Search results for "Teas"

showing 10 items of 619 documents

Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells

1994

AbstractExocytosis of secretory granules by adrenal chromaffin cells is blocked by the tetanus toxin light chain in a zinc specific manner. Here we show that cellular synaptobrevin is almost completely degraded by the tetanus toxin light chain within 15 min. We used highly purified adrenal secretory granules to show that synaptobrevin, which can be cleaved by the tetanus toxin light chain, is localized in the vesicular membrane. Proteolysis of synaptobrevin in cells and in secretory granules is reversibly inhibited by the zinc chelating agent dipicolinic acid. Moreover, cleavage of synaptobrevin present in secretory granules by the tetanus toxin light chain is blocked by the zinc peptidase …

SynaptobrevinProteolysismedicine.medical_treatmentMolecular Sequence DataBiophysicsSynaptobrevinNerve Tissue ProteinsIn Vitro Techniquesmedicine.disease_causeImmunoglobulin light chainBiochemistryExocytosisExocytosisR-SNARE ProteinsStructural BiologyGeneticsmedicineAnimalsChromaffin GranulesAmino Acid SequenceMolecular BiologySecretory granuleR-SNARE ProteinsAdrenal medullaProteasemedicine.diagnostic_testChemistryToxinMembrane ProteinsCell BiologyPeptide FragmentsTetanus toxinmedicine.anatomical_structureBiochemistryCattleAdrenal medullaFEBS Letters
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Taspase1: a 'misunderstood' protease with translational cancer relevance

2015

Proteolysis is not only a critical requirement for life, but the executing enzymes also play important roles in numerous pathological conditions, including cancer. Therefore, targeting proteases is clearly relevant for improving cancer patient care. However, to effectively control proteases, a profound knowledge of their mechanistic function as well as their regulation and downstream signalling in health and disease is required. The highly conserved protease Threonine Aspartase1 (Taspase1) is overexpressed in numerous liquid and solid malignancies and was characterized as a 'non-oncogene addiction' protease. Although Taspase1 was shown to cleave various regulatory proteins in humans as well…

Threonine0301 basic medicineCancer ResearchProteasesmedicine.medical_treatmentProteolysisComputational biologyDiseaseBiologyBioinformaticsmedicine.disease_causeAspartate Ammonia-LyaseGene Expression Regulation EnzymologicTranslational Research Biomedical03 medical and health sciencesNeoplasmsEndopeptidasesGeneticsmedicineHumansEnzyme InhibitorsMolecular BiologyProteaseMolecular Structuremedicine.diagnostic_testCancermedicine.diseaseGene Expression Regulation Neoplastic030104 developmental biologyProteasomeCarcinogenesisBiologieFunction (biology)Oncogene
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Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

2003

Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

Time FactorsLeupeptinsApoptosisRetinoblastoma ProteinAntioxidantsAmino Acid Chloromethyl KetonesMembrane Potentialschemistry.chemical_compoundSettore BIO/10 - BiochimicaMG132Caspase 8OsteosarcomaChemistryCaspase 3Cytochromes cFlow CytometryMitochondriaCysteine EndopeptidasesProto-Oncogene Proteins c-bcl-2CaspasesOsteosarcomamedicine.drugmusculoskeletal diseasesProteasome Endopeptidase ComplexCell SurvivalBlotting Westernbcl-X Proteinmacromolecular substancesTransfectionMultienzyme ComplexesCell Line Tumorparasitic diseasesmedicineHumansProtease InhibitorsneoplasmsMolecular BiologySaos-2 cellsDose-Response Relationship DrugCell Biologymedicine.diseaseAcetylcysteineApoptosis osteosarcoma proteasome inhibitorsMicroscopy FluorescenceApoptosisCancer researchProteasome inhibitorTumor Suppressor Protein p53Reactive Oxygen Specieshuman activities
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Coordinated Sumoylation and Ubiquitination Modulate EGF Induced EGR1 Expression and Stability

2011

Background Human early growth response-1 (EGR1) is a member of the zing-finger family of transcription factors induced by a range of molecular and environmental stimuli including epidermal growth factor (EGF). In a recently published paper we demonstrated that integrin/EGFR cross-talk was required for Egr1 expression through activation of the Erk1/2 and PI3K/Akt/Forkhead pathways. EGR1 activity and stability can be influenced by many different post-translational modifications such as acetylation, phosphorylation, ubiquitination and the recently discovered sumoylation. The aim of this work was to assess the influence of sumoylation on EGF induced Egr1 expression and/or stability. Methods We …

