Search results for "Reticulum"

showing 10 items of 336 documents

Cellular stress induces cap-independent alpha-enolase/MBP-1 translation.

2015

AbstractMyc promoter-binding protein-1 (MBP-1) is a shorter protein variant of the glycolytic enzyme alpha-enolase. Although several lines of evidence indicate that MBP-1 acts as a tumor suppressor, the cellular mechanisms and signaling pathways underlying MBP-1 expression still remain largely elusive. To dissect these pathways, we used the SkBr3 breast cancer cell line and non-tumorigenic HEK293T cells ectopically overexpressing alpha-enolase/MBP-1. Here, we demonstrate that induced cell stresses promote MBP-1 expression through the AKT/PERK/eIF2α signaling axis. Our results contribute to shedding light on the molecular mechanisms underlying MBP-1 expression in non-tumorigenic and cancer c…

Alpha-enolaseCellEukaryotic Initiation Factor-2Alternative translationBiochemistryeIF-2 KinaseBreast cancerHEK293 CellStructural BiologyProtein IsoformsbiologyMedicine (all)Translation (biology)Recombinant ProteinEndoplasmic Reticulum StressRecombinant ProteinsNeoplasm ProteinsDNA-Binding ProteinsGene Expression Regulation Neoplasticmedicine.anatomical_structureFemaleSignal transductionMyc promoter-binding protein-1Breast NeoplasmHumanSignal TransductionCell SurvivalDNA-Binding ProteinRecombinant Fusion ProteinsBiophysicsBreast NeoplasmsNeoplasm ProteinGeneticCell Line TumorEndoplasmic reticulum streGeneticsmedicineBiomarkers TumorHumansGene SilencingMolecular BiologyProtein kinase BTumor Suppressor ProteinTumor Suppressor ProteinsHEK 293 cellsProtein IsoformCell BiologySettore BIO/18 - GeneticaHEK293 CellsBiophysicGene Expression RegulationPhosphopyruvate HydrataseCancer cellbiology.proteinUnfolded protein responseCancer researchProto-Oncogene Proteins c-aktRecombinant Fusion ProteinFEBS letters
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Androgen-inducible gene 1 increases the ER Ca(2+) content and cell death susceptibility against oxidative stress.

2016

Androgen-induced gene 1 (AIG1) is a transmembrane protein implicated with survival (its expression level was shown to correlate with the survival of patients suffering from hepatocellular carcinoma) and Ca(2+) signaling (over-expression of AIG1 increased transcription mediated by the Ca(2+)-dependent nuclear factor of activated T cells). We aimed to shed light on this less-studied protein and investigated its tissue expression, genomic organization, intracellular localization and membrane topology as well as its effects on cell death susceptibility and the Ca(2+) content of the endoplasmic reticulum. Immunoblotting of mouse tissues demonstrated highest expression of AIG1 in the liver, lung …

0301 basic medicineMaleProgrammed cell deathGene ExpressionBiologyEndoplasmic Reticulum03 medical and health sciencesMiceProtein DomainsGene expressionGeneticsAnimalsSex CharacteristicsCell DeathEndoplasmic reticulumMembrane ProteinsGeneral MedicineEmbryo MammalianMolecular biologyTransmembrane proteinCell biologyMice Inbred C57BLTransmembrane domainCytosolAlternative SplicingOxidative Stress030104 developmental biologyMembrane proteinOrgan SpecificityMembrane topologyCalciumFemaleGene
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Preproinsulin designer antigens excluded from endoplasmic reticulum suppressed diabetes development in nod mice by dna vaccination

2019

DNA vaccines against autoimmune type 1 diabetes (T1D) contain a nonpredictable risk to induce autoreactive T cell responses rather than a protective immunity. Little is known if (and how) antigen expression and processing requirements favor the induction of autoreactive or protective immune responses by DNA immunization. Here, we analyzed whether structural properties of preproinsulin (ppins) variants and/or subcellular targeting of ppins designer antigens influence the priming of effector CD8+ T cell responses by DNA immunization. Primarily, we used H-2b RIP-B7.1 tg mice, expressing the co-stimulator molecule B7.1 in beta cells, to identify antigens that induce or fail to induce autoreacti…

0301 basic medicinepreproinsulin/proinsulin antigensPreproinsulinlcsh:QH426-470type 1 diabetesMouse ModelsBiologyMajor histocompatibility complexArticleDNA vaccinationDNA vaccines03 medical and health sciences0302 clinical medicineImmune systemAntigenImmunityGeneticsmouse models:Science::Medicine [DRNTU]lcsh:QH573-671Molecular BiologyNOD micelcsh:Cytologylcsh:Geneticsendoplasmic reticulum030104 developmental biology030220 oncology & carcinogenesisImmunologybiology.proteinType 1 DiabetesMolecular MedicineCD8
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Characterization of a mutant form of human apolipoprotein B (Thr26_Tyr27del) associated with familial hypobetalipoproteinemia

