Search results for "Thioredoxin"

showing 10 items of 51 documents

Decreased cell proliferation and higher oxidative stress in fibroblasts from Down Syndrome fetuses. Preliminary study

2013

Abstract Down Syndrome is the most common chromosomal disease and is also known for its decreased incidence of solid tumors and its progeroid phenotype. Cellular and systemic oxidative stress has been considered as one of the Down Syndrome phenotype causes. We correlated, in a preliminary study, the fibroblast proliferation rate and different cell proliferation key regulators, like Rcan1 and the telomere length from Down Syndrome fetuses, with their oxidative stress profile and the Ribonucleic acid and protein expression of the main antioxidant enzymes together with their activity. Increased oxidized glutathione/glutathione ratio and high peroxide production were found in our cell model. Th…

Malemedicine.medical_specialtyAntioxidantmedicine.medical_treatmentPrimary Cell CultureSuperoxide dismutasemedicine.disease_causeSuperoxide dismutasechemistry.chemical_compoundFetusSuperoxide Dismutase-1ThioredoxinsInternal medicineGlutaredoxinmedicineHumansThioredoxinMolecular BiologyGlutaredoxinsCell ProliferationSkinchemistry.chemical_classificationReactive oxygen speciesGlutathione PeroxidaseTelomere lengthbiologyGlutathione peroxidaseTelomere HomeostasisGlutathioneRcan1FibroblastsTelomereCatalaseGlutathioneProgeroidOxidative StressEndocrinologychemistryBiochemistryGene Expression Regulationbiology.proteinMolecular MedicineFemaleThioredoxinDown SyndromeOxidative stressSignal TransductionBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
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Mitochondrial dynamics in type 2 diabetes: Pathophysiological implications

2017

Mitochondria play a key role in maintaining cellular metabolic homeostasis. These organelles have a high plasticity and are involved in dynamic processes such as mitochondrial fusion and fission, mitophagy and mitochondrial biogenesis. Type 2 diabetes is characterised by mitochondrial dysfunction, high production of reactive oxygen species (ROS) and low levels of ATP. Mitochondrial fusion is modulated by different proteins, including mitofusin-1 (MFN1), mitofusin-2 (MFN2) and optic atrophy (OPA-1), while fission is controlled by mitochondrial fission 1 (FIS1), dynamin-related protein 1 (DRP1) and mitochondrial fission factor (MFF). PARKIN and (PTEN)-induced putative kinase 1 (PINK1) partici…

MiD51 mitochondrial dynamics proteins of 51 kDaΔΨm mitochondrial membrane potential0301 basic medicineMitochondrial fission factorClinical BiochemistryMitochondrial DegradationMFN2Review ArticleTXNIP thioredoxin interacting proteinMitochondrial DynamicsBiochemistryAdenosine TriphosphateGRP78 78 kDa glucose-regulated proteinMFF mitochondrial fission factorMFN2 mitofusin 2TRX2 thioredoxin 2Redox biologylcsh:QH301-705.5NF-κB nuclear factor kappa Blcsh:R5-920MitophagyType 2 diabetesDRP1 dynamin-related protein 1FIS1 fission protein 1BNIP3 BCL2/adenovirus E1B 19 kDa interacting protein 3MitochondriaOPA1 optic atrophy 1SIRT1/3 sirtuin 1/3Biochemistrymitochondrial fusionTGF-β1 transforming growth factor-β1Mitochondrial fissionOMM outer mitochondrial membranelcsh:Medicine (General)MiD49 mitochondrial dynamics proteins of 49Nox 4 NADPH oxidase-4IMM inner mitochondrial membraneFIS1ATF6 activating transcription factor 6PINK1mTOR mammalian target of rapamycinCHOP C/EBP homologous proteinBiologymdivi-1 mitochondrial division inhibitor-1Mitochondrial Proteins03 medical and health sciencesROS reactive oxygen speciessXBP1 spliced X-box binding protein 1UCP-1 uncoupling protein-1MFN1 mitofusin 1SOD superoxide dismutaseLC3 1 A/1B-light chain 3HumansPINK1 (PTEN)-induced putative kinase 1S3 15-OxospiramilactoneOrganic ChemistrymtDNA mitochondrial DNAAMPK AMP-activated protein kinase030104 developmental biologyDiabetes Mellitus Type 2Mitochondrial biogenesislcsh:Biology (General)Oxidative stressp38 MAPK p38 mitogen-activated protein kinasep62/SQSTM1 ubiquitin and sequestosome-1Reactive Oxygen SpeciesRedox Biology
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Factors Determining Sensitivity and Resistance of Tumor Cells to Arsenic Trioxide

2012

Previously, arsenic trioxide showed impressive regression rates of acute promyelocytic leukemia. Here, we investigated molecular determinants of sensitivity and resistance of cell lines of different tumor types towards arsenic trioxide. Arsenic trioxide was the most cytotoxic compound among 8 arsenicals investigated in the NCI cell line panel. We correlated transcriptome-wide microarray-based mRNA expression to the IC(50) values for arsenic trioxide by bioinformatic approaches (COMPARE and hierarchical cluster analyses, Ingenuity signaling pathway analysis). Among the identified pathways were signaling routes for p53, integrin-linked kinase, and actin cytoskeleton. Genes from these pathways…

