Search results for "glycoproteins"

showing 10 items of 496 documents

Dysbiosis and zonulin upregulation alter gut epithelial and vascular barriers in patients with ankylosing spondylitis

2017

BackgroundDysbiosis has been recently demonstrated in patients with ankylosing spondylitis (AS) but its implications in the modulation of intestinal immune responses have never been studied. The aim of this study was to investigate the role of ileal bacteria in modulating local and systemic immune responses in AS.MethodsIleal biopsies were obtained from 50 HLA-B27+ patients with AS and 20 normal subjects. Silver stain was used to visualise bacteria. Ileal expression of tight and adherens junction proteins was investigated by TaqMan real-time (RT)-PCR and immunohistochemistry. Serum levels of lipopolysaccharide (LPS), LPS-binding protein (LPS-BP), intestinal fatty acid-BP (iFABP) and zonulin…

Genetics and Molecular Biology (all)Fatty Acid-Binding ProteinAnkylosing SpondylitisMonocyteBiochemistryMonocytesTransgenic0302 clinical medicineIntestinal MucosaMembrane GlycoproteinsZonulinCadherinsAdherens JunctionUp-RegulationAntigenAcute DiseaseMembrane GlycoproteinRats TransgenicInfectionHumanAnkylosingImmunologyGeneral Biochemistry Genetics and Molecular BiologyArticlePermeabilityTight Junctions03 medical and health sciencesRheumatologyAntigens CDIleumAnti-Bacterial AgentHuman Umbilical Vein Endothelial CellsHumansRNA MessengerEndotheliumProtein PrecursorsAnkylosing SpondylitiBiochemistry Genetics and Molecular Biology (all)BacteriaAnimalmedicine.diseaseDysbiosiSettore MED/16 - Reumatologia030104 developmental biologychemistryCase-Control StudiesImmunologyRatCarrier ProteinsAcute-Phase ProteinsSpondylitis0301 basic medicineLipopolysaccharidesLipopolysaccharideMessengerAcute-Phase ProteinGene Expressionchemistry.chemical_compoundIntestinal mucosaImmunology and AllergyMembrane ProteinHLA-B27 AntigenCaco-2 CellTight junctionTight JunctionAdherens JunctionsIleitisIleitiAnti-Bacterial AgentsCDmedicine.anatomical_structureAnkylosing Spondylitis; Infections; Inflammation; Acute Disease; Acute-Phase Proteins; Adherens Junctions; Animals; Anti-Bacterial Agents; Antigens CD; Bacteria; Caco-2 Cells; Cadherins; Carrier Proteins; Case-Control Studies; Cholera Toxin; Chronic Disease; Dysbiosis; Endothelium; Fatty Acid-Binding Proteins; Gene Expression; HLA-B27 Antigen; Human Umbilical Vein Endothelial Cells; Humans; Ileitis; Ileum; Interleukin-8; Intestinal Mucosa; Junctional Adhesion Molecule A; Lipopolysaccharides; Membrane Glycoproteins; Membrane Proteins; Monocytes; Permeability; RNA Messenger; Rats; Rats Transgenic; Spondylitis Ankylosing; Tight Junctions; Up-Regulationmedicine.symptomCase-Control StudieCholera ToxinHuman Umbilical Vein Endothelial CellLipopolysaccharideInflammationInfectionsFatty Acid-Binding ProteinsAdherens junctionmedicineAnkylosing Spondylitis; Infections; Inflammation; Acute Disease; Acute-Phase Proteins; Adherens Junctions; Animals; Anti-Bacterial Agents; Antigens CD; Bacteria; Caco-2 Cells; Cadherins; Carrier Proteins; Case-Control Studies; Cholera Toxin; Chronic Disease; Dysbiosis; Endothelium; Fatty Acid-Binding Proteins; Gene Expression; HLA-B27 Antigen; Human Umbilical Vein Endothelial Cells; Humans; Ileitis; Ileum; Interleukin-8; Intestinal Mucosa; Junctional Adhesion Molecule A; Lipopolysaccharides; Membrane Glycoproteins; Membrane Proteins; Monocytes; Permeability; RNA Messenger; Rats; Rats Transgenic; Spondylitis Ankylosing; Tight Junctions; Up-Regulation; Immunology and Allergy; Rheumatology; Immunology; Biochemistry Genetics and Molecular Biology (all)AnimalsSpondylitis AnkylosingAntigensSpondyliti030203 arthritis & rheumatologyInflammationHaptoglobinsbusiness.industryMonocyteInterleukin-8Membrane ProteinsRatsJunctional Adhesion Molecule AChronic DiseaseCadherinDysbiosisRNACaco-2 CellsCarrier ProteinbusinessDysbiosis
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Cystinuria subtype and nephrolithiasis

1999

GeneticsMembrane glycoproteinsBiochemistryNephrologyCarrier proteinMutation (genetic algorithm)biology.proteinmedicineCystinuriaBiologymedicine.diseaseKidney International
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Genotyping of a nosocomial outbreak of pandemic influenza A/H1N1 2009

