Search results for "Fucose"

showing 10 items of 28 documents

Differences between the Glycosylation Patterns of Haptoglobin Isolated from Skin Scales and Plasma of Psoriatic Patients

2012

Improved diagnosis of psoriasis, by new biomarkers, is required for evaluating the progression rate of the disease and the response to treatment. Haptoglobin (Hpt), a glycoprotein secreted by hepatocytes and other types of cells including keratinocytes, was found with glycan changes in psoriasis and other diseases. We previously reported that Hpt isolated from plasma of psoriatic patients is more fucosylated than Hpt of healthy subjects. The aim of this study was to compare the glycosylation pattern of Hpt isolated from skin scales or plasma of patients with psoriasis with that of Hpt from cornified epidermal layer or plasma of healthy subjects. High performance liquid chromatography analys…

GlycosylationGlycobiologylcsh:MedicineDermatologic PathologyBiochemistryMass SpectrometryFucosechemistry.chemical_compoundLectinsBlood plasmalcsh:ScienceChromatography High Pressure LiquidFucosylationchemistry.chemical_classificationglycanMultidisciplinarybiologyHaptoglobinGlycopeptideshaptoglobinMedicineResearch ArticleAdultskinProtein Structuremedicine.medical_specialtyGlycanGlycosylationInflammatory DiseasesImmunologyDermatologyAutoimmune DiseasesPolysaccharidesInternal medicinePsoriasismedicinePsoriasisHumansAmino Acid SequenceImmunoassaysBiologyGlycoproteinsHaptoglobinslcsh:RProteinsmedicine.diseasecarbohydrates (lipids)EndocrinologychemistryImmunologyImmunologic Techniquesbiology.proteinglycanslectinClinical Immunologylcsh:QGlycoproteinBiomarkers
researchProduct

A lytic mechanism based on soluble phospholypases A2 (sPLA2) and b-galactoside specific lectins is exerted by Ciona intestinalis (ascidian) unilocula…

2011

Abstract Hemocytes from the ascidian Ciona intestinalis exert in vitro Ca 2+ -dependent cytotoxic activity toward mammalian erythrocytes and K562 cells. To examine the lytic mechanism, hemocyte populations were separated (B1–B6 bands) through a Percoll discontinuous density gradient, the hemocyte cytotoxic activity (HCA) and the lytic activity of the hemocyte lysate supernatant (HLS) were assayed. In addition the separated hemocytes were cultured and the cell-free culture medium (CFM) assayed after 3 h culture. Results support that unilocular refractile hemocytes (URGs), enriched in B5, are cytotoxic. The B5-HLS contains lysins and the activity of B5-CFM shows that lysins can be released in…

HemocytesPhospholipase A2 Inhibitorsmedicine.medical_treatmentLysinDibucaineSettore BIO/05 - ZoologiaAquatic ScienceBiologyFucoseCell membranechemistry.chemical_compoundmedicineEnvironmental ChemistryAnimalsHumansCiona intestinalisLectins C-TypeEnzyme InhibitorsProteaseErythrocyte MembraneGeneral Medicinebiology.organism_classificationCytotoxicity Tests Immunologicbeta-GalactosidaseGalactosideCiona intestinalisPhospholipases A2medicine.anatomical_structurechemistryBiochemistryLytic cycleInvertebrate immunity Ciona intestinalis Hemocyte Cytotoxicity Soluble phospholipase A2 Rabbit erythrocyte K562QuinacrineCaspasesImmunologyMicroscopy Electron ScanningRabbitsK562 CellsPercoll
researchProduct

Unique Microbial Catabolic Pathway for the Human Core N-Glycan Constituent Fucosyl-α-1,6-N-Acetylglucosamine-Asparagine

2020

The survival of commensal bacteria in the human gut partially depends on their ability to metabolize host-derived molecules. The use of the glycosidic moiety of N-glycoproteins by bacteria has been reported, but the role of N-glycopeptides or glycoamino acids as the substrates for bacterial growth has not been evaluated. We have identified in Lactobacillus casei strain BL23 a gene cluster (alf-2) involved in the catabolism of the glycoamino acid fucosyl-α-1,6-N-GlcNAc-Asn (6′FN-Asn), a constituent of the core-fucosylated structures of mammalian N-glycoproteins. The cluster consists of the genes alfHC, encoding a major facilitator superfamily (MFS) permease and the α-l-fucosidase AlfC, and t…

Lactobacillus caseiGlycanMolecular Biology and Physiologyalpha-l-fucosidaseGlycosylasparaginaseMicrobiologiacore fucosylationGut floraMicrobiologydigestive systemFucosylated Nglycopeptideschemistry.chemical_compoundVirologyfucosylated N-glycopeptidesN-AcetylglucosamineHumansAsparagineSymbiosisFucosebiologyHost Microbial InteractionsChemistryProbioticsbiology.organism_classificationMajor facilitator superfamilyQR1-502LactobacilsglycosylasparaginaseCore fucosylationGastrointestinal TractMetabolic pathwayLacticaseibacillus caseiBiochemistryAlpha-L-fucosidaseMultigene Familybiology.proteinAsparagineLactobacillus caseiBacteriaMetabolic Networks and PathwaysResearch Article
researchProduct

Terpioside B, a difucosyl GSL from the marine sponge Terpios sp. is a potent inhibitor of NO release.

