Search results for "Nectin"

showing 10 items of 355 documents

Expression of cell adhesion molecules in inflammatory myopathies.

1995

We examined the expression of cell adhesion molecules in 25 cases of inflammatory myopathies. Inflammatory myopathies showed upregulation of adhesion molecules. ICAM-1 was strongly expressed on endothelial cells as well as on fibroblasts and infiltrating leukocytes while the expression of VCAM-1, similar in its distribution, was much weaker. A few muscle fibers in polymyositis revealed sarcolemmal labeling for ICAM-1. ELAM-1 showed only weak expression on vessels. The inflammatory cellular infiltrates contained varying amounts of cells bearing the VCAM-1 ligand VLA-4 and the ELAM-1 ligand SLeX as well as large amounts of cells expressing LFA-1 alpha and beta, ligands of ICAM-1.

ImmunologyIntercellular Adhesion Molecule-1Lewis X AntigenVascular Cell Adhesion Molecule-1InflammationNectinReceptors Very Late AntigenE-selectinmedicineImmunology and AllergyHumansCell adhesionbiologyMyositisCell adhesion moleculeChemistrySoluble cell adhesion moleculesIntercellular Adhesion Molecule-1Lymphocyte Function-Associated Antigen-1Cell biologyNeurologycardiovascular systembiology.proteinNeural cell adhesion moleculeNeurology (clinical)medicine.symptomE-SelectinCell Adhesion MoleculesJournal of neuroimmunology
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Binding of human fibronectin to Aspergillus fumigatus conidia.

1996

Aspergillus fumigatus conidia exhibited the ability to bind purified human fibronectin, whereas mycelial forms did not bind the ligand, as detected by an indirect immunofluorescence assay with an antifibronectin polyclonal antibody after incubation of the cells with fibronectin. Flow cytometry confirmed that binding of the ligand to conidia was dose dependent and saturable. Pretreatment of the cells with trypsin markedly reduced binding, which suggested a protein nature for the binding sites present at the surface of conidia. Intact conidia were also able to adhere to fibronectin or antifibronectin antibodies, a significant reduction (from 88 to 92%) in the binding of conidia was noticed, t…

ImmunologyMicrobiologyAspergillus fumigatusFungal ProteinsMicemedicineAnimalsAspergillosisHumansTrypsinBinding siteGel electrophoresisFungal proteinbiologyAspergillus fumigatusLigand (biochemistry)biology.organism_classificationTrypsinFlow CytometryFibronectinsFibronectinInfectious DiseasesBiochemistryPolyclonal antibodiesbiology.proteinParasitologymedicine.drugResearch ArticleInfection and immunity
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Binding of extracellular matrix proteins to Aspergillus fumigatus conidia

1996

As detected by confocal immunofluorescence microscopy, binding of fibronectin and laminin appeared to be associated with the protrusions present on the outer cell wall layer of resting Aspergillus fumigatus conidia. Flow cytometry confirmed that binding of laminin to conidia was dose dependent and saturable. Laminin binding was virtually eliminated in trypsin-treated organisms, thus suggesting the protein nature of the binding site. Conidia were also able to specifically adhere to laminin immobilized on microtiter plates. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting (immunoblotting) with laminin and antilaminin antibody of whole conidial homogenates allowed…

ImmunologyMicrobiologyAspergillus fumigatusLamininCell AdhesionBinding siteCell adhesionLaminin bindingGel electrophoresischemistry.chemical_classificationExtracellular Matrix ProteinsMicroscopy ConfocalbiologyAspergillus fumigatusFlow Cytometrybiology.organism_classificationMolecular biologyFibronectinInfectious DiseasesBiochemistrychemistrybiology.proteinParasitologyGlycoproteinProtein BindingResearch ArticleInfection and Immunity
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Estrogens control inflammation in experimental colitis.

2014

There is now a wealth of experimental evidence indicating that the deficit in endogenous estrogen facilitates the onset of inflammation that can be antagonized by estrogen replacement therapy. This work investigated the role of estrogen in the control of intestinal inflammation in a panel of colitis models, focusing on the morphological changes, the activity of mast cells, the expression of cytokines (IL-1beta, IL-6, and TNF-alpha), fibronectin and reactive oxygen species. Two hundred adult male rats were divided into 4 groups: colitis was induced in Group I and Group II but only the latter was treated with estrogen; Group III received estrogen only, and Group IV saline. Colitis was induced…

InflammationMaleRats Sprague-DawleyDisease Models AnimalColonestrogens colitis inflammation.AnimalsCytokinesEstrogensMast CellsColitisFibronectinsRats
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Endothelial cell-matrix interactions.

