Search results for "proteoglycan"

showing 10 items of 94 documents

Decorin transfection induces proteomic and phenotypic modulation in breast cancer cells 8701-BC

2008

Decorin is a prototype member of the small leucine-rich proteoglycan family widely distributed in the extracellular matrices of many connective tissues, where it has been shown to play multiple important roles in the matrix assembly process, as well as in some cellular activities. A major interest for decorin function concerns its role in tumorigenesis, as growth-inhibitor of different neoplastic cells, and potential antimetastatic agent. The aim of our research was to investigate wide-ranged effects of transgenic decorin on breast cancer cells. To this purpose we utilized the well-characterized 8701-BC cell line, isolated from a ductal infiltrating carcinoma of the breast, and two derived …

DecorinTransgeneBlotting WesternOligonucleotidesBreast NeoplasmsBiologymedicine.disease_causeProteomicsBiochemistryproteomicsRheumatologyCell Line TumorSettore BIO/10 - BiochimicaCell AdhesionmedicineHumansElectrophoresis Gel Two-DimensionalOrthopedics and Sports MedicineSettore BIO/06 - Anatomia Comparata E CitologiaMolecular BiologyCell ProliferationdecorinExtracellular Matrix ProteinsCell growthGene Expression ProfilingCell BiologyTransfectionbrest cancer cellGene Expression Regulation Neoplasticcarbohydrates (lipids)Settore BIO/18 - GeneticaProteoglycanCell cultureMicroscopy Electron Scanningbiology.proteinCancer researchdecorin; brest cancer cells; proteomicsFemaleProteoglycansCarcinogenesis
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Possible control mechanism of cell motility in the gorgonian Eunicella cavolinii

1985

In a previous study it was demonstrated that a lectin controls cell-cell interaction in the gorgonian Eunicella cavolinii (Koch) as a negative modulator. Now we describe the procedure to purify this lectin to homogeneity; its molecular weight is 23 400. The homologous proteoglycans were identified as positive modulators of cell-cell (and/or cell substrate) interaction. The purified single proteoglycan aggregates were 1200±700 nm long and the distance between the attachment points of the proteoglycan subunits was about 45 nm. The glycosaminoglycan residues of the gorgonian proteoglycans were identified as hyaluronic acid (35.5%), heparan sulfate (47.9%) and dermatan sulfate (14.1%). Binding …

EcologybiologyLectinMotilityHeparan sulfateAquatic ScienceDermatan sulfatecarbohydrates (lipids)Glycosaminoglycanchemistry.chemical_compoundProteoglycanchemistryBiochemistryCell–cell interactionHyaluronic acidbiology.proteinEcology Evolution Behavior and SystematicsMarine Biology
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Disruption of apical-basal polarity of human embryonic stem cells enhances hematoendothelial differentiation

2007

Abstract During murine development, the formation of tight junctions and acquisition of polarity are associated with allocation of the blastomeres on the outer surface of the embryo to the trophoblast lineage, whereas the absence of polarization directs cells to the inner cell mass. Here, we report the results of ultrastructural analyses that suggest a similar link between polarization and cell fate in human embryos. In contrast, the five human embryonic stem cell (hESC) lines displayed apical-basal, epithelial-type polarity with electron-dense tight junctions, apical microvilli, and asymmetric distribution of organelles. Consistent with these findings, molecules that are components of tigh…

Embryoid bodyBiologyCell fate determinationMiceCell polarityAnimalsHumansInner cell massCells CulturedEmbryonic Stem Cellsreproductive and urinary physiologyembryoid body formationTight junctionMesenchymal stem cellapical-basal polarityCell PolarityCell DifferentiationEpithelial CellsCell Biologyinner cell masshuman embryonic stem cellsEmbryonic stem cellHematopoiesisCell biologyDrug CombinationsIntercellular JunctionsPhenotypeembryonic structuresMolecular Medicinehernatoendothelial differentiationProteoglycansCollagenEndothelium VascularLamininStem cellDevelopmental Biology
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Expression patterns of matrix genes during human skeletal development.

1994

Extracellular Matrix ProteinsHistologyBone DevelopmentChemistryClinical BiochemistryCell DifferentiationCell BiologyComputational biologyExpression (computer science)Cartilage Oligomeric Matrix ProteinAlkaline PhosphataseMatrix (mathematics)Gene Expression RegulationProtein BiosynthesisBiglycanHumansMatrilin ProteinsLectins C-TypeOsteonectinProteoglycansAggrecansCollagenDecorinGeneGlycoproteinsProgress in histochemistry and cytochemistry
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A BMP7 Variant Inhibits Tumor Angiogenesis In Vitro and In Vivo through Direct Modulation of Endothelial Cell Biology

