Search results for "glycan"

showing 10 items of 237 documents

Inhibition of glycosaminoglycan modification of perlecan domain I by site-directed mutagenesis changes protease sensitivity and laminin-1 binding act…

1998

AbstractGlycosaminoglycan attachment to perlecan domain I (173 residues) was completely prevented by site-directed mutagenesis of Ser-65, Ser-71 and Ser-76 as shown by recombinant production in mammalian cells. This did not interfere with the proper folding of the domain's SEA module but enhanced its sensitivity to neutral proteases. Lack of substitution also abolished binding to the two major heparin binding sites of laminin-1.

ProteasesBasement membraneRecombinant proteinmedicine.medical_treatmentMolecular Sequence DataBiophysicsPerlecanBiochemistrySubstrate SpecificityStructural BiologyLamininEndopeptidasesGeneticsmedicineAnimalsAmino Acid SequenceBinding siteSite-directed mutagenesisMolecular BiologyGlycosaminoglycansSite-directed mutagenesisBinding SitesProteasebiologyChemistryMutagenesisCell BiologyRecombinant ProteinsBiochemistryProteoglycanProteoglycanProteolysisMutagenesis Site-Directedbiology.proteinProteoglycansHeparitin SulfateLamininHeparan Sulfate ProteoglycansProtein BindingFEBS Letters
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Heparan sulfate proteoglycans interact exclusively with conformationally intact HPV L1 assemblies: basis for a virus-like particle ELISA.

2004

In this article, we demonstrate that interaction of human papillomavirus-like particles (HPV-VLPs) with the putative glucosaminoglycan binding receptor is strictly dependent on conformational integrity. Such conformations are present on VLPs and capsomeres but not on monomers of the major capsid protein, L1, confirming reports that capsomeres can induce virus-neutralizing antibodies. Furthermore, we show the suitability of this specific interaction for development of VLP-based enzyme-linked immunosorbent assays (ELISAs), using heparin for indirect coupling of VLPs to microtiter plates, which may add an intrinsic quality control. This avoids presentation of linear, often highly cross-reactiv…

Protein DenaturationProtein ConformationvirusesEnzyme-Linked Immunosorbent AssayPlasma protein bindingCross ReactionsAntibodies ViralEpitopeEpitopesProtein structureVirus-like particleNeutralization TestsVirologyCentrifugation Density GradientHumansPapillomaviridaeGlycosaminoglycansbiologyHeparinCapsomerevirus diseasesOncogene Proteins ViralVirologyInfectious DiseasesProteoglycanCapsidbiology.proteinReceptors VirusCapsid ProteinsHeparan Sulfate ProteoglycansConformational epitopeProtein BindingJournal of medical virology
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Unraveling the role of the secretor antigen in human rotavirus attachment to histo-blood group antigens

2019

25 Páginas, 7 figuras, 2 tablas

RNA virusesRotavirusViral DiseasesPhysiologyViral Nonstructural ProteinsPathology and Laboratory MedicineCrystallography X-Raymedicine.disease_causeBiochemistryBinding AnalysisReovirusesImmune PhysiologyRotavirusMedicine and Health SciencesChemical PrecipitationBiology (General)Antigens ViralGastroenterologiachemistry.chemical_classification0303 health sciencesImmune System ProteinsCrystallographyMolecular StructurebiologyPhysics030302 biochemistry & molecular biologyChemical ReactionsRNA-Binding ProteinsCondensed Matter PhysicsLigand (biochemistry)Amino acidChemistryInfectious DiseasesMedical MicrobiologyViral PathogensVirusesPhysical SciencesCrystal StructurePathogensCrystallizationResearch ArticleChemical ElementsGlycanQH301-705.5Virus RNAViral proteinImmunologyResearch and Analysis MethodsMicrobiologyABO Blood-Group SystemCell Line03 medical and health sciencesAntigenVirologyGeneticsmedicineSolid State PhysicsHumansAntigensBinding siteMicrobial PathogensMolecular BiologyRotavirus InfectionChemical Characterization030304 developmental biologyChemical PhysicsBinding SitesBiology and life sciencesMutagenesisOrganismsProteinsRC581-607Molecular biologyCarbonchemistrybiology.proteinCapsid ProteinsParasitologyImmunologic diseases. AllergyPLOS Pathogens
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The Proteoglycan NG2 Is Complexed with α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors by the PDZ Glutamate Receptor Interactio…

