Search results for "Heparitin Sulfate"

showing 10 items of 12 documents

Observational Prospective Natural History of Patients with Sanfilippo Syndrome Type B

2017

To evaluate the natural course of disease progression in patients with Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB), identify potential end points for future therapy trials, and characterize biomarkers related to the disease.A prospective, multicenter study was conducted. Baseline, 6-month, and 12-month assessments included neurodevelopmental status (Bayley Scales of Infant Development, Third edition), adaptive status (Vineland Adaptive Behavior Scales, Second Edition), volumetric brain magnetic resonance imaging, cerebrospinal fluid heparan sulfate, and urine glycosaminoglycan (GAG) measurements.Nineteen patients aged 1.6-31.7 years were enrolled. Over 12 months, cognition,…

AdultMale0301 basic medicinePediatricsmedicine.medical_specialtyAdolescentDiseaseBayley Scales of Infant DevelopmentMucopolysaccharidosis IIIYoung Adult03 medical and health sciences0302 clinical medicineMucopolysaccharidosis IIImedicineHumansLongitudinal StudiesProspective StudiesYoung adultChildProspective cohort studyCerebrospinal FluidGlycosaminoglycansSanfilippo syndromemedicine.diagnostic_testbusiness.industryBrainInfantMagnetic resonance imagingmedicine.diseaseMagnetic Resonance ImagingVineland Adaptive Behavior Scale030104 developmental biologyNeurodevelopmental DisordersChild PreschoolPediatrics Perinatology and Child HealthDisease ProgressionFemaleHeparitin SulfatebusinessBiomarkers030217 neurology & neurosurgeryThe Journal of Pediatrics
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Agonist-induced formation of FGFR1 homodimers and signaling differ among members of the FGF family

2011

Fibroblast growth factor receptor 1 (FGFR1) is known to be activated by homodimerization in the presence of both the FGF agonist ligand and heparan sulfate glycosaminoglycan. FGFR1 homodimers in turn trigger a variety of downstream signaling cascades via autophosphorylation of tyrosine residues in the cytoplasmic domain of FGFR1. By means of Bioluminescence Energy Resonance Transfer (BRET) as a sign of FGFR1 homodimerization, we evaluated in HEK293T cells the effects of all known FGF agonist ligands on homodimer formation. A significant correlation between BRET(2) signaling and ERK1/2 phosphorylation was observed, leading to a further characterization of the binding and signaling properties…

AgonistMAPK/ERK pathwaymedicine.drug_classBiophysicsSettore BIO/11 - Biologia MolecolareBiologyLigandsFibroblast growth factorSettore BIO/09 - FisiologiaBiochemistrychemistry.chemical_compoundFluorescence Resonance Energy TransfermedicineHumansReceptor Fibroblast Growth Factor Type 1Molecular BiologyMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Fibroblast growth factor receptor 1HEK 293 cellsAutophosphorylationCell BiologyHeparan sulfateFibroblast growth factors FGFR1 Homodimerization BRET MAPKCell biologyFibroblast Growth Factorsstomatognathic diseasesHEK293 CellschemistrySettore BIO/14 - FarmacologiaPhosphorylationHeparitin SulfateProtein MultimerizationBiochemical and Biophysical Research Communications
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Perlecan Maintains the Integrity of Cartilage and Some Basement Membranes

1999

Perlecan is a heparan sulfate proteoglycan that is expressed in all basement membranes (BMs), in cartilage, and several other mesenchymal tissues during development. Perlecan binds growth factors and interacts with various extracellular matrix proteins and cell adhesion molecules. Homozygous mice with a null mutation in the perlecan gene exhibit normal formation of BMs. However, BMs deteriorate in regions with increased mechanical stress such as the contracting myocardium and the expanding brain vesicles showing that perlecan is crucial for maintaining BM integrity. As a consequence, small clefts are formed in the cardiac muscle leading to blood leakage into the pericardial cavity and an ar…

Heart Defects Congenitalcardiac muscleMesenchymeSchwartz–Jampel syndromeRestriction MappingPerlecanBasement MembraneExtracellular matrixMiceMice CongenicchondrodysplasiaCalcification PhysiologicexencephalyLamininmedicineAnimalsNeural Tube DefectsCells CulturedBasement membranebiologyCartilageOssification HeterotopicHomozygoteCell Biologymedicine.diseaseMice Mutant StrainsBasement membrane assemblyCell biologyperlecanMutagenesis Insertionalmedicine.anatomical_structureCartilageBiochemistryGene Targetingbiology.proteinOriginal ArticleGenes LethalProteoglycansCollagenHeparitin SulfateExostoses Multiple HereditaryHeparan Sulfate ProteoglycansThe Journal of Cell Biology
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Inhibition of Transfer to Secondary Receptors by Heparan Sulfate-Binding Drug or Antibody Induces Noninfectious Uptake of Human Papillomavirus

