Search results for "glycosylation"

showing 10 items of 190 documents

Expression and purification of polyhistidine-tagged rotavirus NSP4 proteins in insect cells

2003

The rotavirus nonstructural NSP4 protein, a transmembrane endoplasmic reticulum-specific glycoprotein, has been described as the first viral enterotoxin. Purified NSP4 or a peptide corresponding to NSP4 residues 114-135 induces diarrhea in young mice. NSP4 has a membrane-destabilizing activity and causes an increase in intracellular calcium levels and chloride secretion by a calcium-dependent signalling pathway in eucaryotic cells. In this study, four recombinant baculoviruses were generated expressing the rotavirus NSP4 glycoprotein from the human strains Wa and Ito, the porcine strain OSU, and the simian strain SA11, which belong to two different NSP4 genotypes, A and B. The recombinant g…

DiarrheaRotavirusGlycosylationInsectaImmunoprecipitationRecombinant Fusion ProteinsvirusesGenetic VectorsViral Nonstructural ProteinsProtein Engineeringmedicine.disease_causelaw.inventionMicelawRotavirusmedicineAnimalsHumansHistidinePolyacrylamide gel electrophoresisCells CulturedGlycoproteinsToxins Biologicalchemistry.chemical_classificationChemistryEndoplasmic reticulumbiochemical phenomena metabolism and nutritionMolecular biologyTransmembrane proteinBlotGene Expression RegulationRecombinant DNAElectrophoresis Polyacrylamide GelGlycoproteinBiotechnologyProtein Expression and Purification
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Are the new genetic tools for diagnosis of Wilson disease helpful in clinical practice?

2020

Summary The diagnosis of Wilson disease is not always easy. For many patients, a combination of tests reflecting disturbed copper metabolism may be needed. Testing for ATP7B variants has become part of the routine diagnostic approach. The methods of genetic testing include analysis of the 21 coding exons and intronic flanking sequences, in which exons with recurrent variants would be prioritised depending on the mutation frequency in the local population. If sequencing the entire ATP7B gene cannot identify 2 variants and the suspicion for Wilson disease is high, after reviewing the clinical data, WES (whole-exome sequencing) or WGS (whole-genome sequencing) could be applied. A workflow base…

DiseaseReviewIndian childhood cirrhosisBioinformaticsDNA sequencingWES whole-exome sequencingPFIC progressive familial intrahepatic cholestasisInternal MedicinemedicineImmunology and AllergyMultiplex ligation-dependent probe amplificationWGS whole-genome sequencingExome sequencingGenetic testingWilson diseaseWhole genome sequencingWhole-genome sequencingHepatologymedicine.diagnostic_testMEDNIK syndromebusiness.industryCopper metabolismGastroenterologyMLPA multiplex ligation-dependent probe amplificationmedicine.diseaseICC Indian childhood cirrhosisNGS next-generation sequencingDMR differentially methylated regionsWhole-exome sequencingNext-generation sequencingbusinessICT idiopathic or primary copper toxicosisCDG congenital disorders of glycosylationGenetic diseasesJHEP Reports
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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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Synthesis of Fluorinated Glycosyl Amino Acid Building Blocks for MUC1 Cancer Vaccine Candidates by Microreactor-Assisted Glycosylation

2012

Abstract MUC1-type glycopeptides have already shown their potential as possible cancer vaccine candidates. In addition, first examples of fluorinated antigen structures, especially containing the Thomsen–Friedenreich antigen, with similar antibody recognition have been reported. Using microreactor techniques for improvement of the crucial step, the complex glycosylation reactions, is an efficient way to find optimized reaction parameter as well as to circumvent well-known scale-up drawbacks. Besides, this is the first report of continuous flow glycosylations of glycosyl amino acids, in particular with fluorinated glycosyl building blocks.

Fluid Flow and Transfer Processeschemistry.chemical_classificationGlycosylationChemistryOrganic ChemistryCombinatorial chemistryGlycopeptideAmino acidcarbohydrates (lipids)chemistry.chemical_compoundAntigenChemistry (miscellaneous)Organic chemistrylipids (amino acids peptides and proteins)GlycosylCancer vaccineMicroreactorMUC1Journal of Flow Chemistry
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Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

1998

SUMMARYThe cell wall is essential to nearly every aspect of the biology and pathogenicity of Candida albicans. Although it was intially considered an almost inert cellular structure that protected the protoplast against osmotic offense, more recent studies have demonstrated that it is a dynamic organelle. The major components of the cell wall are glucan and chitin, which are associated with structural rigidity, and mannoproteins. The protein component, including both mannoprotein and nonmannoproteins, comprises some 40 or more moieties. Wall proteins may differ in their expression, secretion, or topological location within the wall structure. Proteins may be modified by glycosylation (prima…

Fungal proteinGlycosylationBiologyMicrobiologyArticleHsp70Fungal ProteinsCell wallchemistry.chemical_compoundInfectious DiseasesBiochemistrychemistryMembrane proteinCell WallCandida albicansOrganelleExtracellularSecretionMolecular BiologyMicrobiology and Molecular Biology Reviews
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Synthetic O-glycopeptides as model substrates for glycosyltransferases

1993

Abstract A new approach to O-glycopeptides of the glucosamine type is described. N-Urethane protected, peracetylated glucosamine is converted into its 1-thio (1-bromo) derivative and used for glycosylation of a variety of protected serine or threonine derivatives as acceptors. The urethane group is easily exchanged for the natural N-acetyl moiety and O-deacetylation is achieved with hydrazine/methanol. The resulting O-GlcNAc derivatives are subjected to an enzymatic galactosylation procedure using β-1,4-galactosyltransferase (EC 2.4.1.22) to furnish O-glycopeptides of the neolactosamine type.