2016

We have previously identified a deletion mutant of human apoB [apoB (Thr26_Tyr27del)] in a subject with primary hypobetalipoproteinemia. The present study determined the effect of Thr26_Tyr27del mutation on apoB secretion using transfected McA-RH7777 cells. Transient or stable transfection of apoB-48 containing the Thr26_Tyr27del mutation showed drastically reduced secretion of the mutant as compared to wild-type apoB-48. No lipoproteins containing the mutant apoB-48 were secreted into the medium. Incubation of transfected cells in a lipid-rich medium in the presence of cycloheximide showed rapid turnover of cell-associated mutant apoB-48 as compared to that of wild-type apoB-48. Immunofluo…

0301 basic medicineSettore MED/09 - Medicina InternaTime FactorsApolipoprotein B-48 secretionApolipoprotein BMutantDNA Mutational AnalysisApolipoprotein B mutation Apolipoprotein B-48 secretion Hypobetalipoproteinemia Proteasomal degradation030204 cardiovascular system & hematologymedicine.disease_causeEndoplasmic ReticulumHypobetalipoproteinemiaschemistry.chemical_compound0302 clinical medicineProteasomal degradationProteolysiSequence DeletionMutationbiologyMedicine (all)TransfectionProteasome InhibitorPhenotypeBiochemistryApolipoprotein B-100lipids (amino acids peptides and proteins)Proteasome InhibitorsHumanHeterozygoteProteasome Endopeptidase ComplexTime FactorCycloheximideTransfectiondigestive systemCell LineDNA Mutational Analysi03 medical and health sciencesmedicineHumansSecretionGenetic Predisposition to DiseaseMolecular BiologyEndoplasmic reticulumnutritional and metabolic diseasesCell Biologymedicine.diseaseMolecular biology030104 developmental biologychemistryProteolysisbiology.proteinHypobetalipoproteinemiaApolipoprotein B mutationApolipoprotein B-48Hypobetalipoproteinemia
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Molecular partners of hNOT/ALG3, the human counterpart of the Drosophila NOT and yeast ALG3 gene, suggest its involvement in distinct cellular proces…

2018

This study provides first insights into the involvement of hNOT/ALG3, the human counterpart of the Drosophila Neighbour of TID and yeast ALG3 gene, in various putative molecular networks. HNOT/ALG3 encodes two translated transcripts encoding precursor proteins differing in their N-terminus and showing 33% identity with the yeast asparagine-linked glycosylation 3 (ALG3) protein. Experimental evidence for the functional homology of the proteins of fly and man in the N-glycosylation has still to be provided. In this study, using the yeast two-hybrid technique we identify 17 molecular partners of hNOT-1/ALG3-1. We disclose the building of hNOT/ALG3 homodimers and provide experimental evidence f…

0301 basic medicineGlycosylationSaccharomyces cerevisiae ProteinsRNA-binding proteinSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumMannosyltransferases03 medical and health scienceschemistry.chemical_compoundCongenital Disorders of GlycosylationNeoplasmsNuclear Receptor Subfamily 4 Group A Member 2GeneticsAnimalsDrosophila ProteinsHumansMolecular BiologyTranscription factorOSBPGeneGenetics (clinical)Cellular compartmentEndoplasmic reticulumMembrane ProteinsRNA-Binding ProteinsGeneral MedicineLRP1Cell biology030104 developmental biologychemistryNerve DegenerationDrosophilaCarrier ProteinsHuman molecular genetics
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Does Metformin Modulate Endoplasmic Reticulum Stress and Autophagy in Type 2 Diabetic Peripheral Blood Mononuclear Cells?

2018

Since type 2 diabetes (T2D) is associated with oxidative stress and metformin has been shown to exert a protective role against the said stress, we wondered whether metformin treatment might also modulate endoplasmic reticulum (ER) stress and autophagy in leukocytes of T2D patients. We studied 53 T2D patients (37 of whom had been treated with metformin 1700 mg for at least 1 year) and 30 healthy volunteers. Leukocytes from both groups of T2D patients exhibited increased protein levels of 78-kDa glucose-regulated protein (GRP78) with respect to controls, whereas activating transcription factor 6 (ATF6) was enhanced specifically in nonmetformin-treated T2D, and (s-xbp1) and phosphorylated euk…