2010

Terpioside B (2a), a unique glycolipid containing two fucose residues in the furanose form in its pentasaccharide chain, was isolated from the marine sponge Terpios sp. Its complete stereostructure was solved by interpretation of mass spectrometric and NMR data along with CD and GG-MS analyses of its degradation products. Terpioside B is a potent inhibitor against LPS-induced NO release, and is considerably more active than simpler glycosphingolipids such as terpioside A and monoglucosylceramide.

LipopolysaccharidesTerpiosStereochemistryClinical BiochemistryMolecular ConformationPharmaceutical ScienceNitric Oxide01 natural sciencesBiochemistryFucoseCell Line03 medical and health scienceschemistry.chemical_compoundGlycolipidDrug DiscoveryAnimalsMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesbiology010405 organic chemistryChemistryMacrophagesOrganic ChemistryAbsolute configurationGlycosphingolipidOligosaccharideMacrophage Activationbiology.organism_classificationFuranose0104 chemical sciencesPoriferaSpongeBiochemistryMolecular MedicineGlycolipidsBioorganicmedicinal chemistry
researchProduct

Synthesis of glycopeptides and neoglycoproteins containing the fucosylated linkage region of N-glycoproteins.

1994

Abstract N-Glycoproteins fucosylated in the core region occur in tumor membranes and virus envelopes. Partial structures of such N-glycoproteins containing fucosylated chitobiosyl asparagine conjugates were synthesized using the allyloxycarbonyl (Aloc) and the tert-butyl ester protecting groups in the peptide portion. As the α-fucosidic bond of the conjugates revealed to be very sensitive to acids when carrying ether-type protecting groups, a method for exchanging the protecting groups of the fucose portion of saccharides was developed. Conjugates containing O-acetyl protected fucose proved to be stable against acids used in glycopeptide syntheses. These methods were applied in the synthesi…

Magnetic Resonance SpectroscopyGlycoconjugateClinical BiochemistryMolecular Sequence DataPharmaceutical SciencePeptideChitobioseDisaccharidesBiochemistryFucosechemistry.chemical_compoundViral ProteinsViral envelopeDrug DiscoveryAsparagineAmino Acid SequenceBovine serum albuminMolecular BiologyGlucansFucoseGlycoproteinschemistry.chemical_classificationbiologyOrganic ChemistryGlycopeptidesFucosyltransferasesGlycopeptidechemistryBiochemistryCarbohydrate Sequencebiology.proteinMolecular MedicineAsparagineBioorganicmedicinal chemistry
researchProduct

The possible association of clusterin fucosylation changes with male fertility disorders

2021

AbstractIn the seminal plasma (n = 118) and serum (n = 90) clusterin (CLU) the fucosylation and the expression of selected fucosyltransferases (FUTs) were analyzed. Samples from infertile men were divided into groups based on the results of the standard semen analysis: normozoospermic (N), teratozoospermic (T), asthenoteratozoospermic (AT) and oligoasthenoteratozoospermic (OAT). The CLU fucosylation was analyzed using lectin-ELISAs with biotinylated lectins specific to α1,3-, α1,2-linked antennary fucose, and α1,6-linked core fucose (LTA, UEA, and LCA, respectively). The concentrations of FUT3 and FUT4, reflecting the expression of Le oligosaccharide structures, were measured using ELISA te…

Male0301 basic medicineGlycosylationMolecular biologyScienceDiseasesBiologySemen analysisArticleFucoseMale infertilityAndrologyFucosyltransferases03 medical and health scienceschemistry.chemical_compound0302 clinical medicineBlood serumPolysaccharidesmedicineHumansInfertility MaleFucosylation030219 obstetrics & reproductive medicineMultidisciplinaryClusterinmedicine.diagnostic_testQRmedicine.diseaseSpermClusterin030104 developmental biologychemistrybiology.proteinMedicineBiomarkersScientific Reports
researchProduct

Distribution patterns in glycoconjugate expression during the development of the rat palate.

1994

The distribution of complex carbohydrate structures during the embryonic development of the rat palate was analysed by examining lectin-binding patterns in serial paraffin and cryostat sections. With few exceptions, the binding patterns showed a general increase in lectin receptors in the more developed stages of palatogenesis. High mannose oligosaccharides were especially amplified during development. Terminal fucose molecules were not expressed. In contrast, terminal sialic acid molecules were ubiquitously distributed in epithelial and mesenchymal tissues. Non-sialylated terminal N-acetylglucosamine was specifically restricted to evolving bone matrix. Before palatal fusion, quantitative b…