2011

Background: Epidemiological surveys have revealed outbreaks of pandemic influenza A (H1N1) 2009 in several different contexts. Molecular characterization of the influenza virus could help to provide a more accurate description of these outbreaks. Objective: To genotype pandemic influenza A (H1N1) 2009 isolates from an epidemiologically defined nosocomial outbreak. Study design: We sequenced the neuraminidase (NA) and hemagglutinin (HA) influenza A (H1N1) 2009 genes from ten HIV-positive patients involved in an epidemiologically defined outbreak in the Clinical Microbiology and Infectious Diseases (CMID) Department. Sequences were aligned to search for specific genetic features of the involv…

Genotyping TechniquesGenotypeMolecular Sequence DataNeuraminidaseHemagglutinin Glycoproteins Influenza VirusContext (language use)medicine.disease_causePandemic H1N1Disease OutbreaksViral ProteinsInfluenza A Virus H1N1 SubtypeVirologyPandemicHIV SeropositivityInfluenza HumanInfluenza A virusmedicineHumansViral ProteinSequencingHemagglutinin Glycoproteins Influenza ViruPandemicsGenotypingPhylogenyCross InfectionDisease OutbreakbiologyPandemicCoinfectionTransmissibilityOutbreakvirus diseasesOutbreakVirologyInfluenza A virus subtype H5N1Infectious DiseasesAmino Acid SubstitutionMutationbiology.proteinHuman mortality from H5N1Genotyping TechniqueNeuraminidaseHuman
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Molecular organization of selected prokaryotic S-layer proteins.

2005

Regular crystalline surface layers (S-layers) are widespread among prokaryotes and probably represent the earliest cell wall structures. S-layer genes have been found in approximately 400 different species of the prokaryotic domains bacteria and archaea. S-layers usually consist of a single (glyco-)protein species with molecular masses ranging from about 40 to 200 kDa that form lattices of oblique, tetragonal, or hexagonal architecture. The primary sequen ces of hyperthermophilic archaeal species exhibit some characteristic signatures. Further adaptations to their specific environments occur by various post-translational modifications, such as linkage of glycans, lipids, phosphate, and sulf…

GlycanArchaeal ProteinsImmunologyMolecular Sequence DataApplied Microbiology and BiotechnologyMicrobiologyCell wallBacterial ProteinsCell WallGeneticsExtracellularMolecular BiologyGeneMembrane GlycoproteinsbiologyBacteriaBase SequenceGeneral Medicinebiology.organism_classificationArchaeaBiochemistryCytoplasmbiology.proteinProtein stabilizationBacteriaArchaeaCanadian journal of microbiology
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Isolation and characterization of a 60-70-kD plasma membrane glycoprotein involved in the contact-dependent inhibition of growth

1990

Previous studies have shown that plasma membrane compounds are involved in the contact-dependent inhibition of growth of human diploid fibroblasts. The purification of the active plasma membrane glycoprotein is described in this report. The glycoprotein has an apparent molecular mass of 60-70 kD and, due to differential sialylation, isoelectric points between pH 5.5. and 6.2. Treatment with sialidase yielded one spot in two-dimensional gel electrophoresis with an isoelectric point of 6.3. After removal of the N-glycosidically linked oligosaccharide chains, the apparent molecular mass is reduced by approximately 22 kD. Treatment was diluted NaOH, which removes the O-glycosidically linked por…

GlycanCell CommunicationCell LineAnimalsHumansPolyacrylamide gel electrophoresisCells CulturedCytoskeletonGel electrophoresischemistry.chemical_classificationMembrane GlycoproteinsbiologyMolecular massContact InhibitionCell MembraneContact inhibitionCell BiologyArticlesFibroblastsMolecular biologyMolecular WeightMicroscopy ElectronIsoelectric pointchemistryBiochemistryCell culturebiology.proteinChromatography GelElectrophoresis Polyacrylamide GelGlycoproteinCell DivisionThe Journal of Cell Biology
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Contact-dependent inhibition of growth of normal diploid human fibroblasts by plasma membrane glycoproteins.

1988

Homeostasis in vivo is maintained by a highly complex network of positive and negative signals. At the cellular level, this regulatory microenvironment can be divided, in a simplified fashion, into two major compartments: the humoral compartment, including compounds such as hormones, growth factors and nutrients, and the contact-environment compartment, including cell-cell and cell-matrix interactions. At least in cultures of diploid, non-transformed cells, cell-cell and cell-matrix interactions have been shown to be of major importance for the regulation of growth as well as of differentiation. Although until now the glycoprotein involved in the contact-dependent inhibition of growth has n…

GlycanCell CommunicationPlatelet Membrane GlycoproteinsBiochemistrychemistry.chemical_compoundmedicineCompartment (development)AnimalsHumansReceptors ImmunologicFibroblastReceptorCells Culturedchemistry.chemical_classificationMembrane GlycoproteinsbiologyContact InhibitionCell MembraneAntibodies MonoclonalBiological activityGeneral MedicineFibroblastsMembrane glycoproteinsmedicine.anatomical_structureCell Transformation NeoplasticchemistryBiochemistryPlatelet Glycoprotein GPIb-IX Complexbiology.proteinGrowth inhibitionGlycolipidsGlycoproteinCell DivisionBiochimie
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Role of the Netrin-like Domain of Procollagen C-Proteinase Enhancer-1 in the Control of Metalloproteinase Activity