Time FactorsTranscription GeneticSUMO proteinlcsh:MedicineUbiquitin-conjugating enzymeBiochemistrychemistry.chemical_compoundEpidermal growth factorMG132protein 1lcsh:ScienceMitogen-Activated Protein Kinase 1Regulation of gene expressionMitogen-Activated Protein Kinase 3MultidisciplinaryProtein translationProtein Stabilitygene expression regulationCell biologyepidermal growth factorResearch Articlemedicine.drugProteasome Endopeptidase Complexendocrine systemkinase 1SUMO-1 ProteinBiologyDNA-binding proteinsGeneticsmedicineHumansBiologySettore BIO/10 - BIOCHIMICAProtein kinase BPI3K/AKT/mTOR pathwayEarly Growth Response Protein 1lcsh:RMitogen-activated proteinProteinsSumoylationRegulatory proteinsenzyme activationRNA stabilityMolecular biologychemistryProteolysisUbiquitin-Conjugating EnzymesProteasome inhibitorlcsh:QEarly growth responseGene expressionCell linePLoS ONE
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α-Synuclein expression levels do not significantly affect proteasome function and expression in mice and stably transfected PC12 cell lines

2004

α-Synuclein (α-syn) is a small protein of unknown function that is found aggregated in Lewy bodies, the histopathological hallmark of sporadic Parkinson disease and other synucleinopathies. Mutations in the α-syn gene and a triplication of its gene locus have been identified in early onset familial Parkinson disease. α-Syn turnover can be mediated by the proteasome pathway. A survey of published data may lead to the suggestion that overexpression of α-syn wild type, and/or their variants (A53T and A30P), may produce a decrease in proteasome activity and function, contributing to α-syn aggregation. To investigate the relationship between synuclein expression and proteasome function we have s…

Time Factorsanimal diseasesmedicine.disease_causePC12 CellsBiochemistryMicechemistry.chemical_compoundTransgenesPromoter Regions GeneticMice KnockoutGeneticsMutationInnervationBrainParkinson DiseaseProteasome complexAmyloidosisCell biologyInnervacióalpha-SynucleinAdditions and CorrectionsPèptidsPlasmidsProteasome Endopeptidase ComplexPrionsProtein subunitBlotting WesternImmunoblottingSynucleinsMice TransgenicNerve Tissue ProteinsBiologyTransfectionBacterial ProteinsMultienzyme ComplexesmedicineAnimalsImmunoprecipitationMolecular BiologyAlpha-synucleinSynucleinopathiesEpilepsyWild typeGenetic VariationCell BiologyAxonsRatsnervous system diseasesMice Inbred C57BLEpilèpsiaDisease Models AnimalLuminescent ProteinschemistryProteasomenervous systemSinapsiMutationSynapsesSynucleinAmiloïdosiPeptides
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Factor VIIa-induced interaction with integrin controls the release of tissue factor on extracellular vesicles from endothelial cells.

2019

Essentials Prothrombotic extracellular vesicles (EV) carry agonist pathway-specific proteomes Agonists for protease activated receptor (PAR) 2 signaling have distinct effects on EV composition PAR2 signaling rapidly generates prothrombotic EV and slowly EV with inactive tissue factor (TF) FVIIa integrin ligation restricts TF incorporation into EV from endothelial cells SUMMARY: Background Cell injury signal-induced activation and release of tissue factor (TF) on extracellular vesicles (EVs) from immune and vessel wall cells propagate local and systemic coagulation initiation. TF trafficking and release on EVs occurs in concert with the release of cell adhesion receptors, including integrin …

Time Factorsmedia_common.quotation_subjectIntegrinFactor VIIa030204 cardiovascular system & hematologyThromboplastin03 medical and health sciencesTissue factorchemistry.chemical_compoundExtracellular Vesicles0302 clinical medicineHumansReceptor PAR-2Protease-activated receptorintegrin traffickingInternalizationReceptorCell adhesionBlood CoagulationCells Culturedmedia_commonbiologyFactor VIIChemistryIntegrin beta1protease-activated receptorsEndothelial CellsHematologytissue factorCell biologyProtein Transportbiology.proteinOligopeptidesIntracellularSignal TransductionJournal of thrombosis and haemostasis : JTH
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Proteasome comprising a beta1 inducible subunit acts as a negative regulator of NADPH oxidase during elicitation of plant defense reactions.

2005

Elicitation of defense reactions in tobacco by cryptogein, triggered a production of active oxygen species (AOS) via the NADPH oxidase, NtrbohD, and an accumulation of beta1din, a defense induced beta-type subunit of 20S proteasome. The proteasome inhibitor, MG132, stimulated this AOS production. Tobacco cells transformed with sense constructs of beta1din showed an inhibition of the AOS production following elicitin treatment, whereas the antisense transformed cells showed a strongly enhanced AOS production. In cells transformed with sense construct of beta1din, the NtrbohD transcripts failed to be induced by cryptogein as observed in control and antisense transformed cells. Conversely, in …

