Search results for "glycosylation"

showing 10 items of 190 documents

Heterodimerization of Two Pathological Mutants Enhances the Activity of Human Phosphomannomutase2

2015

The most frequent disorder of glycosylation is due to mutations in the gene encoding phosphomannomutase2 (PMM2-CDG). For this disease, which is autosomal and recessive, there is no cure at present. Most patients are composite heterozygous and carry one allele encoding an inactive mutant, R141H, and one encoding a hypomorphic mutant. Phosphomannomutase2 is a dimer. We reproduced composite heterozygosity in vitro by mixing R141H either with the wild type protein or the most common hypomorphic mutant F119L and compared the quaternary structure, the activity and the stability of the heterodimeric enzymes. We demonstrated that the activity of R141H/F119L heterodimers in vitro, which reproduces t…

Genetics and Molecular Biology (all)HeterozygoteProtein StructureGlycosylationMutantlcsh:MedicineGlucose-6-PhosphateBiologymedicine.disease_causeBiochemistryQuaternaryCongenital Disorders of GlycosylationProtein structuremedicineAlleles; Congenital Disorders of Glycosylation; Dimerization; Glucose-6-Phosphate; Glycosylation; Heterozygote; Humans; Mutation; Phosphorylation; Phosphotransferases (Phosphomutases); Protein Structure Quaternary; Agricultural and Biological Sciences (all); Biochemistry Genetics and Molecular Biology (all); Medicine (all)HumansPhosphorylationAlleleProtein Structure Quaternarylcsh:ScienceGeneAllelesMutationMultidisciplinaryMedicine (all)lcsh:RWild typeMolecular biologyEnzyme structureProteostasisAgricultural and Biological Sciences (all)heterodimresPhosphotransferases (Phosphomutases)Mutationlcsh:QCDG-PMM2DimerizationResearch ArticlePLOS ONE
researchProduct

Isolation of theMNN9gene ofYarrowia lipolytica(YlMNN9) and phenotype analysis of a mutantylmnn9Δ strain

2003

In this work we describe the isolation of the Yarrowia lipolytica homologue of Saccharomyces cerevisiae MNN9 gene, which we have named YlMNN9, and the phenotype analysis of a Y. lipolytica strain containing the disrupted YlMNN9 allele. YlMNN9 was cloned using degenerate consensus oligonucleotides to generate specific probes that were in turn used to screen mini-gene libraries. The gene is defined by a 1014 bp ORF predicted to encode a protein 337 amino acids long that shares significant homology with the Mnn9ps of S. cerevisiae, Candida albicans and Hansenula polymorpha, including a putative N-terminal transmembrane domain. Disruption of YlMNN9 leads to phenotypes such as resistance to sodi…

GeneticsGlycosylationbiologySaccharomyces cerevisiaeMutantBioengineeringYarrowiabiology.organism_classificationApplied Microbiology and BiotechnologyBiochemistryHomology (biology)Transmembrane domainchemistry.chemical_compoundchemistryGeneticsGeneHygromycin BBiotechnologyYeast
researchProduct

Rat mammary-gland transferrin: nucleotide sequence, phylogenetic analysis and glycan structure

1995

The complete cDNA for rat mammary-gland transferrin (Tf) has been sequenced and also the native protein isolated from milk in order to analyse the structure of the main glycan variants present. A lactating-rat mammary-gland cDNA library in lambda gt10 was screened with a partial cDNA copy of rat liver Tf and subsequently rescreened with 5′ fragments of the longest clones. This produced a 2275 bp insert coding for an open reading frame of 695 amino acid residues. This includes a 19-amino acid signal sequence and the mature protein containing 676 amino acids and one N-glycosylation site in the C-terminal domain at residue 490. Phylogenetic analysis was carried out using 14 translated Tf nucle…

GlycanDNA ComplementaryGlycosylationMolecular Sequence DataOligosaccharidesSequence alignmentAnimal Population GroupsBiochemistrychemistry.chemical_compoundMammary Glands AnimalSugar AlcoholsSpecies SpecificityPolysaccharidesComplementary DNANeuraminic acidCarbohydrate ConformationAnimalsRats WistarMolecular BiologyPhylogenyBase SequencebiologycDNA libraryTransferrinNucleic acid sequenceCell BiologyMilk ProteinsMolecular biologyN-Acetylneuraminic AcidRatsSialic acidMilkCarbohydrate SequenceGeneschemistryBiochemistryMultigene FamilySialic Acidsbiology.proteinFemaleNeuraminic AcidsProtein Processing Post-TranslationalSequence AlignmentN-Acetylneuraminic acidResearch ArticleBiochemical Journal
researchProduct