Male0301 basic medicinemedicine.medical_specialtyendocrine system diseasesPhysiologyClinical BiochemistryAdministration OralType 2 diabetesBiologymedicine.disease_causeBiochemistry03 medical and health sciencesInternal medicineAutophagymedicineHumansEndoplasmic Reticulum Chaperone BiPMolecular BiologyGeneral Environmental ScienceDose-Response Relationship DrugATF6Endoplasmic reticulumAutophagynutritional and metabolic diseasesCell BiologyBECN1Middle AgedEndoplasmic Reticulum Stressmedicine.diseaseMetforminMetforminOxidative StressCross-Sectional Studies030104 developmental biologyEndocrinologyDiabetes Mellitus Type 2Leukocytes MononuclearUnfolded protein responseGeneral Earth and Planetary SciencesFemaleOxidative stressmedicine.drugAntioxidants & Redox Signaling
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Different conformations of nascent polypeptides during translocation across the ER membrane

2000

Abstract Background In eukaryotic cells, proteins are translocated across the ER membrane through a continuous ribosome-translocon channel. It is unclear to what extent proteins can fold already within the ribosome-translocon channel, and previous studies suggest that only a limited degree of folding (such as the formation of isolated α-helices) may be possible within the ribosome. Results We have previously shown that the conformation of nascent polypeptide chains in transit through the ribosome-translocon complex can be probed by measuring the number of residues required to span the distance between the ribosomal P-site and the lumenally disposed active site of the oligosaccharyl transfer…

GlycosylationProlineProtein ConformationAmino Acid MotifsMolecular Sequence DataEndoplasmic ReticulumPeptide MappingDogsLeucineMicrosomesAnimalsAmino Acid Sequencelcsh:QH573-671Alaninelcsh:CytologyCèl·lules eucariotesMembrane Transport ProteinsValineIntracellular MembranesProtein TransportAminoàcidsPèptidsRibosomesSignal Recognition ParticleResearch Article
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Tubulin-folding cofactor E deficiency is associated with vascular dysfunction and endoplasmatic reticulum stress of vascular smooth muscle cells

2021

Abstract Introduction Endothelial function assessed via flow mediated dilatation (FMD) has shown to predict risk in individuals with established cardiovascular diseases, whereas its predictive value is uncertain in the setting primary prevention. Purpose The aim of the current work was to discover and evaluate novel mediators of vascular dysfunction in the general population and in conditional knock-out transgenic animal models. Methods In order to identify novel targets that were negatively correlated with FMD and investigate their contribution in vascular function, a Genome Wide Association Study (GWAS) of 5,000 participants was performed and subsequently immune cell-, endothelial- and va…

Tubulin foldingVascular smooth musclebusiness.industryMedicineCOFACTOR ECardiology and Cardiovascular MedicinebusinessReticulumCell biologyEuropean Heart Journal
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In vivo Trafficking and Localization of p24 Proteins in Plant Cells

2008

p24 proteins constitute a family of putative cargo receptors that traffic in the early secretory pathway. p24 proteins can be divided into four subfamilies (p23, p24, p25 and p26) by sequence homology. In contrast to mammals and yeast, most plant p24 proteins contain in their cytosolic C-terminus both a dilysine motif in the -3, -4 position and a diaromatic motif in the -7, -8 position. We have previously shown that the cytosolic tail of Arabidopsis p24 proteins has the ability to interact with ARF1 and coatomer (through the dilysine motif) and with COPII subunits (through the diaromatic motif). Here, we establish the localization and trafficking properties of an Arabidopsis thaliana p24 pr…

Recombinant Fusion ProteinsMolecular Sequence DataArabidopsisGolgi ApparatusVacuoleProtein Sorting SignalsBiologyEndoplasmic ReticulumBiochemistrysymbols.namesakeStructural BiologyArabidopsisGeneticsAnimalsHumansProtein IsoformsAmino Acid SequenceMolecular BiologyCOPIISecretory pathwayArabidopsis ProteinsLysineEndoplasmic reticulumMembrane ProteinsCell BiologyCOPIGolgi apparatusbiology.organism_classificationActinsCell biologyDNA-Binding ProteinsProtein TransportBiochemistryCoatomerVacuolessymbolsCOP-Coated VesiclesCarrier ProteinsTranscription FactorsTraffic
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Separation of chitosomes and secretory vesicles from the ?slime? variant of Neurospora crassa

1987

Cells from the “slime” variant of Neurospora crassa were broken in isotonic conditions by use of triethanolamine buffer plus EDTA. After removal of large membranous structures by low-speed centrifugation, chitosomes and secretory vesicles were separated by means of gel filtration, precipitation of membranous contaminants with Concanavalin A, and centrifugation in sucrose or glycerol gradients. Polypeptidic composition of fractions enriched in secretory vesicles or chitosomes was found to be distinct. By these criteria we concluded that chitosomes and secretory vesicles represent different populations of microvesicles. Both microvesicular populations appeared free of endoplasmic reticulum an…

biologyEndoplasmic reticulumGeneral Medicinebiology.organism_classificationBiochemistryMicrobiologyNeurosporaSecretory VesicleMicrovesiclesNeurospora crassaInvertaseBiochemistryConcanavalin AGeneticsbiology.proteinCentrifugationMolecular BiologyArchives of Microbiology
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