2003

The proteoglycan NG2 is expressed by immature glial cells in the developing and adult central nervous system. Using the COOH-terminal region of NG2 as bait in a yeast two-hybrid screen, we identified the glutamate receptor interaction protein GRIP1, a multi-PDZ domain protein, as an interacting partner. NG2 exhibits a PDZ binding motif at the extreme COOH terminus which binds to the seventh PDZ domain of GRIP1. In addition to the published expression in neurons, GRIP1 is expressed by immature glial cells. GRIP1 is known to bind to the GluRB subunit of the AMPA glutamate receptor expressed by subpopulations of neurons and immature glial cells. In cultures of primary oligodendrocytes, cells c…

Receptor complexbiologyProtein subunitPDZ domainProtein domainGlutamate receptorCell BiologyAMPA receptorTransfectionBiochemistryMolecular biologynervous systemProteoglycanbiology.proteinMolecular BiologyJournal of Biological Chemistry
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High-Generation Amphiphilic Janus-Dendrimers as Stabilizing Agents for Drug Suspensions

2018

Pharmaceutical nanosuspensions are formed when drug crystals are suspended in aqueous media in the presence of stabilizers. This technology offers a convenient way to enhance the dissolution of poorly water-soluble drug compounds. The stabilizers exert their action through electrostatic or steric interactions, however, the molecular requirements of stabilizing agents have not been studied extensively. Here, four structurally related amphiphilic Janus-dendrimers were synthesized and screened to determine the roles of different macromolecular domains on the stabilization of drug crystals. Physical interaction and nanomilling experiments have substantiated that Janus-dendrimers with fourth gen…

Recrystallization (geology)huumeetPolymers and Plastics116 Chemical sciences02 engineering and technology01 natural sciencesdrugsContact angleMaterials ChemistryHUMAN LECTINSSurface plasmon resonanceta116chemistry.chemical_classificationChemistryBIOLOGICAL-MEMBRANES021001 nanoscience & nanotechnologyPROGRAMMABLE GLYCAN LIGANDSINDOMETHACIN317 PharmacyCLICK CHEMISTRYfarmaseuttinen kemia0210 nano-technologyHydrophobic and Hydrophilic InteractionsDendrimersSURFACEBioengineeringPoloxamer010402 general chemistryRSPOORLY SOLUBLE DRUGBiomaterialsHydrophobic effectSurface-Active AgentsSuspensionslääkeyhdisteetDendrimerAmphiphileGLYCODENDRIMERSOMESta216ta215AlkylMODULAR SYNTHESISWaterPoloxamerCombinatorial chemistry0104 chemical scienceslääkkeet1182 Biochemistry cell and molecular biologypharmaceutical nanosuspensionsCOMPLEX ARCHITECTURESBiomacromolecules
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Identification of a β-Dystroglycan Immunoreactive Subcompartment in Photoreceptor Terminals

2005

PURPOSE Mutations in the dystrophin-associated glycoprotein complex (DGC) cause various forms of muscular dystrophy. These diseases are characterized by progressive loss of skeletal muscle tissue and by dysfunctions in the central nervous system (CNS). The CNS deficits include an altered electroretinogram, caused by an impaired synaptic transmission between photoreceptors and their postsynaptic target cells in the outer plexiform layer (OPL). The DGC is concentrated in the OPL but its exact distribution is controversial. Therefore, the precise distribution of beta-dystroglycan, the central component of the DGC, within the OPL of the mature chick retina, was determined. METHODS Double immuno…

Retinal Bipolar Cellsgenetic structuresPresynaptic TerminalsOuter plexiform layerNerve Tissue ProteinsRetinal Horizontal CellsNeurotransmissionRibbon synapseImaging Three-DimensionalGlycoprotein complexImage Processing Computer-AssistedmedicineDystroglycanAnimalsActive zoneDystroglycansFluorescent Antibody Technique IndirectSynaptic ribbonRetinabiologyAnatomyCell CompartmentationCell biologyMicroscopy Electronmedicine.anatomical_structureMicroscopy Fluorescencebiology.proteinsense organsChickensPhotoreceptor Cells VertebrateInvestigative Opthalmology & Visual Science
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Subtercola boreus gen. nov., sp. nov. and Subtercola frigoramans sp. nov., two new psychrophilic actinobacteria isolated from boreal groundwater.

