Search results for "Fibronectin"

showing 10 items of 165 documents

Contribution of sinusoidal endothelial liver cells to liver fibrosis: expression of transforming growth factor-beta 1 receptors and modulation of pla…

1993

Transforming growth factor-beta 1 is an important cytokine in the pathophysiology of liver fibrosis, stimulating the production of extracellular matrix. Whether this cytokine can also control the degradation of matrix proteins in liver cells has not been investigated. Because plasmin is an important protease for the degradation of matrix glycoproteins, we investigated whether sinusoidal endothelial liver cells could contribute to fibrosing liver disease through the modulation of plasmin-generating enzymes in response to transforming growth factor-beta 1. Sinusoidal endothelial cells from guinea pig liver were investigated in pure monolayer culture. Using 125I-labelled transforming growth fa…

PlasminGuinea PigsBiologyLiver Cirrhosis Experimental03 medical and health sciencesPlasminogen Activators0302 clinical medicineCell surface receptorTransforming Growth Factor betaPlasminogen Activator Inhibitor 1medicineAnimalsFibrinolysinCells Cultured030304 developmental biology0303 health sciencesHepatology3. Good healthCell biologyFibronectinEndothelial stem cellBiochemistryLiverTransforming growth factor beta 3Cell culturebiology.protein030211 gastroenterology & hepatologyFemaleEndothelium VascularPlasminogen activatorReceptors Transforming Growth Factor betamedicine.drugTransforming growth factorHepatology (Baltimore, Md.)
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Specific processing of tenascin-C by the metalloprotease meprinβ neutralizes its inhibition of cell spreading

2009

The metalloprotease meprin has been implicated in tissue remodelling due to its capability to degrade extracellular matrix components. Here, we investigated the susceptibility of tenascin-C to cleavage by meprinbeta and the functional properties of its proteolytic fragments. A set of monoclonal antibodies against chicken and human tenascin-C allowed the mapping of proteolytic fragments generated by meprinbeta. In chicken tenascin-C, meprinbeta processed all three major splicing variants by removal of 10kDa N-terminal and 38kDa C-terminal peptides, leaving a large central part of subunits intact. A similar cleavage pattern was found for large human tenascin-C variant where two N-terminal pep…

Proteasesanimal structuresColonRecombinant Fusion ProteinsProtein subunitMolecular Sequence DataTenascinCleavage (embryo)Cell LineCrohn DiseaseCell AdhesionAnimalsHumansProtein IsoformsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyPeptide sequencebiologyAlternative splicingTenascin CMetalloendopeptidasesTenascinMolecular biologyPeptide FragmentsExtracellular MatrixFibronectinsFibronectinAlternative SplicingProtein Subunitsembryonic structuresbiology.proteinProtein MultimerizationChickensMatrix Biology
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Thin-layer affinity chromatography in analysis of protein-ligand affinity.

1996

Protein DenaturationHot TemperatureThin layerIon chromatographyBiophysicsPlasma protein bindingLigandsBiochemistryChromatography AffinityAffinity chromatographyHumansMolecular BiologyFluorescent DyesChromatographybiologyChemistryProteinsCell BiologyAvidinFibronectinsFibronectinsbiology.proteinChromatography Thin LayerAzo CompoundsProtein ligandAvidinProtein BindingAnalytical biochemistry
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The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains.

2007

Abstract Procollagen C-proteinase (PCP) removes the C-terminal pro-peptides of procollagens and also processes other matrix proteins. The major splice form of the PCP is termed BMP1 (bone morphogenetic protein 1). Active BMP1 is composed of an astacin-like protease domain, three CUB (complement, sea urchin Uegf, BMP1) domains and one EGF-like domain. Here we compare the recombinant human full-length BMP1 with its isolated proteolytic domain to further unravel the functional influence of the CUB and EGF domains. We show that the protease domain alone cleaves truncated procollagen VII within the short telopeptide region into fragments of similar size as the full-length enzyme does. However, u…

