Search results for "Disulfide"

showing 10 items of 171 documents

Verwertbarkeit verschiedener Cysteinderivate bei langfristiger parenteraler Ernährung

1989

Utilization of cysteine derivatives for parenteral nutrition was established by means of nitrogen balance of growing rats. N,N-bis-acetylcystine and bisacetyl-glycyl-cystine were not utilized as substrates. N-acetylcysteine, glutathione disulfide, and L-thiazolidine-(4)-carboxylic acid gave evidence as suitable cysteine sources for parenteral nutrition.

Nitrogen balancechemistry.chemical_compoundParenteral nutritionBiochemistryChemistryMedicine (miscellaneous)Glutathione disulfideBiochemistryNitrogen cycleFood ScienceCysteineZeitschrift für Ernährungswissenschaft
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Regulation of tumour cell sensitivity to TNF-induced oxidative stress and cytotoxicity: Role of glutathione

1998

Glutathione (GSH) and the rate of cellular proliferation determine tumour cell sensitivity to tumour necrosis factor (TNF). Buthionine sulphoximine (BSO), a selective inhibitor of GSH synthesis, inhibits tumour growth and increases recombinant human TNF (rhTNF)-alpha cytoxicity in vitro. Administration of sublethal doses of rhTNF-alpha to Ehrlich ascites-tumour (EAT)-bearing mice induces oxidative stress (as measured by increases in intracellular peroxide levels, O2.- generation and mitochondrial GSSG). ATP-induced selective GSH depletion, when combined with rhTNF-alpha administration, affords a 61% inhibition of tumour growth and results in a significant extent of host survival. Administra…

Programmed cell deathCell SurvivalClinical BiochemistryMitochondrionPharmacologyBiologymedicine.disease_causeBiochemistryMicechemistry.chemical_compoundSuperoxidesmedicineAnimalsHumansCarcinoma Ehrlich TumorGlutathione DisulfideTumor Necrosis Factor-alphaGeneral MedicineGlutathioneGlutathioneRecombinant ProteinsOxidative StresschemistryBiochemistryCancer cellMolecular MedicineGlutathione disulfideTumor necrosis factor alphaOxidative stressIntracellularBioFactors
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Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex.

2002

Folding and post-translational modification of the thyroid hormone precursor, thyroglobulin (Tg), in the endoplasmic reticulum (ER) of the thyroid epithelial cells is facilitated by several molecular chaperones and folding enzymes, such as BiP, GRP94, calnexin, protein disulfide isomerase, ERp72, and others. They have been shown to associate simultaneously and/or sequentially with Tg in the course of its maturation, thus forming large heterocomplexes in the ER of thyrocytes. Here we present evidence that such complexes include a novel member, an ER-resident lumenal protein, ERp29, which is present in all mammalian tissues with exceptionally high levels of expression in the secretory cells. …

Protein DenaturationProtein FoldingImmunoprecipitationmedicine.medical_treatmentBlotting WesternThyroid GlandThyrotropinBiologyEndoplasmic ReticulumLigandsBiochemistryThyroglobulinRats Sprague-DawleyCalnexinmedicineCentrifugation Density GradientAnimalsUreaSecretionProtein disulfide-isomeraseMolecular BiologyCells CulturedHeat-Shock ProteinsThyroid Epithelial CellsChromatographyEndoplasmic reticulumCell BiologyPrecipitin TestsRatsCross-Linking ReagentsBiochemistryLiverMicroscopy FluorescenceMicrosomes LiverProtein foldingThyroglobulinProtein BindingThe Journal of biological chemistry
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The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.

2007

Abstract Procollagen C-proteinase (PCP) removes the C-terminal pro-peptides of procollagens and also processes other matrix proteins. The major splice form of the PCP is termed BMP1 (bone morphogenetic protein 1). Active BMP1 is composed of an astacin-like protease domain, three CUB (complement, sea urchin Uegf, BMP1) domains and one EGF-like domain. Here we compare the recombinant human full-length BMP1 with its isolated proteolytic domain to further unravel the functional influence of the CUB and EGF domains. We show that the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. However, u…

Protein FoldingCollagen Type VIIDNA Complementarymedicine.medical_treatmentClinical BiochemistryAmino Acid MotifsGene ExpressionGlutamic AcidBiochemistryBone morphogenetic protein 1Mass SpectrometryBone Morphogenetic Protein 1Cell LineSubstrate SpecificityProtein structuremedicineEscherichia coliAnimalsHumansCysteineDisulfidesMolecular BiologyInclusion BodiesMetalloproteinaseProteasebiologyChemistryMetalloendopeptidasesRecombinant ProteinsProtein Structure TertiaryFibronectinProcollagen peptidaseDrosophila melanogasterBiochemistryBone Morphogenetic ProteinsMutationbiology.proteinProtein foldingAstacinBiological chemistry
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Disulfide stress: a novel type of oxidative stress in acute pancreatitis.