Cohen syndrome is associated with major glycosylation defects

2014

International audience; Cohen syndrome (CS) is a rare autosomal recessive disorder with multisytemic clinical features due to mutations in the VPS13B gene, which has recently been described encoding a mandatory membrane protein involved in Golgi integrity. As the Golgi complex is the place where glycosylation of newly synthesized proteins occurs, we hypothesized that VPS13B deficiency, responsible of Golgi apparatus disturbance, could lead to glycosylation defects and/or mysfunction of this organelle, and thus be a cause of the main clinical manifestations of CS. The glycosylation status of CS serum proteins showed a very unusual pattern of glycosylation characterized by a significant accum…

GlycanGlycosylationGlycosylationEndosomeDevelopmental Disabilities[SDV]Life Sciences [q-bio]Vesicular Transport ProteinsGolgi ApparatusFingers03 medical and health scienceschemistry.chemical_compoundsymbols.namesake0302 clinical medicineAntigens CDIntellectual DisabilityMyopiaGeneticsHumansObesityMolecular BiologyGenetics (clinical)030304 developmental biology0303 health sciencesbiology[ SDV ] Life Sciences [q-bio]Retinal DegenerationTransferrinGeneral MedicineFibroblastsBrefeldin AGolgi apparatusIntercellular Adhesion Molecule-1Cell biologyVPS13BchemistryMembrane proteinBiochemistryMicrocephalysymbolsO-linked glycosylationbiology.proteinMuscle HypotoniaElectrophoresis Polyacrylamide GelRNA InterferenceCell Adhesion Molecules030217 neurology & neurosurgery
researchProduct

Mouse Testican-2

2005

Mouse testican-2 was cloned, sequenced, and shown to be a proteoglycan with a multidomain structure closely similar to that of the human ortholog, previously described as a calcium binding extracellular matrix molecule of the BM-40/SPARC/osteonectin family (Vannahme, C., Schubel, S., Herud, M., Gosling, S., Hulsmann, H., Paulsson, M., Hartmann, U., and Maurer, P. (1999). J. Neurochem. 73, 12–20). Recombinant mouse testican-2 was used to prepare specific antibodies that allowed the detection of testican-2 in various brain structures but also in lung, testis, and in several endocrine glands. Although the testican-2 expressed in EBNA-293 cells carried both heparan sulfate and chondroitin/derma…

GlycanGlycosylationbiologyNeuriteCell BiologyHeparan sulfateBiochemistryMolecular biologyDermatan sulfatecarbohydrates (lipids)Extracellular matrixchemistry.chemical_compoundProteoglycanchemistrybiology.proteinOsteonectinMolecular BiologyJournal of Biological Chemistry
researchProduct

Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles.

1998

ABSTRACT Unlike those of the S and the L envelope proteins, the functional role of the related M protein in the life cycle of the hepatitis B virus (HBV) is less understood. We now demonstrate that a single N glycan, specific for M, is required for efficient secretion of M empty envelope particles. Moreover, this glycan mediates specific association of M with the chaperone calnexin. Conversely, the N glycan, common to all three envelope proteins, is involved neither in calnexin binding nor in subviral particle release. As proper folding and trafficking of M need the assistance of the chaperone, the glycan-dependent association of M with calnexin may thus play a crucial role in the assembly …

GlycanHepatitis B virusGlycosylationGlycosylationCalnexinImmunologyBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundCytosolN-linked glycosylationViral Envelope ProteinsVirologyCalnexinmedicineAnimalsSecretionPeptide sequenceHepatitis B virusBase SequenceCalcium-Binding ProteinsVirus-Cell Interactionscarbohydrates (lipids)BiochemistrychemistryOligodeoxyribonucleotidesInsect ScienceChaperone (protein)COS Cellsbiology.proteinMutagenesis Site-DirectedJournal of virology
researchProduct

Glycation alters ligand binding, enzymatic, and pharmacological properties of human albumin.

2015

Albumin, the major circulating protein in blood plasma, can be subjected to an increased level of glycation in a diabetic context. Albumin exerts crucial pharmacological activities through its drug binding capacity, i.e., ketoprofen, and via its esterase-like activity, allowing the conversion of prodrugs into active drugs. In this study, the impact of the glucose-mediated glycation on the pharmacological and biochemical properties of human albumin was investigated. Aggregation product levels and the redox state were quantified to assess the impact of glycation-mediated changes on the structural properties of albumin. Glucose-mediated changes in ketoprofen binding properties and esterase-lik…

Glycation End Products AdvancedGlycosylationGlycosylationSerum albuminContext (language use)Plasma protein bindingProtein aggregationBiochemistryChromatography AffinityMass SpectrometryProtein Structure Secondarychemistry.chemical_compoundGlycationAlbuminsBlood plasmaHumansGlycated Serum AlbuminSerum AlbuminbiologyAlbuminAlbuminSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Spectrometry FluorescencechemistryBiochemistryKetoprofenbiology.proteinHumanProtein BindingBiochemistry
researchProduct