Protein FoldingCollagen Type VIIDNA Complementarymedicine.medical_treatmentClinical BiochemistryAmino Acid MotifsGene ExpressionGlutamic AcidBiochemistryBone morphogenetic protein 1Mass SpectrometryBone Morphogenetic Protein 1Cell LineSubstrate SpecificityProtein structuremedicineEscherichia coliAnimalsHumansCysteineDisulfidesMolecular BiologyInclusion BodiesMetalloproteinaseProteasebiologyChemistryMetalloendopeptidasesRecombinant ProteinsProtein Structure TertiaryFibronectinProcollagen peptidaseDrosophila melanogasterBiochemistryBone Morphogenetic ProteinsMutationbiology.proteinProtein foldingAstacinBiological chemistry
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Purification of a biologically active recombinant glyceraldehyde 3-phosphate dehydrogenase fromCandida albicans

1999

We report here the purification of a functionally active recombinant glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from Candida albicans. The GAPDH protein encoded by the TDH1 gene was obtained as a glutathione S-transferase fusion protein by expression in the vector pGEX-4T-3, and purified by affinity chromatography and thrombin digestion. The purified protein displays GAPDH enzymatic activity (42 micromol NADH min(-1) mg(-1)) as well as the laminin and fibronectin binding activities previously described. In addition, the recombinant GAPDH is covalently modified by NAD linkage; this modification is stimulated by nitric oxide and probably involves a sulfhydryl group (cysteine) residue si…

Recombinant Fusion ProteinsDehydrogenaseBiologyMicrobiologyChromatography Affinitylaw.inventionchemistry.chemical_compoundstomatognathic systemAffinity chromatographylawGlyceraldehydeCandida albicansEscherichia coliGeneticsCloning MolecularMolecular BiologyGlyceraldehyde 3-phosphate dehydrogenaseGlutathione TransferaseThrombinGlyceraldehyde-3-Phosphate DehydrogenasesMolecular biologyRecombinant ProteinsKineticschemistryBiochemistryFibronectin bindingbiology.proteinRecombinant DNAGlyceraldehyde 3-phosphateCysteineFEMS Microbiology Letters
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Overexpression of apolipoprotein J in human fibroblasts protects against cytotoxicity and premature senescence induced by ethanol and tert-butylhydro…

2008

Human diploid fibroblasts (HDFs) exposed to subcytotoxic stresses under H2O2, tert-butylhydroperoxide (t-BHP), and ethanol (EtOH) undergo stress-induced premature senescence (SIPS) characterized by many biomarkers of HDFs replicative senescence. Among these biomarkers are a growth arrest, an increase in the senescence-associated β-galactosidase activity, a senescent morphology, an overexpression of p21waf-1 and the subsequent inability to phosphorylate pRb, the presence of the common 4977-bp mitochondrial deletion, and an increase in the steady-state level of several senescence-associated genes such as apolipoprotein J (apo J). Apo J has been described as a survival gene against cytotoxic s…

SenescenceCell SurvivalGene ExpressionSimian virus 40Biologymedicine.disease_causeTritiumBiochemistrytert-ButylhydroperoxideGene expressionmedicineHumansOsteonectinRNA MessengerCytotoxicityCells CulturedCellular SenescenceCell Line TransformedGlycoproteinsClusterinEthanolCentral Nervous System DepressantsCell BiologyTransfectionOriginal ArticlesFibroblastsbeta-GalactosidaseMolecular biologyRecombinant ProteinsFibronectinsOxidative StressClusterinbiology.proteinPhosphorylationMitogensCell agingOxidative stressMolecular ChaperonesThymidineCell Stress and Chaperones
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Type-II Transmembrane Prolyl Dipeptidases and Matrix Metalloproteinases in Membrane Vesicles of Active Endothelial Cells

