Search results for "endoplasmic reticulum"

showing 10 items of 306 documents

Paraoxonase-2 Reduces Oxidative Stress in Vascular Cells and Decreases Endoplasmic Reticulum Stress–Induced Caspase Activation

2007

Background— In the vascular system, elevated levels of reactive oxygen species (ROS) produce oxidative stress and predispose to the development of atherosclerosis. Therefore, it is important to understand the systems producing and those scavenging vascular ROS. Here, we analyzed the ROS-reducing capability of paraoxonase-2 (PON2) in different vascular cells and its involvement in the endoplasmic reticulum stress pathway known as the unfolded protein response. Methods and Results— Quantitative real-time polymerase chain reaction and Western blotting revealed that PON2 is equally expressed in vascular cells and appears in 2 distinct glycosylated isoforms. By determining intracellular ROS, we…

Protein FoldingNuclear EnvelopeRecombinant Fusion ProteinsEndoplasmic Reticulummedicine.disease_causeMuscle Smooth VascularPhysiology (medical)medicineHumansNuclear membraneCells CulturedCaspaseEndoplasmchemistry.chemical_classificationReactive oxygen speciesbiologyAryldialkylphosphataseEndoplasmic reticulumGene Transfer TechniquesEndothelial CellsFibroblastsCoronary VesselsCell biologyEnzyme ActivationOxidative Stressmedicine.anatomical_structurechemistryBiochemistryCaspasesUnfolded protein responsebiology.proteinReactive Oxygen SpeciesCardiology and Cardiovascular MedicineIntracellularOxidative stressSignal TransductionCirculation
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Dithiothreitol Treatment of Madin-Darby Canine Kidney Cells Reversibly Blocks Export from the Endoplasmic Reticulum but Does Not Affect Vectorial Tar…

1995

Addition of dithiothreitol (DTT) to the culture medium of Madin-Darby canine kidney (MDCK) cells blocks transport of newly synthesized gp80 (clusterin, apolipoprotein J), a soluble marker protein for apical exocytosis in this epithelial cell line. In cells treated with DTT during pulse labeling, gp80 is retained in the endoplasmic reticulum. After removal of the reducing agent, gp80 is posttranslationally oxidized and secreted at the apical surface of MDCK cell monolayers. This demonstrates that when folded and oxidized posttranslationally, gp80 can acquire a conformation that exhibits sorting signals for vectorial targeting. In the continuous presence of DTT, the transepithelial electrical…

Protein FoldingProtein ConformationBiologyEndoplasmic ReticulumKidneySulfur RadioisotopesBiochemistryEpitheliumExocytosisDithiothreitolCell LineMembrane Potentialssymbols.namesakechemistry.chemical_compoundDogsMethioninemedicineAnimalsCysteineSalivary Proteins and PeptidesMolecular BiologySecretory pathwayGlycoproteinsTight junctionEndoplasmic reticulumCell MembraneCell BiologyGolgi apparatusEpitheliumCell biologyDithiothreitolClusterinmedicine.anatomical_structureSecretory proteinchemistrysymbolsOxidation-ReductionProtein Processing Post-TranslationalMolecular ChaperonesJournal of Biological Chemistry
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Transmembrane but not soluble helices fold inside the ribosome tunnel

2018

Integral membrane proteins are assembled into the ER membrane via a continuous ribosome-translocon channel. The hydrophobicity and thickness of the core of the membrane bilayer leads to the expectation that transmembrane (TM) segments minimize the cost of harbouring polar polypeptide backbones by adopting a regular pattern of hydrogen bonds to form α-helices before integration. Co-translational folding of nascent chains into an α-helical conformation in the ribosomal tunnel has been demonstrated previously, but the features governing this folding are not well understood. In particular, little is known about what features influence the propensity to acquire α-helical structure in the ribosom…

Protein FoldingSequence Homology Amino AcidScienceQProteïnes de membranaMembrane ProteinsMolecular Dynamics SimulationEndoplasmic ReticulumArticleProtein Structure SecondaryAnimalslcsh:QAmino Acid Sequencelcsh:ScienceHydrophobic and Hydrophilic InteractionsSignal Recognition ParticleRibosomes
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Calcium negatively regulates meprin β activity and attenuates substrate cleavage

2015

The meprin β metalloproteinase is an important enzyme in extracellular matrix turnover, inflammation, and neurodegeneration in humans and mice. Previous studies showed a diminished cleavage of certain meprin β substrates in the presence of calcium, although the mechanism was not clear. With the help of a specific fluorogenic peptide assay and the human amyloid precursor protein as substrate, we demonstrated that the influence of calcium is most likely a direct effect on human meprin β itself. Analyzing the crystal structures of pro- and mature meprin β helped to identify a cluster of negatively charged amino acids forming a potential calcium binding site. Mutation of 2 of these residues (D2…

