0000000000306464

AUTHOR

Dalila Darmoul

showing 3 related works from this author

Decrease of mRNA levels and biosynthesis of sucrase-isomaltase but not dipeptidylpeptidase IV in forskolin or monensin-treated Caco-2 cells.

1991

International audience; Treatment for 48 h of differentiated, confluent Caco-2 cells with 2.5 10(-5) M forskolin or 10(-6) M monensin, which produces a significant decrease of the de novo biosynthesis of sucrase-isomaltase, does not change quantitatively the de novo biosynthesis of dipeptidylpeptidase IV. Western blot analysis and silver nitrate staining indicate that neither drug induces any modification in the steady state expression of these two brush border hydrolases. Northern blot analysis shows that the level of dipeptidylpeptidase IV mRNA does not change in treated as compared to control Caco-2 cells. In contrast, forskolin and monensin dramatically decrease the level of sucrase-iso…

Brush borderDipeptidyl Peptidase 4Blotting WesternAdenocarcinomaBiology03 medical and health sciencesCellular and Molecular Neurosciencechemistry.chemical_compoundWestern blot[ CHIM.ORGA ] Chemical Sciences/Organic chemistryCyclic AMPTumor Cells CulturedmedicineHumansRNA MessengerNorthern blotMonensinDipeptidyl-Peptidases and Tripeptidyl-PeptidasesMolecular Biology030304 developmental biologyPharmacology0303 health sciencesForskolinmedicine.diagnostic_test[CHIM.ORGA]Chemical Sciences/Organic chemistryColforsin030302 biochemistry & molecular biologyMonensinAntibodies MonoclonalCell BiologyMetabolismBlotting Northern[CHIM.ORGA] Chemical Sciences/Organic chemistrySucrase-Isomaltase ComplexGlucosechemistryBiochemistryCell cultureColonic NeoplasmsMolecular MedicineSucrase-isomaltase
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The N-glycan processing in HT-29 cells is a function of their state of enterocytic differentiation. Evidence for an atypical traffic associated with …

1991

International audience; When the human colon cancer cells HT-29 undergo enterocytic differentiation, they correctly process their N-glycans, whereas their undifferentiated counterpart are unable to process Man9-8-GlcNAc2 species, the natural substrate of alpha-mannosidase I. As this enzyme is fully active in both HT-29 cell populations, we hypothesize that N-glycoproteins are unable to reach the cis Golgi, the site where alpha-mannosidase I has been localized. We have demonstrated this point by using 1-deoxymannojirimycin, leupeptin, and monensin. In the presence of 1-deoxymannojirimycin, a specific inhibitor of alpha-mannosidase I, differentiated HT-29 cells, as expected, accumulate Man9-8…

Proteases1-DeoxynojirimycinColonLeupeptinsCellular differentiationCellIn Vitro TechniquesBiologyBiochemistry03 medical and health sciencessymbols.namesakechemistry.chemical_compoundPolysaccharidesalpha-Mannosidase[ CHIM.ORGA ] Chemical Sciences/Organic chemistryMannosidasesTumor Cells CulturedmedicineHumansMonensinMolecular Biology030304 developmental biologychemistry.chemical_classificationGlucosamine0303 health sciencesMembrane Glycoproteins[CHIM.ORGA]Chemical Sciences/Organic chemistryEndoplasmic reticulum030302 biochemistry & molecular biologyLeupeptinBiological TransportCell DifferentiationCell BiologyCompartment (chemistry)Golgi apparatus[CHIM.ORGA] Chemical Sciences/Organic chemistrymedicine.anatomical_structureBiochemistrychemistryColonic NeoplasmssymbolsGlycoproteinProtein Processing Post-Translational
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N-Glycosylation modification of proteins is an early marker of the enterocytic differentiation process of HT-29 cells

1990

International audience; The human colon cancer cell line HT-29 remains totally undifferentiated when glucose is present in the culture medium (HT-29 Glc+), while the same cells may undergo typical enterocytic differentiation after reaching confluence when grown in glucose-deprived medium (HT-29 Glc-). Recently, we demonstrated a deficiency in the overall N-glycan processing in confluent undifferentiated cells, whereas differentiated cells follow a classical pattern of N-glycosylation. The main changes in N-glycosylation observed in confluent undifferentiated cells may be summarised as follows: 1) the conversion of high mannose into complex glycopeptides is greatly decreased; 2) this decreas…

EmbryologyGlycosylationGrowth phaseCellular differentiationMedicine (miscellaneous)macromolecular substancesBiology03 medical and health sciences0302 clinical medicineN-linked glycosylationPolysaccharides[ CHIM.ORGA ] Chemical Sciences/Organic chemistry[SDV.BDD] Life Sciences [q-bio]/Development BiologyTumor Cells CulturedHumansProcess (anatomy)[SDV.BDLR] Life Sciences [q-bio]/Reproductive Biology030304 developmental biologychemistry.chemical_classification0303 health sciences[CHIM.ORGA]Chemical Sciences/Organic chemistryProteinsCell Differentiation[CHIM.ORGA] Chemical Sciences/Organic chemistryGlycopeptideIntestinescarbohydrates (lipids)Human colon cancer[SDV.AEN] Life Sciences [q-bio]/Food and NutritionGlucoseReproductive MedicineBiochemistrychemistryCell culture030220 oncology & carcinogenesisColonic Neoplasmslipids (amino acids peptides and proteins)Animal Science and ZoologyGlycoproteinMannoseCell DivisionDevelopmental BiologyFood Science
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