2010

The netrin-like (NTR) domain is a feature of several extracellular proteins, most notably the N-terminal domain of tissue inhibitors of metalloproteinases (TIMPs), where it functions as a strong inhibitor of matrix metalloproteinases and some other members of the metzincin superfamily. The presence of a C-terminal NTR domain in procollagen C-proteinase enhancers (PCPEs), proteins that stimulate the activity of astacin-like tolloid proteinases, raises the possibility that this might also have inhibitory activity. Here we show that both long and short forms of the PCPE-1 NTR domain, the latter beginning at the N-terminal cysteine known to be critical for TIMP activity, show no inhibition, at …

Glycobiology and Extracellular MatricesMatrix metalloproteinaseBiochemistryBONE MORPHOGENETIC PROTEIN-1AdamalysinFIBRILLAR PROCOLLAGENSTolloid ProteinaseExtracellular Matrix Proteins0303 health sciencesADAMTSFRIZZLED-RELATED PROTEINS030302 biochemistry & molecular biologyTissue Inhibitor of Metalloproteinases11 Medical And Health SciencesALPHA-CONVERTING-ENZYMEI PROCOLLAGENADAM ProteinsExtracellular MatrixPLASMINOGEN ACTIVATIONBiochemistryCollagen03 Chemical SciencesLife Sciences & BiomedicineProcollagenBiochemistry & Molecular BiologyTERMINAL DOMAINTolloid-Like MetalloproteinasesADAMTSBiologyBone morphogenetic protein 1Cell Line03 medical and health sciencesDisintegrinHumansHUMAN TISSUE INHIBITORMatrix MetalloproteinaseMolecular BiologyGlycoproteins030304 developmental biologyThrombospondinScience & TechnologyHeparinADAMCell Biology06 Biological SciencesMATRIX-METALLOPROTEINASESProtein Structure TertiaryADAM ProteinsProcollagen peptidaseSULFATED GLYCOSAMINOGLYCANSEnzymologybiology.proteinJournal of Biological Chemistry
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Synthesis of undulin by rat liver fat-storing cells: Comparison with fibronectin and tenascin

1992

Abstract Fat-storing cells (FSCs) are known to synthesize various components of the hepatic extracellular matrix and thereby play an important role during liver fibrogenesis. The aim of our study was to investigate the synthesis of undulin, a recently described connective tissue protein belonging to the fibronectin—tenascin superfamily of glycoproteins, by fat-storing cells in primary culture. SDS-PAGE analysis of immunoprecipitates from cell layer lysates or media pulse-labeled with radioactive methionine revealed undulin-specific bands A (270 kDa), B1 (190 kDa), and B2 (180 kDa) after reduction. A single undulin-specific transcript was detected at about 7 kb. Undulin synthesized by cell-f…

GlycosylationCell Adhesion Molecules NeuronalMolecular Sequence DataTenascinConnective tissueExtracellular matrixchemistry.chemical_compoundBiosynthesisAdipocytemedicineAnimalsRNA MessengerRats WistarConnective Tissue CellsGlycoproteinschemistry.chemical_classificationExtracellular Matrix ProteinsBase SequencebiologyTunicamycinTenascinCell BiologyTunicamycinFibronectinsRatsCell biologyFibronectinKineticsmedicine.anatomical_structureLiverBiochemistrychemistryConnective TissueProtein Biosynthesisbiology.proteinFemaleCollagenOligonucleotide ProbesGlycoproteinProtein Processing Post-TranslationalExperimental Cell Research
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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
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Evidence for the formation of covalent bonds between macromolecules in the domain of the wall of Candida albicans mycelial cells

1989

An O-glycosylated mannoprotein, after its incorporation into the wall, showed an increase in its molecular weight, due at least to its association with N-glycosidic sugar chain(s). This was shown by rendering the material soluble after partial degradation of the wall structure. At present it is unknown whether this phenomenon is due to an additional transglycosylation process or whether the partial degradation of the wall solubilizes a supramolecular structure formed between the original O-glycosylated protein which becomes linked either directly or indirectly through a protein to the N-sugar chain(s).

GlycosylationMacromolecular SubstancesBlotting WesternBiophysicsSupramolecular chemistryPolysaccharideBiochemistryFungal ProteinsCell wallCell WallCandida albicansCandida albicansMolecular Biologychemistry.chemical_classificationGel electrophoresisMembrane Glycoproteinsbiologybeta-GlucosidaseAntibodies MonoclonalGlucan 13-beta-GlucosidaseCell Biologybiology.organism_classificationMolecular Weightcarbohydrates (lipids)ProteoglycanBiochemistrychemistryCovalent bondbiology.proteinBiophysicsProtein Processing Post-TranslationalMacromoleculeBiochemical and Biophysical Research Communications
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