MicroarraysTumor PhysiologyCancer Treatmentlcsh:MedicineToxicologyArsenicalschemistry.chemical_compoundArsenic TrioxideBasic Cancer ResearchRNA NeoplasmArsenic trioxidelcsh:ScienceOligonucleotide Array Sequence AnalysisMultidisciplinaryintegumentary systemCytotoxinsOxidesTransfectionNeoplasm ProteinsGene Expression Regulation NeoplasticActin CytoskeletonOncologyMedicineThioredoxinSignal TransductionResearch Articleinorganic chemicalsAcute promyelocytic leukemiaToxic Agentschemistry.chemical_elementAntineoplastic AgentsBiologyComplementary and Alternative MedicineCell Line TumormedicineHumansRNA MessengerBiologyArseniclcsh:RComputational BiologyCancers and Neoplasmsmedicine.diseaseActin cytoskeletonMolecular biologychemistryDrug Resistance NeoplasmApoptosisCell culturelcsh:QPLoS ONE
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Wine yeast peroxiredoxin TSA1 plays a role in growth, stress response and trehalose metabolism in biomass propagation

2020

This article belongs to the Special Issue Wine Yeast 1.0.

Microbiology (medical)Protein moonlightingperoxiredoxinsThioredoxin reductaseSaccharomyces cerevisiaeMutantWineSaccharomyces cerevisiaeMicrobiology<i>Saccharomyces cerevisiae</i>03 medical and health scienceschemistry.chemical_compoundVirologyoxidative stressBiomasswinelcsh:QH301-705.5030304 developmental biologychemistry.chemical_classification0303 health sciencesTsa1biologybiomass030306 microbiologyChemistryPeroxiredoxinsbiology.organism_classificationTrehaloseYeast in winemakingEnzymeBiochemistrylcsh:Biology (General)Oxidative stressPeroxiredoxinMicroorganisms
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Identification of Resistance Genes and Response to Arsenic in Rhodococcus aetherivorans BCP1

2019

This is the accepted manuscript of the paper &quot;Identification of Resistance Genes and Response to Arsenic in Rhodococcus aetherivorans BCP1&quot;, published as final paper in &quot;Frontiers in Microbiology Volume 10, 07 May 2019, Pages 888 https://doi.org/10.3389/fmicb.2019.00888&rdquo;. Arsenic (As) ranks among the priority metal(loid)s that are of public health concern. In the environment, arsenic is present in different forms, organic or inorganic, featured by various toxicity levels. Bacteria have developed different strategies to deal with this toxicity involving different resistance genetic determinants. Bacterial strains of Rhodococcus genus, and more in general Actinobacteria p…

Microbiology (medical)arsenic resistance geneThioredoxin reductaselcsh:QR1-502chemistry.chemical_elementMicrobiologylcsh:MicrobiologyNO03 medical and health scienceschemistry.chemical_compoundR. aetherivorans BCP1Gene clusterRhodococcusArsenic030304 developmental biologyArseniteOriginal Research0303 health sciencesbiology030306 microbiologyarsenate reductionarsenic resistance genesbiology.organism_classificationActinobacteriaArsenate reductaseBiochemistrychemistryarsenic resistance genes arsenate reduction Rhodococcus R. aetherivorans BCP1 ActinobacteriaThioredoxinEnergy sourceRhodococcusRhodococcuFrontiers in Microbiology
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Unexpected multivalent display of proteins by temperature triggered self-assembly of elastin-like polypeptide block copolymers

2012

We report herein the unexpected temperature triggered self-assembly of proteins fused to thermally responsive elastin-like polypeptides (ELPs) into spherical micelles. A set of six ELP block copolymers (ELP(BC)) differing in hydrophilic and hydrophobic block lengths were genetically fused to two single domain proteins, thioredoxin (Trx) and a fibronectin type III domain (Fn3) that binds the α(v)β(3) integrin. The self-assembly of these protein-ELP(BC) fusions as a function of temperature was investigated by UV spectroscopy, light scattering, and cryo-TEM. Self-assembly of the ELP(BC) was unexpectedly retained upon fusion to the two proteins, resulting in the formation of spherical micelles …

Models MolecularHydrodynamic radiusPolymers and PlasticsIntegrinBioengineeringFibronectin type III domainMicelleArticleBiomaterialsThioredoxinsMaterials ChemistryCopolymerTumor Cells CulturedHumansParticle SizeMicellesbiologyChemistryTemperatureFibronectinsElastinFibronectinsBiochemistryBiophysicsbiology.proteinSelf-assemblyThioredoxinK562 CellsPeptidesHydrophobic and Hydrophilic Interactions
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Luminescent alkynyl-gold(i) coumarin derivatives and their biological activity

