Search results for "Endoplasm"

showing 10 items of 323 documents

Protective effect of paraoxonase-2 against endoplasmic reticulum stress-induced apoptosis is lost upon disturbance of calcium homoeostasis

2008

PON2 (paraoxonase-2) is a ubiquitously expressed antioxidative protein which is largely found in the ER (endoplasmic reticulum). Addressing the cytoprotective functions of PON2, we observed that PON2 overexpression provided significant resistance to ER-stress-induced caspase 3 activation when the ER stress was induced by interference with protein modification (by tunicamycin or dithiothreitol), but not when ER stress was induced by disturbance of Ca2+ homoeostasis (by thapsigargin or A23187). When analysing the underlying molecular events, we found an activation of the PON2 promoter in response to all tested ER-stress-inducing stimuli. However, only tunicamycin and dithiothreitol resulted i…

ThapsigarginRNA StabilityApoptosisCaspase 3Protein degradationEndoplasmic ReticulumBiochemistryGene Expression Regulation EnzymologicCell Linechemistry.chemical_compoundStress PhysiologicalHomeostasisHumansEnzyme InhibitorsPromoter Regions Genetic3' Untranslated RegionsMolecular BiologyCalcimycinIonophoresbiologyAryldialkylphosphataseCalpainTunicamycinEndoplasmic reticulumCalpainCell BiologyTunicamycinCell biologyDithiothreitolchemistryApoptosisbiology.proteinUnfolded protein responseThapsigarginCalcium5' Untranslated RegionsBiochemical Journal
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Modulation of intracellular calcium concentrations and T cell activation by prickly pear polyphenols.

2004

Opuntia ficus indica (prickly pear) polyphenolic compounds (OFPC) triggered an increase in [Ca2+]i in human Jurkat T-cell lines. Furthermore, OFPC-induced rise in [Ca2+]i was significantly curtailed in calcium-free buffer (0% Ca2+) as compared to that in 100% Ca2+ medium. Preincubation of cells with tyrphostin A9, an inhibitor of Ca2+ release-activated Ca2+ (CRAC) channels, significantly diminished the OFPC-induced sustained response on the increases in [Ca2+]i. Lanthanum and nifedipine, the respective inhibitors of voltage-dependent and L-type calcium channels, failed to curtail significantly the OFPC-induced calcium response. As OFPC still stimulated increases in [Ca2+]i in 0% Ca2+ medium…

ThapsigarginT-LymphocytesClinical Biochemistrychemistry.chemical_elementGene ExpressionBiologyCalciumLymphocyte ActivationCalcium in biologyMembrane Potentialschemistry.chemical_compoundJurkat CellsPhenolsmedicineHumansCalcium SignalingRNA MessengerMolecular BiologyCalcium signalingCalcium metabolismFlavonoidsVoltage-dependent calcium channelDose-Response Relationship DrugPlant ExtractsReverse Transcriptase Polymerase Chain ReactionEndoplasmic reticulumOpuntiaPolyphenolsCell BiologyGeneral MedicineTyrphostinsMechanism of actionBiochemistrychemistryBiophysicsInterleukin-2ThapsigarginCalciummedicine.symptomMolecular and cellular biochemistry
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Regulation of calcium signalling by docosahexaenoic acid in human T-cells: implication of CRAC channels

2000

Abstract We elucidated the role of docosahexaenoic acid (DHA) on the increases in free intracellular calcium concentrations, [Ca2+]i, in human (Jurkat) T-cell lines. DHA evoked an increase in [Ca2+]i in a dose-dependent manner in these cells. Anti-CD3 antibody, known to stimulate increases in Ca2+ from endoplasmic reticulum (ER) via the production of inositol trisphosphate, also evoked increases in [Ca2+]i in Jurkat T-cells. We also used thapsigargin which inhibits Ca2+-ATPase of the ER and, therefore, increases Ca2+ in the cytosol. Interestingly, addition of DHA during the thapsigargin-induced peak response exerted an additive effect on the increases in [Ca2+]i in human T-cells, indicating…

ThapsigarginVoltage-dependent calcium channelEndoplasmic reticulumchemistry.chemical_elementInositol trisphosphateQD415-436Cell BiologyCalciumpolyunsaturated fatty acidCD3BiochemistryJurkat cellsJurkat T-cellsCalcium in biologyCell biologychemistry.chemical_compoundEndocrinologychemistrythapsigarginCalcium signalingJournal of Lipid Research
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Role of three isoforms of phospholipase A2in capacitative calcium influx in human T-cells