2006

Endothelia cells in sparse culture are migratory and increase the production of gelatinases of serine- and metallo-classes in membrane vesicles. Collectively, proteases associated with membrane vesicles degrade extracellular matrix components including type-I and type-IV collagens, laminin and fibronectin. Inhibitor studies suggest the existence of small gelatinases that were derived from these serine- and metallo-proteases. Thus, further studies are warranted to demonstrate the cooperative action of metallo- and serine proteases on cell surfaces and in extracellular vesicles during endothelial cell migration in 3D collagenous matrices, and potential proteolytic activation mechanism for the…

SerineExtracellular matrixFibronectinGelatinasesProteasesbiologyChemistryLamininbiology.proteinMatrix metalloproteinaseTransmembrane proteinCell biology
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Differing expression of metalloprotease and of adhesion molecules in signet-ring cell and intestinal colorectal carcinoma.

2009

Abstract. Background: Pure signet-ring cell colorectal carcinoma (SRCC) is an infrequent and highly malignant histological variant of colorectal cancer (CRC), while it is present as a histological component in colorectal carcinomas more frequently. Materials and Methods: The aim of this work was to widen the knowledge of the biological factors involved in the pathogenesis and aggressiveness of SRCC by the identification and evaluation of possible molecular abnormalities. By means of immunohistochemistry the expression of the proteolytic degradation enzyme matrix metalloprotease (MMP)-1, that is a collagenase specifically degrading collagens I, II, III and of the adhesion proteins Ecadherin,…

Settore MED/08 - Anatomia PatologicaColorectal cancer cadherin catenin fibronectin metalloprotease-1 signet-ring cell.
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The hemagglutinin of Staphylococcus saprophyticus is a major adhesin for uroepithelial cells.

1996

The 160-kDa hemagglutinin of Staphylococcus saprophyticus also serves as a fibronectin-binding protein, and the two activities may be present on different parts of the molecule. Bacteria expressing the 160-kDa hemagglutinin bound in large numbers to histological sections of human ureters, whereas nonhemagglutinating bacteria did not bind. Binding was decreased by an antiserum to the 160-kDa protein and by a preparation of sheep erythrocyte membranes. Fibronectin had no effect. We therefore conclude that binding of S. saprophyticus to uroepithelial cells is mediated by the hemagglutinating activity of the 160-kDa surface protein.

StaphylococcusImmunologyBiologymedicine.disease_causeMicrobiologyBacterial AdhesionEpitheliumMicrobiologymedicineAnimalsHumansAntiserumchemistry.chemical_classificationStaphylococcus saprophyticusSheepBinding proteinErythrocyte MembraneHemagglutininbiology.organism_classificationFibronectinsBacterial adhesinInfectious DiseasesHemagglutininschemistryParasitologyUreterGlycoproteinStaphylococcusBacteriaResearch ArticleInfection and immunity
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Adsorption and Conformation Behavior of Biotinylated Fibronectin on Streptavidin-Modified TiOX Surfaces Studied by SPR and AFM

2011

It is well-known that protein-modified implant surfaces such as TiO(2) show a higher bioconductivity. Fibronectin is a glycoprotein from the extracellular matrix (ECM) with a major role in cell adhesion. It can be applied on titanium oxide surfaces to accelerate implant integration. Not only the surface concentration but also the presentation of the protein plays an important role for the cellular response. We were able to show that TiO(X) surfaces modified with biotinylated fibronectin adsorbed on a streptavidin-silane self-assembly multilayer system are more effective regarding osteoblast adhesion than surfaces modified with nonspecifically bound fibronectin. The adsorption and conformati…

StreptavidinConformational changeProtein ConformationSurface PropertiesBiotinNanotechnologyMicroscopy Atomic Forcechemistry.chemical_compoundAdsorptionMonolayerElectrochemistryGeneral Materials ScienceSurface plasmon resonanceSpectroscopyTitaniumbiologyChemistrytechnology industry and agricultureSurfaces and InterfacesAdhesionSurface Plasmon ResonanceCondensed Matter PhysicsFibronectinsFibronectinBiotinylationbiology.proteinBiophysicsAdsorptionStreptavidinLangmuir
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