MaleGlycoconjugateMolecular Sequence DataOligosaccharidesFucoseAcetylglucosamineRats Sprague-Dawleychemistry.chemical_compoundPregnancyLectinsmedicineAnimalsTissue DistributionReceptorFucosechemistry.chemical_classificationParaffin EmbeddingbiologyPalateLectinGalactoseCell BiologyImmunohistochemistryEpitheliumCell biologySialic acidExtracellular MatrixRatsmedicine.anatomical_structureGlucosechemistryBiochemistryCarbohydrate Sequencebiology.proteinJacalinBasal laminaFemaleAnatomyGlycoconjugatesMannoseThe Histochemical journal
researchProduct

Infant Gut Microbial Metagenome Mining of α- l -Fucosidases with Activity on Fucosylated Human Milk Oligosaccharides and Glycoconjugates

2022

The gastrointestinal microbiota members produce α-l-fucosidases that play key roles in mucosal, human milk, and dietary oligosaccharide assimilation. Here, 36 open reading frames (ORFs) coding for putative α-l-fucosidases belonging to glycosyl hydrolase family 29 (GH29) were identified through metagenome analysis of breast-fed infant fecal microbiome. Twenty-two of those ORFs showed a complete coding sequence with deduced amino acid sequences displaying the highest degree of identity with α-l-fucosidases from Bacteroides thetaiotaomicron, Bacteroides caccae, Phocaeicola vulgatus, Phocaeicola dorei, Ruminococcus gnavus, and Streptococcus parasanguinis. Based on sequence homology, 10 α-l-fuco…

Microbiology (medical)PhysiologyInfant gutMicrobiologiaHisto-blood group antigensOligosaccharidesPolysaccharidesGeneticsAnimalsHumansα-l-fucosidaseGlycoproteinsFucoseMammalsalpha-L-FucosidaseMilk HumanGeneral Immunology and MicrobiologyEcologyMicrobiotaHuman milk oligosaccharidesInfant NewbornInfantCell BiologyGastrointestinal MicrobiomeGenòmicaInfectious DiseasesBlood Group AntigensMetagenomeGlycoconjugatesMicrobiology Spectrum
researchProduct

Polymeric Selectin Ligands Mimicking Complex Carbohydrates: From Selectin Binders to Modifiers of Macrophage Migration

2016

Novel polymeric cell adhesion inhibitors were developed in which the selectin tetrasaccharide sialyl-LewisX (SLeX ) is multivalently presented on a biocompatible poly(2-hydroxypropyl)methacrylamide (PHPMA) backbone either alone (P1) or in combination with O-sulfated tyramine side chains (P2). For comparison, corresponding polymeric glycomimetics were prepared in which the crucial "single carbohydrate" substructures fucose, galactose, and sialic acid side chains were randomly linked to the PHPMA backbone (P3 or P4 (O-sulfated tyramine)). All polymers have an identical degree of polymerization, as they are derived from the same precursor polymer. Binding assays to selectins, to activated endo…

OligosaccharidesTyramine02 engineering and technologyLigands010402 general chemistry01 natural sciencesCatalysisFucoseInhibitory Concentration 50chemistry.chemical_compoundPolymethacrylic AcidsCell MovementHuman Umbilical Vein Endothelial CellsSide chainHumansTetrasaccharideMethacrylamideSialyl Lewis X AntigenCell adhesionCells CulturedMacrophagesGeneral ChemistrySurface Plasmon ResonanceFlow Cytometry021001 nanoscience & nanotechnologyIn vitro0104 chemical sciencesSialic acidMicroscopy Fluorescence MultiphotonNanomedicinechemistryBiochemistrySelectins0210 nano-technologySelectinAngewandte Chemie International Edition
researchProduct

F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacter…

2021

Abstract The increasing availability of sequenced genomes has enabled a deeper understanding of the complexity of fish lectin repertoires involved in early development and immune recognition. The teleost fucose-type lectin (FTL) family includes proteins that preferentially bind fucose and display tandemly arrayed carbohydrate-recognition domains (CRDs) or are found in mosaic combinations with other domains. They function as opsonins, promoting phagocytosis and the clearance of microbial pathogens. The Antarctic fish Trematomus bernacchii is a Perciforme living at extremely low temperatures (−1.68 °C) which is considered a model for studying adaptability to the variability of environmental w…

PhysiologyAntarctic fishLectins F-type lectin Antarctic fish Trematomus bernacchii Bacterial agglutinationAntarctic RegionsTrematomus bernacchiiBiochemistryAntarctic fish; Bacterial agglutination; F-type lectin; Lectins; Trematomus bernacchii; Amino Acid Sequence; Animals; Antarctic Regions; Bacteria; Base Sequence; Fucose; Lectins; Perciformes; PhylogenyFucose03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAffinity chromatographyWestern blotLectinsTrematomusmedicineAnimalsAmino Acid SequenceSea bassPerciformeMolecular BiologyOpsoninPhylogeny030304 developmental biologyFucoseAntarctic Region0303 health sciencesbiologyMolecular massmedicine.diagnostic_testBacteriaBase SequenceAnimalLectinBacterial agglutinationbiology.organism_classificationPerciformesBiochemistrychemistrybiology.proteinLectinF-type lectin030215 immunologyComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
researchProduct