2000

Psychrophilic actinobacterial isolates from permanently cold groundwater in Finland were characterized using a polyphasic approach. Growth on agar plates was observed at temperatures down to -2 degrees C, with an optimum at 15-17 degrees C, but no growth was observed at 30 degrees C. The peptidoglycan type was B2y and the characteristic diamino acid was diaminobutyric acid. The cell wall sugars of strain K265T were rhamnose, ribose, xylose and mannose and those of strain K300T were glucose, rhamnose and xylose. The polar lipids included phosphatidylglycerol, diphosphatidylglycerol, one unknown phospholipid and two glycolipids. The main whole-cell fatty acids were 12-methyltetradecanoic acid…

RhamnoseMolecular Sequence DataFresh WaterDiamino acidBiologyMicrobiologyActinobacteriaMicrobiologychemistry.chemical_compoundRNA Ribosomal 16SBotanyEcology Evolution Behavior and SystematicsPhylogenyFatty AcidsTemperatureGenes rRNAGeneral MedicineSequence Analysis DNARibosomal RNAMicrobacteriaceaebiology.organism_classificationActinobacteriaCold TemperaturechemistryChemotaxonomyGenes BacterialPeptidoglycanClavibacter michiganensis
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Influence of retinol on human chondrocytes in agarose culture

1992

Vitamin A and its congeners, collectively called retinoids, are known to have teratogenic potential and have induced craniofacial and limb malformations in numerous animal species. More importantly, retinoids are recognized as teratogenic to fetuses of pregnant women who have taken such preparations for dermatologic disorders. Information gathered from the study of animal models suggests that retinoids interfere with cartilage differentiation. If chondrogenesis in limb development is disturbed it may contribute to limb reductions and malformations. In vitro studies using various animal systems have shown that cartilage matrix macromolecules are altered to resemble those secreted by mesenchy…

SepharoseCartilageMesenchymal stem cellType II collagenBiologyChondrogenesisAgricultural and Biological Sciences (miscellaneous)ChondrocyteCartilageTeratogensmedicine.anatomical_structureBiochemistryProteoglycanCell culturemedicinebiology.proteinHumansProteoglycansCollagenAnatomyVitamin ACells CulturedType I collagenThe Anatomical Record
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AtPGAP1 functions as a GPI inositol-deacylase required for efficient transport of GPI-anchored proteins

2021

Abstract Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) play an important role in a variety of plant biological processes including growth, stress response, morphogenesis, signaling, and cell wall biosynthesis. The GPI anchor contains a lipid-linked glycan backbone that is synthesized in the endoplasmic reticulum (ER) where it is subsequently transferred to the C-terminus of proteins containing a GPI signal peptide by a GPI transamidase. Once the GPI anchor is attached to the protein, the glycan and lipid moieties are remodeled. In mammals and yeast, this remodeling is required for GPI-APs to be included in Coat Protein II-coated vesicles for their ER export and subsequent t…

Signal peptideGlycanGenotypePhysiologyGlycosylphosphatidylinositolsPlant ScienceGenes Plantchemistry.chemical_compoundGene Expression Regulation PlantArabidopsisGeneticsArabidopsis thalianaInositolbiologyChemistryArabidopsis ProteinsEndoplasmic reticulumGenetic VariationMembrane Proteinsbiology.organism_classificationYeastPhosphoric Monoester HydrolasesCell biologyFocus Issue on Transport and Signalingcarbohydrates (lipids)Protein Transportbiology.proteinlipids (amino acids peptides and proteins)Function (biology)
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Function of AtPGAP1 in GPI anchor lipid remodeling and transport to the cell surface of GPI-anchored proteins

2021

ABSTRACTGPI-anchored proteins (GPI-APs) play an important role in a variety of plant biological processes including growth, stress response, morphogenesis, signalling and cell wall biosynthesis. The GPI-anchor contains a lipid-linked glycan backbone that is synthesized in the endoplasmic reticulum (ER) where it is subsequently transferred to the C-terminus of proteins containing a GPI signal peptide by a GPI transamidase. Once the GPI anchor is attached to the protein, the glycan and lipid moieties are remodelled. In mammals and yeast, this remodelling is required for GPI-APs to be included in Coat Protein II (COPII) coated vesicles for their ER export and subsequent transport to the cell s…

Signal peptideGlycanbiologyChemistryEndoplasmic reticulumCellCoated vesiclebiology.organism_classificationCell biologycarbohydrates (lipids)chemistry.chemical_compoundmedicine.anatomical_structureArabidopsismedicinebiology.proteinlipids (amino acids peptides and proteins)InositolCOPII
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