2013

Glutathione oxidation and protein glutathionylation are considered hallmarks of oxidative stress in cells because they reflect thiol redox status in proteins. Our aims were to analyze the redox status of thiols and to identify mixed disulfides and targets of redox signaling in pancreas in experimental acute pancreatitis as a model of acute inflammation associated with glutathione depletion. Glutathione depletion in pancreas in acute pancreatitis is not associated with any increase in oxidized glutathione levels or protein glutathionylation. Cystine and homocystine levels as well as protein cysteinylation and γ-glutamyl cysteinylation markedly rose in pancreas after induction of pancreatitis…

Protein FoldingFree RadicalsCystineProtein Disulfide-IsomerasesProtein glutathionylationmedicine.disease_causeBiochemistrychemistry.chemical_compoundStress PhysiologicalPhysiology (medical)medicineAnimalsCysteineDisulfidesSulfhydryl CompoundsProtein disulfide-isomeraseGlutathione DisulfideProtein phosphatase 2GlutathioneKEAP1Oxidative StressBiochemistrychemistryPancreatitisOxidation-ReductionOxidative stressCysteineFree radical biologymedicine
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Expression and glycosylation studies of human FGF receptor 4

2001

Fibroblast growth factor receptor subtype 4 (FGFR4) has been shown to have special activation properties and just one splicing form, unlike the other FGFRs. FGFR4 overexpression is correlated with breast cancer and therefore FGFR4 is a target for drug design. Our aim is to overexpress high amounts of homogeneous FGFR4 extracellular domain (FGFR4ed) for structural studies. We show that baculovirus-insect cell-expressed FGFR4ed is glycosylated on three (N88, N234, and N266) of the six possible N-glycosylation sites but is not O-glycosylated. The deglycosylated triple mutant was expressed and had binding properties similar to those of glycosylated FGFR4ed, but was still heterogeneous. Large am…

Protein FoldingGlycosylationGlycosylationBlotting WesternImmunoblottingMolecular Sequence DataProtein RenaturationBiologyFibroblast growth factorMass SpectrometryInclusion bodiesCell Line03 medical and health scienceschemistry.chemical_compoundSDG 3 - Good Health and Well-beingEscherichia coliAnimalsHumansReceptor Fibroblast Growth Factor Type 4TrypsinAmino Acid SequenceDisulfidesReceptorChromatography High Pressure Liquid030304 developmental biologyInclusion Bodies0303 health sciencesHeparin030302 biochemistry & molecular biologyFibroblast growth factor receptor 4Fibroblast growth factor receptor 3Receptors Fibroblast Growth FactorMolecular biologyRecombinant Proteins3. Good healthchemistryFibroblast growth factor receptorMutationRNA splicing/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingBaculoviridaeBiotechnology
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Identification of disulphide bonds in the refolding of bovine pancreatic RNase A

1996

Background: Comprehension of the rules that govern the folding process is still far from satisfactory, though it is nevertheless clear that all the information required to define the folding is encoded in the amino acid sequence. In proteins that contain disulphide bonds, folding is associated with disulphide bond formation. Protein species with different numbers of disulphides tend to accumulate during the process; these species can be trapped in a stable form, by quenching any remaining free SH groups, and then characterized in order to identify the disulphide bonds formed. Results The refolding pathway of reduced and denatured RNase A has been studied using mass spectrometric strategies …

Protein FoldingSh groupsRNase P010402 general chemistryPeptide Mapping01 natural sciencesBiochemistryrefolding03 medical and health sciencesRNase AAnimalsDisulfidesES-MSPeptide sequencedisulphide bonds030304 developmental biology0303 health sciencesQuenching (fluorescence)ChemistryFAB-MSRibonuclease Pancreatic0104 chemical sciencesFolding (chemistry)CrystallographyMolecular MedicineCattlePancreatic RNaseDisulphide bondsCysteineFolding and Design
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Ex vivo emission of volatile organic compounds from gastric cancer and non-cancerous tissue

2018

The presence of certain volatile organic compounds (VOCs) in the breath of patients with gastric cancer has been reported by a number of research groups; however, the source of these compounds remains controversial. Comparison of VOCs emitted from gastric cancer tissue to those emitted from non-cancerous tissue would help in understanding which of the VOCs are associated with gastric cancer and provide a deeper knowledge on their generation. Gas chromatography with mass spectrometric detection (GC-MS) coupled with head-space needle trap extraction (HS-NTE) as the pre-concentration technique, was used to identify and quantify VOCs released by gastric cancer and non-cancerous tissue samples c…