Thermal aggregation of glycated bovine serum albumin

2010

International audience; Aggregation and glycation processes in proteins have a particular interest in medicine fields and in food technology. Serum albumins are model proteins which are able to self-assembly in aggregates and also sensitive to a non-enzymatic glycation in cases of diabetes. In this work, we firstly reported a study on the glycation and oxidation effects on the structure of bovine serum albumin (BSA). The experimental approach is based on the study of conformational changes of BSA at secondary and tertiary structures by FTIR absorption and fluorescence spectroscopy, respectively. Secondly, we analysed the thermal aggregation process on BSA glycated with different glucose con…

Glycation End Products AdvancedGlycosylationHot TemperatureGlycoxidation02 engineering and technologyProtein aggregationBiochemistryProtein Structure SecondaryAnalytical Chemistrychemistry.chemical_compoundProtein structureGlycationSpectroscopy Fourier Transform InfraredScattering RadiationGlycated Serum AlbuminBovine serum albuminGlycation0303 health sciencesbiologyChemistryTryptophanSerum Albumin Bovine021001 nanoscience & nanotechnology3. Good healthSpectrophotometryProtein aggregation0210 nano-technologyOxidation-ReductionGlycosylationBiophysicsSerum albuminIn Vitro Techniques03 medical and health sciencesAnimalsMolecular BiologySerum Albumin030304 developmental biologyChromatographyAlbuminAlbuminLight scatteringSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein tertiary structureProtein Structure TertiaryKineticsFTIR spectroscopyGlucoseSpectrometry FluorescenceUnfolded Protein Responsebiology.proteinCattleProtein Multimerization[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
researchProduct

Glycosylamines of 4,6-O-butylidene-α-d-glucopyranose: synthesis and characterization of glycosylamines, and the crystal structure of 4,6-O-butylidene…

2002

A total of nine glycosylamines of 4,6-O-butylidene-α-D-glucopyranose were synthesized using primary amines having various groups in their ortho- or para-positions. Among these, six are monoglycosylamines, including one primary glycosylamine, and three are bis-glycosylamines. All these compounds were characterized by 1H, 1H–1H COSY, 1H–13C COSY and 13C NMR spectroscopy and FTIR spectra. The FAB mass spectra provided the molecular weights of the products by exhibiting the corresponding molecular ion peaks. The crystal structure of 4,6-O-butylidene-N-(o-chlorophenyl)-β-D-glucopyranosylamine revealed the C-1 glycosylation, the β-anomeric nature, and the 4C1 chair conformation of the saccharide …

GlycosylamineGlucosamineGlycosylationGlycosylationStereochemistryDimerOrganic ChemistryCyclohexane conformationPolyatomic ionSynthesis (Chemical)General MedicineCrystal structureBiochemistryAnalytical ChemistryConformationsMolecular WeightCrystallographychemistry.chemical_compoundX-Ray DiffractionchemistryCarbohydrate ConformationMass spectrumCarbohydrate conformationAminesCrystallizationCarbohydrate Research
researchProduct

LRP1 modulates APP trafficking along early compartments of the secretory pathway

2008

The amyloid beta peptide (A beta) is a central player in Alzheimer's disease (AD) pathology. A beta liberation depends on APP cleavage by beta- and gamma-secretases. The low density lipoprotein receptor related protein 1 (LRP1) was shown to mediate APP processing at multiple steps. Newly synthesized LRP1 can interact with APP, implying an interaction between these two proteins early in the secretory pathway. We wanted to investigate whether LRP1 mediates APP trafficking along the secretory pathway, and, if so, whether it affects APP processing. Indeed, the early trafficking of APP within the secretory pathway is strongly influenced by its interaction with the C-terminal domain of LRP1. The …

GlycosylationAmyloid betaAmino Acid MotifsPlaque AmyloidCHO CellsSecretory pathwayTrafficinglcsh:RC321-571Amyloid beta-Protein PrecursorCricetulusAlzheimer DiseaseCricetinaemental disordersAmyloid precursor proteinAnimalsHumansReceptorlcsh:Neurosciences. Biological psychiatry. NeuropsychiatrySecretory pathwayNeuronsAmyloid beta-PeptidesbiologyLow density lipoprotein receptor related proteinBrainLRP1Cell CompartmentationProtein Structure TertiaryCell biologyProtein TransportNeurologyBiochemistryAlpha secretaseRetentionAmyloid precursor proteinLDL receptorbiology.proteinLiberationProtein Processing Post-TranslationalLow Density Lipoprotein Receptor-Related Protein-1Signal TransductionNeurobiology of Disease
researchProduct