2013

The synthesis and characterization of three propynyloxycoumarins are reported in this work together with the formation of three different series of gold(i) organometallic complexes. Neutral complexes are constituted by water soluble phosphines (PTA and DAPTA) which confer water solubility to them. The X-ray crystal structure of 7-(prop-2-in-1-yloxy)-1-benzopyran-2-one and its corresponding dialkynyl complex is also shown and the formation of rectangular dimers for the gold derivative in the solid state can be observed. A detailed analysis of the absorption and emission spectra of both ligands and complexes allows us to attribute the luminescent behaviour to the coumarin organic ligand. More…

Models MolecularLuminescenceThioredoxin-Disulfide ReductasePhosphinesAntineoplastic AgentsCrystal structureCrystallography X-RayPhotochemistryInorganic ChemistryMetalchemistry.chemical_compoundCoumarinsCell Line TumorNeoplasmsPolymer chemistryHumansPropynyloxycoumarins; Gold(I) complexes; X-ray crystallography; Luminiscence; Biological activityta116Aqueous solutionLigandWaterBiological activityCoumarinSolubilitychemistryvisual_artvisual_art.visual_art_mediumDrug Screening Assays AntitumorLuminescencePhosphorescenceOrganogold CompoundsDalton Trans.
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Redox regulation of enzymatic activity and proteolytic susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase fromEuglena gracilis.

1992

The activity of ribulose-1,5-bisphosphate carboxylase/oxygenase fromEuglena gracilis decays steadily when exposed to agents that induce oxidative modification of cysteine residues (Cu(2+), benzofuroxan, disulfides, arsenite, oxidized ascorbate). Inactivation takes place with a concomitant loss of cysteine sulfhydryl groups and dimerization of large subunits of the enzyme. 40% activity loss induced by the vicinal thiol-reagent arsenite is caused by modification of a few neighbor residues while the almost complete inactivation achieved with disulfides is due to extensive oxidation leading to formation of mixed disulfides with critical cysteines of the protein. In most cases oxidative inactiva…

OxygenaseCell BiologyPlant ScienceGeneral MedicineGlutathioneBiochemistryDithiothreitolPyruvate carboxylasechemistry.chemical_compoundchemistryBiochemistryCystamineCysteamineThioredoxinCysteinePhotosynthesis research
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Identification of metabolic enzymes in renal cell carcinoma utilizing PROTEOMEX analyses

2003

Abstract PROTEOMEX, an approach which combines conventional proteome analysis with serological screening, is a powerful tool to separate proteins and identify immunogenic components in malignant diseases. By applying this approach, we characterized nine metabolic enzymes which were differentially expressed in renal cell carcinoma (RCC) cell lines and compared their expression profiles to that of normal kidney epithelium cells. Four of these proteins, superoxide dismutase (SODC), triosephosphatase isomerase (TPIS), thioredoxin (THIO) and ubiquitin carboxyl-terminal hydrolase (UBL1) were further analysed for both their constitutive and interferon (IFN)-γ inducible protein expression pattern i…

ProteomeBiophysicsBiologyurologic and male genital diseasesProteomicsBiochemistryAnalytical ChemistryInterferon-gammaThioredoxinsDownregulation and upregulationWestern blotTumor Cells CulturedmedicineHumansElectrophoresis Gel Two-DimensionalCarcinoma Renal CellMolecular BiologyKidneymedicine.diagnostic_testSuperoxide DismutaseImmunohistochemistryMolecular biologyKidney NeoplasmsEpitheliumEnzymesmedicine.anatomical_structureCell cultureProteomeThioredoxinSoftwareTriose-Phosphate IsomeraseBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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Saccharomyces cerevisiae Cytosolic Thioredoxins Control Glycolysis, Lipid Metabolism, and Protein Biosynthesis under Wine-Making Conditions.

2019

Thioredoxins are small proteins that regulate the cellular redox state, prevent oxidative damage, and play an active role in cell repair. Oxidative stress has proven to be of much relevance in biotechnological processes when the metabolism of Saccharomyces cerevisiae is mainly respiratory. During wine yeast starter production, active dry yeast cytosolic thioredoxin Trx2p is a key player in protecting metabolic enzymes from being oxidized by carbonylation. Less is known about the role of redox control during grape juice fermentation. A mutant strain that lacked both cytosolic thioredoxins, Trx1p and Trx2p, was tested for grape juice fermentation. Its growth and sugar consumption were greatly…

ProteomicsSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaethioredoxin-thioredoxin reductase systemsyeastsWineOxidative phosphorylationSaccharomyces cerevisiaeApplied Microbiology and Biotechnology03 medical and health sciencesCytosolThioredoxinsYeastsMetabolomicsVitis030304 developmental biology0303 health sciencesEcologybiology030306 microbiologyChemistryfood and beveragesMembrane ProteinsLipid metabolismMetabolismPeroxiredoxinsglycolysisbiology.organism_classificationLipid MetabolismmetabolomicsYeastYeast in winemakingOxidative StressBiochemistryProtein BiosynthesisFermentationFood MicrobiologyFermentationThioredoxinThioredoxin-thioredoxin reductase systemsGlycolysisOxidation-ReductionGene DeletionFood ScienceBiotechnology
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