Protein Foldingchemistry.chemical_elementCalciumEndoplasmic ReticulumBiochemistryCell LineSubstrate SpecificityAmyloid beta-Protein PrecursorChlorocebus aethiopsGeneticsAmyloid precursor proteinAnimalsHumansAmino Acid SequenceBinding siteProtein precursorMolecular BiologyCellular localizationSecretory pathwayMetalloproteinaseAmyloid beta-PeptidesBinding SitesbiologyEndoplasmic reticulumMetalloendopeptidasesCell biologyHEK293 CellschemistryCOS CellsMutationMetalloproteasesbiology.proteinCalciumAmyloid Precursor Protein SecretasesSequence AlignmentBiotechnologyThe FASEB Journal
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Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spa…

2006

Missense mutations in the humanPLP1gene lead to dysmyelinating diseases with a broad range of clinical severity, ranging from severe Pelizaeus–Merzbacher disease (PMD) to milder spastic paraplegia type 2 (SPG-2). The molecular pathology has been generally attributed to endoplasmic reticulum (ER) retention of misfolded proteolipid protein (PLP) (and its splice isoform DM20) and induction of the unfolded protein response. As opposed to previous studies of heterologous expression systems, we have analyzed PLP/DM20 trafficking in oligodendroglial cells, thereby revealing differences between PMD and SPG-2-associated PLP/DM20 isoforms. PLPA242Vand DM20A242V(jimpy-msdin mice), associated with seve…

Proteolipid protein 1Time FactorsLeupeptinsBlotting WesternGene Expressionchemical and pharmacologic phenomenaNerve Tissue ProteinsBiologyProtein degradationCysteine Proteinase InhibitorsTransfectionMiceMice Neurologic MutantsCricetulusMembrane MicrodomainsMutant proteinimmune system diseasesCricetinaeAnimalsImmunoprecipitationMyelin Proteolipid ProteinLipid raftCells CulturedGeneral NeuroscienceEndoplasmic reticulumCholesterol bindingER retentionArticlesImmunohistochemistryCell biologynervous system diseasesOligodendrogliaProtein TransportCholesterolBiochemistryUnfolded protein responselipids (amino acids peptides and proteins)Mutant ProteinsSubcellular FractionsThe Journal of neuroscience : the official journal of the Society for Neuroscience
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Proteomic identification of the heterogeneous nuclear ribonucleoprotein K as irradiation responsive protein related to migration

2014

Abstract Irradiation resistance is a major obstacle of head and neck squamous cell carcinoma (HNSCC) therapy, limiting treatment success and patient survival. The aim of our experiments was to identify irradiation-regulated proteins as potential drug targets. Two established HNSCC cell lines (HNSCCUM-01T and HNSCCUM-02T) were treated with a single 8 Gy (Gray) fraction of irradiation. Changes in cellular protein expression were studied after 24 h by means of 2D-electrophoresis and MALDI–TOF-mass spectrometry. Ninety-four differentially expressed proteins were identified. The expression levels of four proteins were regulated similarly in both cell lines after irradiation treatment, i.e., GRP7…

ProteomicsBiophysicsBiologyBiochemistryCellular proteinImmunocytochemical stainingHeterogeneous-Nuclear Ribonucleoprotein KCell MovementCell Line TumormedicineHumansHeterogeneous-Nuclear Ribonucleoprotein KIrradiationNeoplasm MetastasisEndoplasmic Reticulum Chaperone BiPmedicine.diseaseMolecular biologyHead and neck squamous-cell carcinomaNeoplasm ProteinsGene Expression Regulation NeoplasticBlotRibonucleoproteinsGamma RaysHead and Neck NeoplasmsBiological significanceCell cultureCarcinoma Squamous CellCancer researchJournal of Proteomics
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Classes of non-conventional tetraspanins defined by alternative splicing

2019

AbstractTetraspanins emerge as a family of membrane proteins mediating an exceptional broad diversity of functions. The naming refers to their four transmembrane segments, which define the tetraspanins‘ typical membrane topology. In this study, we analyzed alternative splicing of tetraspanins. Besides isoforms with four transmembrane segments, most mRNA sequences are coding for isoforms with one, two or three transmembrane segments, representing structurally mono-, di- and trispanins. Moreover, alternative splicing may alter transmembrane topology, delete parts of the large extracellular loop, or generate alternative N- or C-termini. As a result, we define structure-based classes of non-con…