2007

ABSTRACT Infection with various human papillomaviruses (HPVs) induces cervical cancers. Cell surface heparan sulfates (HS) have been shown to serve as primary attachment receptors, and molecules with structural similarity to cell surface HS, like heparin, function as competitive inhibitors of HPV infection. Here we demonstrate that the N , N ′-bisheteryl derivative of dispirotripiperazine, DSTP27, efficiently blocks papillomavirus infection by binding to HS moieties, with 50% inhibitory doses of up to 0.4 μg/ml. In contrast to short-term inhibitory effects of heparin, pretreatment of cells with DSTP27 significantly reduced HPV infection for more than 30 h. Using DSTP27 and heparinase, we fu…

ImmunologyEndocytosisBinding CompetitiveMicrobiologyAntibodiesCell LineExtracellular matrixLamininVirologyHumansReceptorPapillomaviridaeOxadiazolesHeparinasebiologyMolecular biologyEndocytosisVirus-Cell InteractionsPyrimidinesEndocytic vesicleCell cultureInsect Sciencebiology.proteinReceptors VirusHeparan sulfate bindingHeparitin SulfateHeparan Sulfate ProteoglycansJournal of Virology
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Human papillomavirus infection requires cell surface heparan sulfate.

2001

ABSTRACT Using pseudoinfection of cell lines, we demonstrate that cell surface heparan sulfate is required for infection by human papillomavirus type 16 (HPV-16) and HPV-33 pseudovirions. Pseudoinfection was inhibited by heparin but not dermatan or chondroitin sulfate, reduced by reducing the level of surface sulfation, and abolished by heparinase treatment. Carboxy-terminally deleted HPV-33 virus-like particles still bound efficiently to heparin. The kinetics of postattachment neutralization by antiserum or heparin indicated that pseudovirions were shifted on the cell surface from a heparin-sensitive into a heparin-resistant mode of binding, possibly involving a secondary receptor. Alpha-6…

ImmunologyIntegrinIntegrin alpha6Microbiologychemistry.chemical_compoundSulfationAntigens CDVirologymedicineAnimalsHumansChondroitin sulfateReceptorNeural Cell Adhesion MoleculesPapillomaviridaeAntiserumHeparinaseMembrane GlycoproteinsbiologyHeparinVirionHeparan sulfateHeparinMolecular biologyVirus-Cell InteractionschemistryInsect ScienceCOS Cellsbiology.proteinHeparitin SulfateLeukocyte L1 Antigen Complexmedicine.drugJournal of virology
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Perlecan-Induced Suppression of Smooth Muscle Cell Proliferation Is Mediated Through Increased Activity of the Tumor Suppressor PTEN

2004

We were interested in the elucidation of the interaction between the heparan sulfate proteoglycan, perlecan, and PTEN in the regulation of vascular smooth muscle cell (SMC) growth. We verified serum-stimulated DNA synthesis, and Akt and FAK phosphorylation were significantly reduced in SMCs overexpressing wild-type PTEN. Our previous studies showed perlecan is a potent inhibitor of serum-stimulated SMC growth. We report in the present study, compared with SMCs plated on fibronectin, serum-stimulated SMCs plated on perlecan exhibited increased PTEN activity, decreased FAK and Akt activities, and high levels of p27, consistent with SMC growth arrest. Adenoviral-mediated overexpression of cons…

MaleVascular smooth musclePhysiology:CIENCIAS MÉDICAS ::Farmacodinámica [UNESCO]Aorta ThoracicBasement MembraneCulture Media Serum-FreeMuscle Smooth VascularRats Sprague-DawleyMicePhosphorylationCells CulturedGlycosaminoglycansbiologyProtein-Tyrosine KinasesCell cycle:CIENCIAS MÉDICAS [UNESCO]musculoskeletal systemUNESCO::CIENCIAS MÉDICAS ::FarmacodinámicaUNESCO::CIENCIAS MÉDICAScardiovascular systemPhosphorylationSmooth muscle cell proliferationCardiology and Cardiovascular MedicineCell DivisionDNA ReplicationBasement membraneRecombinant Fusion ProteinsPerlecanProtein Serine-Threonine KinasesVascular injurySmooth muscle cell proliferation ; Restenosis ; Vascular injury ; Vascular development ; Basement membraneCatheterizationProto-Oncogene ProteinsAnimalsPTENProtein kinase BRestenosisCell growthVascular developmentOligonucleotides AntisenseFibronectinsRatsFibronectinFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine Kinasesbiology.proteinCancer researchHeparitin SulfateCarotid Artery InjuriesProtein Processing Post-TranslationalProto-Oncogene Proteins c-aktHeparan Sulfate ProteoglycansCirculation Research
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Dynamic In Vivo Biocompatibility of Angiogenic Peptide Amphiphile Nanofibers