2002

The present study was conducted on human Jurkat T-cell lines in order to elucidate the role of phospholipase A2 in capacitative calcium entry. We have employed thapsigargin (TG) that induces increases in [Ca2+]i by emptying the calcium pool of endoplasmic reticulum, followed by capacitative calcium entry. We designed a Ca2+ free/Ca2+ reintroduction (CFCR) protocol for the experiments, conducted in Ca2+-free medium. By employing CFCR protocol, we observed that addition of exogenous arachidonic acid (AA) stimulated TG-induced capacitative calcium influx. The liberation of endogenous AA and its autocrine action seems to be implicated during TG-induced capacitative calcium influx: TG potentiate…

ThapsigarginbiologyEndoplasmic reticulumchemistry.chemical_elementCalciumBiochemistryJurkat cellsCell biologychemistry.chemical_compoundPhospholipase A2chemistryExtracellularbiology.proteinLiberationArachidonic acidEuropean Journal of Biochemistry
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Tributyltin(Iv) butyrate: A novel epigenetic modifier with er stress-and apoptosis-inducing properties in colon cancer cells

2021

Organotin(IV) compounds are a class of non-platinum metallo-conjugates exhibiting antitumor activity. The effects of different organotin types has been related to several mechanisms, including their ability to modify acetylation protein status and to promote apoptosis. Here, we focus on triorganotin(IV) complexes of butyric acid, a well-known HDAC inhibitor with antitumor properties. The conjugated compounds were synthesized and characterised by FTIR spectroscopy, multi-nuclear (1H, 13C and 119Sn) NMR, and mass spectrometry (ESI-MS). In the triorganotin(IV) complexes, an anionic monodentate butyrate ligand was observed, which coordinated the tin atom on a tetra-coordinated, monomeric enviro…

Triorganotin(IV) butyratesPharmaceutical ScienceOrganic chemistryApoptosisButyrateArticleHistone DeacetylasesAnalytical ChemistryEpigenesis GeneticButyric acidchemistry.chemical_compoundQD241-441HDAC inhibitorsCell Line TumorSettore BIO/10 - BiochimicaDrug DiscoveryHumansPhysical and Theoretical ChemistrybiologyAcetylationLigand (biochemistry)Endoplasmic Reticulum StressColon cancerHistonechemistryBiochemistryHistone acetylationChemistry (miscellaneous)ApoptosisAcetylationSettore CHIM/03 - Chimica Generale E InorganicaColonic NeoplasmsTributyltinbiology.proteinUnfolded protein responseMolecular MedicineButyric AcidTrialkyltin CompoundsER stressProtein Processing Post-Translational
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Papel central de la mitocondria en la hepatotoxicidad inducida por Efavirenz

2013

La toxicidad hepática y los desordenes metabólicos son los principales efectos adversos asociados al tratamiento farmacológico de la infección con el virus de la inmunodeficiencia humana (VIH). El Efavirenz (EFV) es el miembro de la familia de los inhibidores de la transcriptasa inversa no análogos de nucleósidos (ITINAN) más ampliamente utilizado en el tratamiento del VIH. Su uso ha sido asociado con el desarrollo de diversos efectos adversos, entre ellos la hepatotoxicidad, pero los mecanismos celulares y moleculares responsables de su aparición aún no han sido caracterizados, aunque algunos trabajos recientes vinculan su toxicidad con disfunción mitocondrial. En esta tesis, describimos u…

UNESCO::CIENCIAS MÉDICAS ::Farmacología ::Análisis de medicamentosmitocondriaUNESCO::CIENCIAS DE LA VIDA::Biología molecular:CIENCIAS MÉDICAS ::Farmacología [UNESCO]VIHmuerte celularefavirenz:CIENCIAS MÉDICAS ::Farmacología ::Análisis de medicamentos [UNESCO]UNESCO::CIENCIAS DE LA VIDA::Biología celularUNESCO::CIENCIAS MÉDICAS ::Farmacología:CIENCIAS DE LA VIDA::Biología molecular [UNESCO]hepatotoxicidad:CIENCIAS DE LA VIDA::Biología celular [UNESCO]estrés de retículo endoplasmáticomitofagiaautofagia
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Mitochondria and endoplasmic reticulum interplay at the core of efavirenz-induced hepatic effects