Tobacco BY-2 cellsHypersensitive responseProteasome Endopeptidase ComplexLeupeptinsBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyCysteine Proteinase InhibitorsBiochemistrychemistry.chemical_compoundStructural BiologyMG132Sense (molecular biology)TobaccoGeneticsmedicineNADPH OXIDASEPROTEASOMEMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSPlant ProteinsCRYPTOGEINNADPH oxidaseTOBACCO BY-2 CELLSNADPH OxidasesElicitinCell BiologyOligonucleotides AntisenseProtein SubunitsProteasomechemistryBiochemistryProteasome inhibitorbiology.proteinPLANT DEFENSEAOS PRODUCTIONReactive Oxygen SpeciesProteasome Inhibitorsmedicine.drugFEBS letters
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Determination of Fungi and Multi-Class Mycotoxins in Camelia sinensis and Herbal Teas and Dietary Exposure Assessment

2020

In this paper, a study of fungal and multi-mycotoxin contamination in 140 Camellia sinensis and 26 herbal teas marketed in Latvia is discussed. The analysis was performed using two-dimensional liquid chromatography with time-of-flight mass spectrometry (2D-LC-TOF-MS) and MALDI-TOF-MS. In total, 87% of the tea samples tested positive for 32 fungal species belonging to 17 genera, with the total enumeration of moulds ranging between 1.00 &times

Tolerable daily intakeOchratoxin ASpectrometry Mass Electrospray IonizationAflatoxinherbal teasHealth Toxicology and MutagenesisColony Count Microbiallcsh:MedicineToxicologyRisk Assessment01 natural sciencesArticleCamellia sinensisDietary Exposurechemistry.chemical_compound0404 agricultural biotechnologymycotoxinsHumansCamellia sinensis2D-LC-TOF-MSFood scienceMycotoxin<i>Camellia sinensis</i> teasTeabiologyDietary exposureCamellia sinensis teaslcsh:R010401 analytical chemistrydietary exposure assessmentfood and beverages04 agricultural and veterinary sciencesContaminationAlternariabiology.organism_classificationLatviaMALDI-TOF-MS040401 food science0104 chemical scienceschemistryConsumer Product SafetySpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationfungi<i>Camellia sinensis </i>teasTeas HerbalChromatography LiquidToxins
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Regulation of stress response in Oenococcus oeni as a function of environmental changes and growth phase

2000

International audience; Oenococcus oeni is a lactic acid bacterium which is able to grow in wine and perform malolactic fermentation. To survive and grow in such a harsh environment as wine, O. oeni uses several mechanisms of resistance including stress protein synthesis. The molecular characterisation of three stress genes hsp18, clpX, trxA encoding for a small heat shock protein, an ATPase regulation component of ClpP protease and a thioredoxin, respectively, allow us to suggest the existence in O. oeni of multiple regulation mechanisms as is the case in Bacillus subtilis. One common feature of these genes is that they are expressed under the control of housekeeping promoters. The express…

Transcription Geneticmedicine.medical_treatment[SDV]Life Sciences [q-bio]bactérie lactiqueBacillus subtilisatpaseMicrobiologygène clppoenococcus oenicaractérisation moléculaire03 medical and health sciencesBacterial ProteinsHeat shock proteinOenococcus;Malolactic fermentation;Stress gene;ATPaseMalolactic fermentationmedicineprotéine de choc thermiquePromoter Regions GeneticGeneHeat-Shock ProteinsOenococcus030304 developmental biologyOenococcus oeniAdenosine Triphosphatases0303 health sciencesProteasebiology030306 microbiologyMalolactic fermentationStress genefood and beveragesGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationGram-Positive CocciBiochemistryThioredoxinOenococcusLeuconostocFood Scienceexpression des gènes
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Pharmacologic Inhibition of ADAM10 Attenuates Brain Tissue Loss, Axonal Injury and Pro-inflammatory Gene Expression Following Traumatic Brain Injury …

2021

The α-secretase A disintegrin and metalloprotease 10 (ADAM10) regulates various physiological and pathophysiological processes. Despite its broad functional implications during development, plasticity, and disease, no pharmacological approaches to inhibit ADAM10 in acute brain injury have been reported. Here, we examined the effects of the ADAM10 inhibitor GI254023X on the neurological and histopathological outcome after experimental traumatic brain injury (TBI). C57BL/6N mice were subjected to the controlled cortical impact (CCI) model of TBI or sham procedure and received GI254023X or vehicle during the acute phase of injury (n = 40, 100 mg/kg, 25% DMSO, 0.1 M Na2CO3, intraperitoneal, 30 …

Traumatic brain injuryADAM10PharmacologyBlood–brain barrierNeuroprotectionneuroinflammationaxonal injuryCell and Developmental Biologymedicinelcsh:QH301-705.5NeuroinflammationOriginal ResearchMicrogliabiologybusiness.industrytraumatic brain injuryADAM10 (a disintegrin and metalloprotease 10)Glutamate receptorCell Biologymedicine.diseaseGI254023Xmedicine.anatomical_structurelcsh:Biology (General)biology.proteinneuroprotectionGRIN2BbusinessDevelopmental BiologyFrontiers in Cell and Developmental Biology
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