaInfectious Diseasesmedicine.anatomical_structurechemistryAlkynesImmunologybiology.proteinNeurogliaNeuroglia
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Mitochondrial DNA variation of Drosophila obscura (Diptera: Drosophilidae) across Europe

2022

Drosophila obscura is a common fruit fly that inhabits the temperate forests of Europe. While it is abundant in the north compared to other Drosophila, its density decreases southwards, where it is gradually replaced by other Drosophila species. This study describes variation in the mitochondrial Cyt b gene of D. obscura from several European populations. We observed a large number of haplotypes, together with the structuring of genetic variation. Genetic variation is higher in the west where O1 and related divergent haplotypes dominate. In the east, the O2 haplotype is most frequent, together with haplotypes that recently arose from it. In the central part of the species range, both O1 and…

Cyt bfylogeografiamitokondrio-DNAmahlakärpäsetInsect Sciencegenetic variationpopulation expansionphylogeographygeneettinen muuntelugeneettinen monimuotoisuus
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Bleomycin genotoxicity alteration by glutathione and cytochrome P-450 cellular content in respiratory proficient and deficient strains of Saccharomyc…

1999

The genotoxic effects of the antiblastic drug bleomycin were studied in the D7 strain of Saccharomyces cerevisiae and on its derivative mitochondrial mutant rho degree at different cellular concentrations of two drug metabolizing systems, glutathione (GSH) and cytochrome P-450. Bleomycin mutagenic activity was evaluated as frequencies of mitotic gene conversion, reversion and total aberrations under different physiological conditions. In the D7 strain, petite mutant induction was also detected. This is important due to the role of the mitochondrial genome in cancer induction, ageing and degenerative diseases. Both strains showed higher convertant than revertant induction. At high cytochrome…

CytochromeHealth Toxicology and MutagenesisSaccharomyces cerevisiaeMutantRespiratory chainCell Culture TechniquesSaccharomyces cerevisiaeToxicologymedicine.disease_causeBleomycinDNA Mitochondrialchemistry.chemical_compoundBleomycinOxygen ConsumptionCytochrome P-450 Enzyme SystemGeneticsmedicinePoint MutationGenetics (clinical)Chromosome AberrationsRecombination GeneticbiologyDose-Response Relationship DrugMutagenicity TestsCytochrome P450Glutathionebiology.organism_classificationGlutathioneBiochemistrychemistryMutagenesisbiology.proteinGenotoxicityMutagenesis
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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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Nuclear and Cytoplasmic Survivin: Molecular Mechanism, Prognostic, and Therapeutic Potential.

2007

Abstract Survivin's proposed dual role as an apoptosis inhibitor and a mitotic effector positioned it in the front line of cancer research. Notably, survivin is detected as a cytoplasmic and nuclear protein in cancer patients, which stimulated numerous studies to investigate and to speculate on the functional and prognostic significance of its dynamic localization. Recent evidence shows that the direct interaction of survivin with the nuclear export receptor Crm1 is critically involved in its intracellular localization and cancer-relevant functions. Here, we review our current understanding of the Crm1/survivin interface and discuss its potential prognostic and therapeutic relevance. [Cance…

CytoplasmCancer ResearchPathologymedicine.medical_specialtyApoptosis InhibitorSurvivinActive Transport Cell NucleusMitosisReceptors Cytoplasmic and NuclearKaryopherinsBiologyModels BiologicalInhibitor of Apoptosis ProteinsNeoplasmsSurvivinmedicineHumansNuclear proteinNuclear export signalReceptorMitosisCell NucleusEffectorCancerPrognosismedicine.diseaseNeoplasm ProteinsGene Expression Regulation NeoplasticOncologyCancer researchMicrotubule-Associated ProteinsBiologie
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Activation and translocation of p38 mitogen-activated protein kinase after stimulation of monocytes with contact sensitizers.

2002

Recently we described the induction of tyrosine phosphorylation by contact sensitizers as an early molecular event during the activation of antigen- presenting cells. In this study, the role of the p38 mitogen-activated protein kinase for the activation of human monocytes after exposure to four structurally unrelated contact sensitizers was analyzed in comparison with the irritant benzalkonium chloride and an inductor of oxidative stress (H 2 O 2 ) using immunofluorescence, Western blotting, and enzyme-linked immunosorbent assay techniques. Bio chemical analysis revealed a translocation of p38 from the cytoplasm to the detergent-resistant cell fraction only upon stimulation with contact sen…

CytoplasmMAP Kinase Signaling SystemPyridinesp38 mitogen-activated protein kinasesDermatologyBiologyIn Vitro TechniquesBiochemistryp38 Mitogen-Activated Protein KinasesMonocyteschemistry.chemical_compoundProto-Oncogene ProteinsHumansEnzyme InhibitorsPhosphorylationProtein kinase ATranscription factorMolecular Biologyets-Domain Protein Elk-1KinaseImidazolesTyrosine phosphorylationBiological TransportCell BiologyMolecular biologyDNA-Binding ProteinsEnzyme ActivationIL-1β/irritantchemistryhaptenMitogen-activated protein kinasebiology.proteinIrritantsPhosphorylationSignal transductionMitogen-Activated Protein KinasesBenzalkonium CompoundsHaptenssignal transductionInterleukin-1Transcription FactorsThe Journal of investigative dermatology
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Cytoplasmic microvesicles in chromophobe cell renal carcinoma demonstrated by freeze fracture

1987

In the chromophobe cell type of renal carcinoma, cytoplasmic microvesicles (frequently with "inner vesicles") demonstrable by transmission electron microscopy are one of the most important diagnostic features. The present paper reports on these microvesicles in freeze fracture replicas. Their diameter is mainly between 140 and 300 micron, but smaller and very much larger vesicles may also occur. The vesicle membrane is devoid of, or contains only scanty intramembranous particles. Cytoplasmic invaginations, probably the precursors of "inner vesicles" can also be detected. Connections with the agranular endoplasmic reticulum, mitochondria or other cell components could not be documented. Larg…

CytoplasmPathologymedicine.medical_specialtyKidneyVesicleCellChromophobe cellVacuoleBiologyMitochondrionKidney NeoplasmsMicrovesiclesmedicine.anatomical_structureCytoplasmmedicineFreeze FracturingHumansCarcinoma Renal CellVirchows Archiv B Cell Pathology Including Molecular Pathology
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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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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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