Pulmonary and Respiratory MedicineAdultMaleUrine01 natural sciencesGas Chromatography-Mass Spectrometry03 medical and health scienceschemistry.chemical_compound0302 clinical medicineLimit of DetectionStomach NeoplasmsmedicineHumansAgedDetection limitCarbon disulfideVolatile Organic CompoundsChromatography010401 analytical chemistryCancerReproducibility of ResultsMiddle Agedmedicine.diseaseToluene0104 chemical sciences3. Good healthchemistryBreath Tests030220 oncology & carcinogenesisFemaleGas chromatographyGas chromatography–mass spectrometryEx vivoBiomarkersJournal of Breath Research
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Substrate impact on the thickness dependence of vibrational and optical properties of large area $MoS_2$ produced by gold-assisted exfoliation

2021

The gold-assisted exfoliation is a very effective method to produce large-area ($cm^2$-scale) membranes of molybdenum disulfide ($MoS_2$) for electronics. However, the strong $MoS_2/Au$ interaction, beneficial for the exfoliation process, has a strong impact on the vibrational and light emission properties of $MoS_2$. Here, we report an atomic force microscopy (AFM), micro-Raman ($\mu-R$) and micro-Photoluminescence ($\mu-PL$) investigation of $MoS_2$ with variable thickness exfoliated on Au and subsequently transferred on an $Al_2O_3/Si$ substrate. The $E_{2g}$ - $A_{1g}$ vibrational modes separation $\Delta\mu$ (typically used to estimate $MoS_2$ thickness) exhibits an anomalous large val…

QuenchingexcitonCondensed Matter - Materials ScienceMaterials sciencePhysics and Astronomy (miscellaneous)ExcitonMaterials Science (cond-mat.mtrl-sci)FOS: Physical sciencesSubstrate (electronics)2D materialsMolecular physicsExfoliation jointchemistry.chemical_compoundchemistryMonolayerLight emissionTrionMoS2Molybdenum disulfide
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Age-dependent regulation of antioxidant genes by p38α MAPK in the liver

2018

p38α is a redox sensitive MAPK activated by pro-inflammatory cytokines and environmental, genotoxic and endoplasmic reticulum stresses. The aim of this work was to assess whether p38α controls the antioxidant defense in the liver, and if so, to elucidate the mechanism(s) involved and the age-related changes. For this purpose, we used liver-specific p38α-deficient mice at two different ages: young-mice (4 months-old) and old-mice (24 months-old). The liver of young p38α knock-out mice exhibited a decrease in GSH levels and an increase in GSSG/GSH ratio and malondialdehyde levels. However, old mice deficient in p38α had higher hepatic GSH levels and lower GSSG/GSH ratio than young p38α knock-…

ROS Reactive oxygen species;RSK1 Ribosomal S6 kinase10301 basic medicineMAPK/ERK pathwayAgingHPLC High-performance liquid chromatographyAntioxidantmedicine.medical_treatmentTBP TATA-binding proteinClinical BiochemistryDEN Diethyl nitrosamine;MKP-1 MAPK phosphatase-1IκB kinaseGCLc Glutamate cysteine ligase catalytic subunitp38 Mitogen-Activated Protein KinasesG6PDH Glucose-6-phosphate dehydrogenaseBiochemistryAntioxidantsMicechemistry.chemical_compoundSuperoxide Dismutase-1Akt Protein kinase B0302 clinical medicineNrf2 Nuclear factor erythroid 2-related factor-2IL InterleukinSOD1 Cu/Zn-superoxide dismutaselcsh:QH301-705.5Mice KnockoutMK2 MAP-activated protein kinase 2;PGC-1α Peroxisome proliferator-activated receptor gamma coactivator 1-alphachemistry.chemical_classificationlcsh:R5-920Trx ThioredoxinGlutathione DisulfideTNF-α Tumor necrosis factor-alphabiologyLPS Lipopolysaccharide;GSSG Oxidized glutathione;MEF Mouse embryonic fibroblastsNF-kappa BGstm1 Glutathione S-transferase mu 1CatalaseEndoplasmic Reticulum StressGlutathioneLiverGSH Reduced glutathione;Catalase030220 oncology & carcinogenesisJNK c-Jun N-terminal kinaselcsh:Medicine (General)Research Papermedicine.medical_specialtyNF-E2-Related Factor 2Glutamate-Cysteine LigaseMKK MAPK kinaseAP-1 Activator protein-1IKK IƙB KinaseGene Expression Regulation EnzymologicSuperoxide dismutase03 medical and health sciencesInternal medicineGlutamate cysteine ligaseEGFR Epidermal growth factor receptormedicineAnimalsNuclear factor ƙBAnd catalaseChIP Chromatin immunoprecipitation;Protein kinase BNF-ƙB Nuclear factor kappa BSuperoxide DismutaseSuperoxide dismutase 1Superoxide dismutase 2Organic ChemistryGlutathioneASK1 Apoptosis signal-regulating kinase 1ATF2 activating transcription factor 2;030104 developmental biologyEndocrinologyEnzymeHsp Heat shock proteinlcsh:Biology (General)chemistrybiology.proteinSOD2 Mn-superoxide dismutaseMAPK mitogen activated protein kinaseNEM N-ethyl maleimide;Redox Biology
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