2016

El inhibidor de la transcriptasa inversa no análogo de nucleósido efavirenz (EFV) es uno de los fármacos más utilizados en la terapia antirretroviral combinada (TARc) empleada en el tratamiento de la infección por el virus de la inmunodeficiencia humana (VIH). Aunque en general se ha considerado seguro, existe una gran preocupación acerca de los efectos secundarios inducidos por las terapias que contienen EFV. Este fármaco se ha asociado con toxicidad hepática y trastornos metabólicos y, aunque los mecanismos implicados no están claros, evidencias recientes han señalado una acción mitocondrial específica de EFV acompañada por la inducción de estrés de retículo endoplasmático (RE)/respuesta …

UNESCO::CIENCIAS MÉDICASVIH efavirenz toxicidad hepática mitocondria reticulo endoplasmático MAMs LONP1:CIENCIAS MÉDICAS [UNESCO]
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Targeting V-ATPase in primary human monocytes by archazolid potently represses the classical secretion of cytokines due to accumulation at the endopl…

2014

The macrolide archazolid inhibits vacuolar-type H(+)-ATPase (V-ATPase), a proton-translocating enzyme involved in protein transport and pH regulation of cell organelles, and potently suppresses cancer cell growth at low nanomolar concentrations. In view of the growing link between inflammation and cancer, we investigated whether inhibition of V-ATPase by archazolid may affect primary human monocytes that can promote cancer by sustaining inflammation through the release of tumor-promoting cytokines. Human primary monocytes express V-ATPase, and archazolid (10-100nM) increases the vesicular pH in these cells. Archazolid (10nM) markedly reduced the release of pro-inflammatory (TNF-α, interleuk…

Vacuolar Proton-Translocating ATPasesmedicine.medical_specialtyp38 mitogen-activated protein kinasesInflammationBiologyEndoplasmic ReticulumBiochemistryMonocytesCell Linechemistry.chemical_compoundInternal medicinemedicineHumansSecretionPhosphorylationProtein kinase BDNA PrimersPharmacologyBase SequenceDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionEndoplasmic reticulumBafilomycinCell biologyIκBαEndocrinologySecretory proteinMicroscopy FluorescencechemistryCytokinesMacrolidesmedicine.symptomSignal TransductionBiochemical Pharmacology
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Membrane topology and post-translational modification of the Saccharomyces cerevisiae essential protein Rot1.

2007

ROT1 is an essential gene that has been related to cell wall biosynthesis, the actin cytoskeleton and protein folding. In order to help to understand its molecular function, we carried out a characterization of the Rot1 protein. It is primarily located at the endoplasmic reticulum-nuclear membrane facing the lumen. Rot1 migrates more slowly than expected, which might suggest post-translational modification. Our results indicate that Rot1 is a protein that is neither GPI-anchored nor O-glycosylated. In contrast, it is N-glycosylated. By a directed mutagenesis of several Asn residues, we identified that the protein is simultaneously glycosylated at N103, N107 and N139. Although the mutation o…

Vesicle-associated membrane protein 8Saccharomyces cerevisiae ProteinsMolecular Sequence DataBioengineeringmacromolecular substancesSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumApplied Microbiology and BiotechnologyBiochemistryProtein structureSEC62Gene Expression Regulation FungalGeneticsAmino Acid SequenceCell MembraneMembrane ProteinsActin cytoskeletonCell biologyTransport proteinProtein Structure TertiaryTransmembrane domainProtein TransportBiochemistryMembrane topologyProtein foldingProtein Processing Post-TranslationalBiotechnologyMolecular ChaperonesYeast (Chichester, England)
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Endoplasmic Reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs

2013

AbstractExit from the Endoplasmic Reticulum (ER) of newly synthesized proteins is mediated by COPII vesicles that bud from the ER at the ER Exit Sites (ERESs). Disruption of ER homeostasis causes accumulation of unfolded and misfolded proteins in the ER. This condition is referred to as ER stress. Previously, we demonstrated that ER stress rapidly impairs the formation of COPII vesicles. Here, we show that membrane association of COPII components, and in particular of Sec23a, is impaired by ER stress-inducing agents suggesting the existence of a dynamic interplay between protein folding and COPII assembly at the ER.

Vesicular Transport ProteinsBiophysicsEndoplasmic ReticulumBiochemistryCell LineVesicular Transport ProteinGeneticStructural BiologyERESGeneticsVesicular Transport ProteinsHumansCOPIIEndoplasmic Reticulum StreMolecular BiologyCOPIIChemistryVesicleEndoplasmic reticulumSec23Cell BiologyCOP-Coated VesiclesSEC23AEndoplasmic Reticulum StressCell biologyBiophysicUnfolded protein responseER streProtein foldingCOP-Coated VesiclesER stressCOP-Coated VesicleHumanProtein BindingFEBS Letters
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