2009

Biomaterials that promote angiogenesis have great potential in regenerative medicine for rapid revascularization of damaged tissue, survival of transplanted cells, and healing of chronic wounds. Supramolecular nanofibers formed by self-assembly of a heparin-binding peptide amphiphile and heparan sulfate-like glycosaminoglycans were evaluated here using a dorsal skinfold chamber model to dynamically monitor the interaction between the nanofiber gel and the microcirculation, representing a novel application of this model. We paired this model with a conventional subcutaneous implantation model for static histological assessment of the interactions between the gel and host tissue. In the stati…

Materials scienceBiocompatibilityAngiogenesisBiophysicsConnective tissueBioengineeringBiocompatible Materials02 engineering and technology010402 general chemistry01 natural sciencesRegenerative medicineArticleMicrocirculationBiomaterialsMiceImplants ExperimentalFluorescence microscopemedicinePeptide amphiphileAnimalsAngiogenic ProteinsMicrocirculation021001 nanoscience & nanotechnology0104 chemical sciences3. Good healthmedicine.anatomical_structureMicroscopy FluorescenceMechanics of MaterialsNanofiberCeramics and CompositesFemaleHeparitin Sulfate0210 nano-technologyBiomedical engineering
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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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Surface-exposed Amino Acid Residues of HPV16 L1 Protein Mediating Interaction with Cell Surface Heparan Sulfate

2007

Efficient infection of cells by human papillomaviruses (HPVs) and pseudovirions requires primary interaction with cell surface proteoglycans with apparent preference for species carrying heparan sulfate (HS) side chains. To identify residues contributing to virus/cell interaction, we performed point mutational analysis of the HPV16 major capsid protein, L1, targeting surface-exposed amino acid residues. Replacement of lysine residues 278, 356, or 361 for alanine reduced cell binding and infectivity of pseudovirions. Various combinations of these amino acid exchanges further decreased cell attachment and infectivity with residual infectivity of less than 5% for the triple mutant, suggesting …

Surface PropertiesLysinePlasma protein bindingBiochemistryAntibodieschemistry.chemical_compoundCapsidChlorocebus aethiopsAnimalsHumansComputer SimulationMolecular Biologychemistry.chemical_classificationAlanineInfectivityHeparinLysineCell MembraneCapsomereOncogene Proteins ViralCell BiologyHeparan sulfateAmino acidchemistryBiochemistryCapsidMutagenesisCOS CellsCapsid ProteinsHeparitin SulfateProtein BindingJournal of Biological Chemistry
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Integrin-dependent and -independent functions of astrocytic fibronectin in retinal angiogenesis

2011

Fibronectin (FN) is a major component of the extracellular matrix and functions in cell adhesion, cell spreading and cell migration. In the retina, FN is transiently expressed and assembled on astrocytes (ACs), which guide sprouting tip cells and deposit a provisional matrix for sprouting angiogenesis. The precise function of FN in retinal angiogenesis is largely unknown. Using genetic tools, we show that astrocytes are the major source of cellular FN during angiogenesis in the mouse retina. Deletion of astrocytic FN reduces radial endothelial migration during vascular plexus formation in a gene dose-dependent manner. This effect correlates with reduced VEGF receptor 2 and PI3K/AKT signalli…

Vascular Endothelial Growth Factor AIntegrinsAngiogenesisIntegrinNeovascularization PhysiologicMice TransgenicExtracellular matrixMicePhosphatidylinositol 3-KinasesCell MovementAnimalsProtein Interaction Domains and MotifsMolecular BiologyResearch ArticlesMice KnockoutSprouting angiogenesisbiologyRetinal VesselsCell migrationKinase insert domain receptorVascular Endothelial Growth Factor Receptor-2Extracellular MatrixFibronectinsCell biologyMice Inbred C57BLFibronectinVascular endothelial growth factor AAstrocytesbiology.proteinHeparitin SulfateOligopeptidesProto-Oncogene Proteins c-aktIntegrin alpha5beta1Signal TransductionDevelopmental BiologyDevelopment
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