GalactosyltransferaseGlycosylationStereochemistryOrganic ChemistryHydrazineChemical synthesisCatalysisInorganic ChemistrySerinechemistry.chemical_compoundchemistryGlucosamineMoietyPhysical and Theoretical ChemistryThreonineTetrahedron: Asymmetry
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Glycosylated macromolecular conjugates of antiviral drugs with a polyaspartamide.

2004

Two new polymeric conjugates for specific liver targeting were prepared by conjugation of sugar moieties and antiviral drugs to alpha, beta-poly[N-2-(hydroxyethyl)-DL-aspartamide] (PHEA). PHEA-galactopyranosylphenylthiocarbamide-mono-O-succinylganciclovir (conjugate 7) and PHEA-mannopyranosylphenylthiocarbamide-O-succinylacyclovir (conjugate 8) were synthesized according to a multi-step procedure which allowed for obtaining high product yield and process standardization. Conjugate 7 contained 7.5 and 8.5% of galactose and ganciclovir (substituent/repeating unit, mol/mol), respectively, and conjugate 8 contained 14.2 and 10.8% of mannose and acyclovir, respectively. In vitro studies demonstr…

Ganciclovirchemistry.chemical_classificationMaleMice Inbred BALB CGlycosylationStereochemistryMacromolecular SubstancesSubstituentPharmaceutical ScienceMannoseGlycosidic bondAntiviral Agentschemistry.chemical_compoundHydrolysisMicePoly(hydroxyethylaspartamide) Bioconjugates Polymer therapeutics Liver targeting AntiviralschemistrySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoGalactosemedicineMoietyAnimalsPeptidesmedicine.drugConjugateJournal of drug targeting
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Posttranslational N-glycosylation of the hepatitis B virus large envelope protein

2007

Abstract Background The addition of N-linked glycans to proteins is normally a cotranslational process that occurs during translocation of the nascent protein to the endoplasmic reticulum. Here, we report on an exception to this rule occurring on the hepatitis B virus (HBV) large L envelope protein that is a subject to co-plus posttranslational N-glycosylation. Results By using an improved detection system, we identified so far unrecognized, novel isoforms of L. Based on mutational analyses, the use of N-glycosylation inhibitors, and pulse-chase studies, we showed that these isoforms are due to posttranslational N-glycan addition to the asparagines 4 and 112 within the preS domain of L. Whi…

Gene Expression Regulation ViralHepatitis B virusGlycosylationGlycosylationViral transformationBiologymedicine.disease_causeHepatitis B virus PRE betaCell Linelcsh:Infectious and parasitic diseaseschemistry.chemical_compoundViral Envelope ProteinsN-linked glycosylationViral entryVirologymedicineHumansProtein Isoformslcsh:RC109-216Hepatitis B viruschemistry.chemical_classificationResearchEndoplasmic reticulumEpithelial CellsVirologyProtein Structure TertiaryCell biologycarbohydrates (lipids)Infectious DiseaseschemistryGlycoproteinProtein Processing Post-TranslationalVirology Journal
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Expression pattern of the Brachyury and Tbx2 homologues from the sponge Suberites domuncula.

2005

Background information. T-box transcription factors are a large family of transcriptional regulators involved in many aspects of embryonic development. In a previous report, we described the isolation and genomic characterization of two T-box genes from the siliceous sponge Suberites domuncula: a Brachyury homologue, Sd-Bra, and a Tbx2 homologue, Sd-Tbx2. Elucidation of the genomic structure of Sd-Bra allowed us to demonstrate the existence of two different isoforms, resulting from alternative splicing. Moreover, we demonstrated that the shorter isoform exists in two different glycosylation states. Results. In the present study, we demonstrate a differential subcellular localization of the …

Gene isoformFetal ProteinsBrachyuryCytoplasmGlycosylationBlotting WesternAnimalsProtein IsoformsGeneTranscription factorCells CulturedGeneticsRegulation of gene expressionCell NucleusbiologyAlternative splicingCell BiologyGeneral Medicinebiology.organism_classificationImmunohistochemistryPoriferaSuberites domunculaAlternative SplicingGene Expression RegulationT-Box Domain ProteinsFunction (biology)Biology of the cell
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Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform enc…

2004

The conversion into abnormally folded prion protein (PrP) plays a key role in prion diseases. PrP(C) carries two N-linked glycan chains at amino acid residues 180 and 196 (mouse). Previous in vitro data indicated that the conversion process may not require glycosylation of PrP. However, it is conceivable that these glycans function as intermolecular binding sites during the de novo infection of cells on susceptible organisms and/or play a role for the interaction of both PrP isoforms. Such receptor-like properties could contribute to the formation of specific prion strains. However, in earlier studies, mutations at the glycosylation sites of PrP led to intracellular trafficking abnormalitie…

Genetically modified mouseGlycanGlycosylationGlycosylationPrionsanimal diseasesBovine spongiform encephalopathyMutantBlotting WesternScrapieMice TransgenicCHO CellsCell SeparationBiologyBiochemistryCell LinePrion Diseaseschemistry.chemical_compoundMicePolysaccharidesCell Line TumorCricetinaemedicineAnimalsImmunoprecipitationProtein IsoformsBiotinylationDisulfidesTransgenesCloning MolecularMolecular BiologyBinding SitesWild typeBrainCell Biologymedicine.diseaseFlow CytometryVirologyMolecular biologyIn vitronervous system diseasesEncephalopathy Bovine SpongiformMice Inbred C57BLchemistryMutationbiology.proteinCattleScrapieThe Journal of biological chemistry
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