Search results for "DISULFIDE-ISOMERASE"

showing 7 items of 17 documents

P046 Vitamin D decreases PDIA3 and prevents the enhanced migration of fibroblasts from stricturing Crohn’s disease

2020

Abstract Background Fibrosis is a common complication in Crohn’s disease (CD) patients and fibroblasts play an important role in the fibrogenic process. Low vitamin D (VD) levels and a defective VD-signalling pathway have been reported in CD. VD signals through both vitamin D receptor (VDR) and protein disulfide-isomerase A3 (PDIA3) and we have previously demonstrated that VDR protein levels are reduced in fibroblasts isolated from CD patients and that VD increased VDR expression in these cells (A-2080; ECCO 2019). We aim to analyse here the effect of VD on both PDIA3 protein levels and migration in CD fibroblasts. Methods We used intestinal fibroblasts isolated from surgical resections of …

Crohn's diseasebusiness.industryGastroenterologyMucous membraneGeneral MedicinePDIA3medicine.diseasemedicine.anatomical_structureVitamin D3 ReceptorFibrosismedicineCancer researchVitamin D and neurologybusinessProtein disulfide-isomeraseHormoneJournal of Crohn's and Colitis
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Endoplasmic Reticulum Chaperones in Viral Infection: Therapeutic Perspectives

2021

SUMMARY Viruses are intracellular parasites that subvert the functions of their host cells to accomplish their infection cycle. The endoplasmic reticulum (ER)-residing chaperone proteins are central for the achievement of different steps of the viral cycle, from entry and replication to assembly and exit. The most abundant ER chaperones are GRP78 (78-kDa glucose-regulated protein), GRP94 (94-kDa glucose-regulated protein), the carbohydrate or lectin-like chaperones calnexin (CNX) and calreticulin (CRT), the protein disulfide isomerases (PDIs), and the DNAJ chaperones. This review will focus on the pleiotropic roles of ER chaperones during viral infection. We will cover their essential role …

GRP78CalnexinReviewGRP94Endoplasmic ReticulumMicrobiologyDNAJcalreticulinImmune systemCalnexinHumansProtein disulfide-isomeraseMolecular BiologyEndoplasmic Reticulum Chaperone BiPchemistry.chemical_classificationbiologyEndoplasmic reticulumIntracellular parasiteprotein disulfide isomeraseCell biologyER chaperoneInfectious DiseaseschemistryApoptosisVirus Diseasesbiology.proteinviral infectionGlycoproteinCalreticulinMolecular ChaperonesMicrobiology and Molecular Biology Reviews : MMBR
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Screening trematodes for novel intervention targets: a proteomic and immunological comparison of Schistosoma haematobium, Schistosoma bovis and Echin…

2011

SUMMARYWith the current paucity of vaccine targets for parasitic diseases, particularly those in childhood, the aim of this study was to compare protein expression and immune cross-reactivity between the trematodes Schistosoma haematobium, S. bovis and Echinostoma caproni in the hope of identifying novel intervention targets. Native adult parasite proteins were separated by 2-dimensional gel electrophoresis and identified through electrospray ionisation tandem mass spectrometry to produce a reference gel. Proteins from differential gel electrophoresis analyses of the three parasite proteomes were compared and screened against sera from hamsters infected with S. haematobium and E. caproni fo…

MaleProteomicsProteome/dk/atira/pure/subjectarea/asjc/2400/2405ProteomicstrematodeimmunologyEXPERIMENTAL-INFECTIONS. bovis0302 clinical medicineCricetinaeEchinostoma/dk/atira/pure/subjectarea/asjc/2700/2725SchistosomiasisParasite hostingElectrophoresis Gel Two-DimensionalChildDIGEGENE-EXPRESSIONGel electrophoresisSchistosoma haematobiumEchinostomiasis0303 health sciencesBiomphalaria/dk/atira/pure/subjectarea/asjc/1100/1103IMMUNE-RESPONSESEchinostosma caproniHelminth ProteinsUp-RegulationPROTEIN DISULFIDE-ISOMERASE3. Good healthPhenotypeInfectious DiseasesProteomeSchistosoma haematobiumSchistosomaEchinostomaResearch ArticleFRIEDI TREMATODABulinus030231 tropical medicineMANSONICross ReactionsBiologyHost-Parasite InteractionsMicrobiologyS. haematobium03 medical and health sciencesproteomicsSpecies SpecificityDIAAnimalsHumansFasciola hepaticaPARASITE030304 developmental biologySchistosomaFASCIOLA-HEPATICAMOLECULAR-CLONINGMesocricetusANCYLOSTOMA-CANINUMbiology.organism_classificationvaccine developmentAntigens HelminthImmunologyAnimal Science and ZoologyParasitologyParasitology
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Novel strategies in the war against antibiotic resistance

2021

The global threat of antibiotic resistance is steadily growing. Antibiotic resistancemay involve any class of antibiotic, including second- and third-line agents that have been considered to date the last-resort drugs to counteract common infections. We may lose our capability to keep under control many common bacterial infections [1]. Despite this, in the past decade significant research efforts have been made to develop new antibacterial strategies able to treat multidrug-resistant infections; however, no new therapeutic approach has yet reached the clinic [2,3]. In order to identify new valuable antimicrobial drugs, it is important to consider the main bacterial resistance mechanisms in …

Methicillin-Resistant Staphylococcus aureusPharmacologyVirulencebiologyChemistryEscherichia coli ProteinsProtein Disulfide-IsomerasesBiofilmDrug Resistance MicrobialAnti-Bacterial AgentsMicrobiologyDsbAAntibiotic resistanceBiofilmsDrug DiscoveryEscherichia colibiology.proteinMolecular Medicineantibiotic resistance antivirulence strategy biofilm DsbA MRSA
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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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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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mp23, a Theileria parva transmembrane protein with homology to the protein disulfide isomerase family

2002

The protozoan parasite Theileria parva (Apicomplexa) causes the bovine disease East Coast Fever in endemic areas in Subsaharan Africa. The intralymphocytic schizont stage is largely responsible for the pathogenicity and induces a transformed phenotype in host cells [1]. Current evidence supports a model in which the schizont perturbs the immune response by inducing production of cytokines and stimulating the growth of parasitized cells [2]. We were interested to identify parasite proteins involved in parasite/host interaction and have described earlier a screening procedure for identification of schizont stage-exported proteins based on cell-free expression of cDNA and testing for transloca…

Signal peptideDNA ComplementarySequence Homology Amino AcidcDNA libraryEndoplasmic reticulumTheileria parvaMolecular Sequence DataProtein Disulfide-IsomerasesProtozoan ProteinsMembrane ProteinsSequence Analysis DNABiologyTheileria parvabiology.organism_classificationMolecular biologyTransmembrane proteinMembrane proteinComplementary DNAparasitic diseasesAnimalsParasitologyAmino Acid SequenceProtein disulfide-isomeraseMolecular BiologyMolecular and Biochemical Parasitology
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