ProteomicsGene isoformRNA splicingTetraspaninslcsh:MedicineComputational biologyBiologyEndoplasmic ReticulumArticleStructure-Activity Relationship03 medical and health sciences0302 clinical medicineIsomerismHumanslcsh:ScienceGene030304 developmental biology0303 health sciencesMultidisciplinarylcsh:RAlternative splicingLipid microdomainMembrane ProteinsTransmembrane proteinAlternative SplicingMembrane protein030220 oncology & carcinogenesisMembrane topologyembryonic structureslcsh:QStructural biologyFunction (biology)Scientific Reports
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Role of JAK/STAT in Interstitial Lung Diseases; Molecular and Cellular Mechanisms

2021

Interstitial lung diseases (ILDs) comprise different fibrotic lung disorders characterized by cellular proliferation, interstitial inflammation, and fibrosis. The JAK/STAT molecular pathway is activated under the interaction of a broad number of profibrotic/pro-inflammatory cytokines, such as IL-6, IL-11, and IL-13, among others, which are increased in different ILDs. Similarly, several growth factors over-expressed in ILDs, such as platelet-derived growth factor (PDGF), transforming growth factor β1 (TGF-β1), and fibroblast growth factor (FGF) activate JAK/STAT by canonical or non-canonical pathways, which indicates a predominant role of JAK/STAT in ILDs. Between the different JAK/STAT iso…

QH301-705.5medicine.medical_treatmentReviewCatalysisstatInorganic ChemistryPulmonary fibrosismedicineHumansProtein IsoformsPhysical and Theoretical ChemistryBiology (General)STAT3Molecular BiologyProtein Kinase InhibitorsQD1-999SpectroscopyCellular SenescenceJanus KinasesbiologyChemistryGrowth factorInterleukinsinterstitial lung disease (ILD)Organic ChemistryJAK-STAT signaling pathwayGeneral Medicinerespiratory systemmedicine.diseaseEndoplasmic Reticulum StressComputer Science Applicationsrespiratory tract diseasesSTAT Transcription FactorsChemistrysignal transducer and activator of transcription (STAT)biology.proteinCancer researchidiopathic pulmonary fibrosis (IPF)Janus kinaseLung Diseases InterstitialJanus kinases (JAK)Platelet-derived growth factor receptorTransforming growth factorSignal TransductionInternational Journal of Molecular Sciences
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The ER-Membrane Transport System Is Critical for Intercellular Trafficking of the NSm Movement Protein and Tomato Spotted Wilt Tospovirus.

2015

Plant viruses move through plasmodesmata to infect new cells. The plant endoplasmic reticulum (ER) is interconnected among cells via the ER desmotubule in the plasmodesma across the cell wall, forming a continuous ER network throughout the entire plant. This ER continuity is unique to plants and has been postulated to serve as a platform for the intercellular trafficking of macromolecules. In the present study, the contribution of the plant ER membrane transport system to the intercellular trafficking of the NSm movement protein and Tomato spotted wilt tospovirus (TSWV) is investigated. We showed that TSWV NSm is physically associated with the ER membrane in Nicotiana benthamiana plants. An…

RNA viruses0301 basic medicineLeavesCell MembranesNicotiana benthamianaPlant ScienceEndoplasmic ReticulumPathology and Laboratory MedicineBiochemistrySolanum lycopersicumTospovirusBunyavirusesMedicine and Health SciencesArabidopsis thalianaMovement proteinBiology (General)Integral membrane proteinSecretory PathwaybiologyPlant BiochemistryPlant AnatomyPlasmodesmataProteïnes de membranafood and beveragesPlantsPlants Genetically ModifiedCell biologyTransport proteinPlant Viral Movement ProteinsProtein TransportMedical MicrobiologyCell ProcessesViral PathogensVirusesPathogensCellular Structures and OrganellesTomato Spotted Wilt VirusResearch ArticleBioquímicaCell PhysiologyQH301-705.5Arabidopsis ThalianaImmunologyPlant PathogensBrassicaPlasmodesmaResearch and Analysis MethodsMicrobiologyPlant Viral Pathogens03 medical and health sciencesModel OrganismsPlant and Algal ModelsVirologyTobaccoGeneticsIntegral Membrane ProteinsSecretionMicrobial PathogensMolecular BiologyPlant DiseasesBiology and life sciencesEndoplasmic reticulumfungiOrganismsMembrane ProteinsCell BiologyPlant PathologyRC581-607biology.organism_classificationVirosis (Plantes)VirologyPlant Leaves030104 developmental biologyMembrane TraffickingParasitologyImmunologic diseases. AllergyPLoS Pathogens
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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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