2015

Bone morphogenetic proteins (BMPs), members of the TGF-β superfamily, have numerous biological activities including control of growth, differentiation, and vascular development. Using an in vitro co-culture endothelial cord formation assay, we investigated the role of a BMP7 variant (BMP7v) in VEGF, bFGF, and tumor-driven angiogenesis. BMP7v treatment led to disruption of neo-endothelial cord formation and regression of existing VEGF and bFGF cords in vitro. Using a series of tumor cell models capable of driving angiogenesis in vitro, BMP7v treatment completely blocked cord formation. Pre-treatment of endothelial cells with BMP7v significantly reduced their cord forming ability, indicating …

Genetics and Molecular Biology (all)MaleVascular Endothelial Growth Factor AFibroblast Growth FactorAngiogenesisBone Morphogenetic Protein 7Nudelcsh:MedicineSmad ProteinsFibroblast growth factorBiochemistryNeovascularizationMiceCell Movementlcsh:ScienceBMP7 Angiogenesis TumorTumorMultidisciplinaryCell DeathNeovascularization PathologicMedicine (all)Cell migrationCell biologyEndothelial stem cellSettore MED/26 - NEUROLOGIAVascular endothelial growth factor ADrug CombinationsAdipose TissueAdipose Tissue; Animals; Bone Morphogenetic Protein 7; Cell Death; Cell Line Tumor; Cell Movement; Cell Proliferation; Collagen; Drug Combinations; Endothelial Cells; Fibroblast Growth Factor 2; Glioblastoma; Human Umbilical Vein Endothelial Cells; Humans; Laminin; Male; Mice Nude; Neoplastic Stem Cells; Neovascularization Pathologic; Neovascularization Physiologic; Proteoglycans; Receptor Fibroblast Growth Factor Type 1; Signal Transduction; Smad Proteins; Vascular Endothelial Growth Factor A; Vascular Endothelial Growth Factor Receptor-2; Xenograft Model Antitumor Assays; Biochemistry Genetics and Molecular Biology (all); Agricultural and Biological Sciences (all)Neoplastic Stem CellsFibroblast Growth Factor 2ProteoglycansCollagenmedicine.symptomReceptorType 1Research ArticleSignal TransductionMice NudeNeovascularization PhysiologicBMP7BiologyCell LineSettore MED/04 - PATOLOGIA GENERALECell Line TumormedicineHuman Umbilical Vein Endothelial CellsAnimalsHumansAgricultural and Biological Sciences (all); Biochemistry Genetics and Molecular Biology (all); Medicine (all)Receptor Fibroblast Growth Factor Type 1PhysiologicNeovascularizationCell ProliferationPathologicMatrigelBiochemistry Genetics and Molecular Biology (all)lcsh:REndothelial CellsKinase insert domain receptorVascular Endothelial Growth Factor Receptor-2Xenograft Model Antitumor AssaysAgricultural and Biological Sciences (all)lcsh:QAngiogenesisLamininGlioblastomaPLoS ONE
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Expression profiling of human fetal growth plate cartilage by EST sequencing.

2005

The differentiation of mesenchymal stem cells into hypertrophic chondrocytes is an integral and multistep process important in pattern formation, endochondral ossification, and postnatal growth of the skeleton. In recent years, novel genes involved in these processes have been identified, but still only little is known about the large-scale gene expression profile during skeletal development. We initiated an expressed sequence tag (EST) project aiming at the identification of genes and pathways involved in this complex process. Candidate genes are expected to be of value for diagnosis and treatment of monogenic and multigenic heritable disorders of the skeleton. Here, we describe the sequen…

GeneticsExpressed Sequence TagsCandidate geneExpressed sequence tagExtracellular Matrix ProteinscDNA libraryIn silicoGene Expression ProfilingGene Expression Regulation DevelopmentalBiologyGene expression profilingFetusGene expressionHumansProteoglycansGrowth PlateMolecular BiologyEndochondral ossificationGeneMatrix biology : journal of the International Society for Matrix Biology
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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
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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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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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Proteoglycan synthesis by cultured human chondrocytes.

1994

Iliac crest biopsies are important in the detection of human skeletal dysplasias. Therefore, culture of these cells may serve as a valuable method for studying proteoglycan metabolism in chondrocytes of individuals with skeletal abnormalities. Morphological and biochemical studies were performed on human iliac crest chondrocytes grown in monolayer and in agarose gels. Two proteoglycan populations of different hydrodynamic size and glycosaminoglycan composition were synthesized by cells grown in monolayer. Chondrocytes cultured in an agarose gel for 2 weeks synthesized proteoglycans identical to those of the native tissue with respect to hydrodynamic size and glycosaminoglycan chain length. …

HistologyAscorbic AcidChondrocyteGlycosaminoglycanIliumchemistry.chemical_compoundmedicineHumansInstrumentationCells CulturedGlycosaminoglycansbiologyChemistryCartilageSepharoseChondroitin SulfatesInfant NewbornCell DifferentiationAscorbic acidCell biologycarbohydrates (lipids)Medical Laboratory Technologymedicine.anatomical_structureCartilageBiochemistryProteoglycanChondroitin Sulfate ProteoglycansCell culturebiology.proteinUltrastructureChromatography GelAgaroseAnatomyMicroscopy research and technique
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