2002

Dynamic interactions between endothelial cells and components of their surrounding extracellular matrix are necessary for the invasion, migration, and survival of endothelial cells during angiogenesis. These interactions are mediated by matrix receptors that initiate intracellular signaling cascades in response to binding to specific extracellular matrix molecules. The interactions between endothelial cells and their environment are also modulated by enzymes that degrade different matrix components and thus enable endothelial invasion. Recent reports on gene targeting in mice have confirmed the role of two classes of matrix receptors, integrins and cell surface heparan sulfate proteoglycans…

IntegrinsHistologybiologyNeovascularization PathologicAngiogenesisIntegrinProteolytic enzymesNeovascularization PhysiologicMatrix (biology)Matrix metalloproteinaseMatrix MetalloproteinasesCell biologyExtracellular MatrixExtracellular matrixEndothelial stem cellFibronectinMedical Laboratory TechnologyMicebiology.proteinAnimalsHumansEndothelium VascularAnatomyInstrumentationHeparan Sulfate ProteoglycansMicroscopy research and technique
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α5β1 integrin-mediated adhesion to fibronectin is required for axis elongation and somitogenesis in mice.

2011

The arginine-glycine-aspartate (RGD) motif in fibronectin (FN) represents the major binding site for α5β1 and αvβ3 integrins. Mice lacking a functional RGD motif in FN (FN(RGE/RGE)) or α5 integrin develop identical phenotypes characterized by embryonic lethality and a severely shortened posterior trunk with kinked neural tubes. Here we show that the FN(RGE/RGE) embryos arrest both segmentation and axis elongation. The arrest is evident at about E9.0, corresponding to a stage when gastrulation ceases and the tail bud-derived presomitic mesoderm (PSM) induces α5 integrin expression and assumes axis elongation. At this stage cells of the posterior part of the PSM in wild type embryos are tight…

IntegrinsMesodermIntegrinEmbryonic Developmentlcsh:MedicineApoptosisBiochemistryMiceSomitogenesisMolecular Cell BiologyCell AdhesionParaxial mesodermmedicineAnimalsSignaling in Cellular ProcessesReceptors VitronectinCell adhesionlcsh:ScienceBiologyAxis elongationCell ProliferationRGD motifMultidisciplinarybiologyGastrulationlcsh:RGene Expression Regulation DevelopmentalCell DifferentiationMolecular DevelopmentFibronectinsExtracellular MatrixCell biologyFibronectinmedicine.anatomical_structureSomitesCytochemistrybiology.proteinlcsh:QOligopeptidesCell Movement SignalingProtein BindingResearch ArticleDevelopmental BiologySignal TransductionPLoS ONE
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The Selective Regulation of αVβ1 Integrin Expression Is Based on the Hierarchical Formation of αV-containing Heterodimers

2002

The integrin beta1 subunit can form a heterodimer with 12 different alpha subunits. According to the present model, the expression level of any alphabeta complex is regulated by the availability of the specific alpha subunit, whereas beta1 subunit is constantly present in a large excess. The expression of several heterodimers containing the alphaV subunit seems to be regulated by an identical mechanism. The fact that many cells express alphaVbeta1 heterodimer, and that this fibronectin/vitronectin receptor may be selectively regulated, compromises the present model of the regulation of beta1 and alphaV integrins. We have tried to solve this problem by assuming that distinct alphabeta hetero…

IntegrinsProtein subunitCellIntegrinBiologyModels BiologicalBiochemistryAntigens CDComplementary DNATumor Cells CulturedmedicineHumansReceptors VitronectinMelanomaMolecular BiologyCell MembraneCell BiologyTransfectionIntegrin alphaVFibronectinsCell biologyGene Expression Regulation NeoplasticFibronectinmedicine.anatomical_structurebiology.proteinVitronectinCollagenDimerizationIntracellularProtein BindingJournal of Biological Chemistry
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Depletion of alphaV integrins from osteosarcoma cells by intracellular antibody expression induces bone differentiation marker genes and suppresses g…

1999

Integrin heterodimers sharing the common alphaV subunit are receptors for adhesion glycoproteins such as vitronectin and fibronectin. They are suggested to play an essential role in cell anchoring, differentiation, and survival. Here, we describe the construction of an expression plasmid coding for an intracellular single-chain antibody against alphaV integrin subunit. Saos-2 osteosarcoma cells transfected with this DNA construct showed an approximately 70-100% decrease in the cell surface expression of alphaVbeta3 and alphaVbeta5 integrins as shown by flow cytometry. Intracellular antibody expression had no effect on the mRNA levels of alphaV integrin. Pulse chase experiments of metabolica…

Intracellular FluidSialoglycoproteinsCellIntegrinBone and Bones03 medical and health sciences0302 clinical medicineAntigens CDmedicineCell AdhesionTumor Cells CulturedHumansOsteopontinVitronectinMolecular BiologyImmunoglobulin Fragments030304 developmental biologyGlycoproteins0303 health sciencesOsteosarcomabiologyOsteoblastCell DifferentiationTransfectionIntegrin alphaVAlkaline PhosphataseMolecular biologyFibronectinsFibronectinmedicine.anatomical_structure030220 oncology & carcinogenesisEnzyme Inductionbiology.proteinMatrix Metalloproteinase 2VitronectinOsteopontinIntracellularBiomarkersMatrix biology : journal of the International Society for Matrix Biology
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Irisin: A new potential hormonal target for the treatment of obesity and type 2 diabetes

2012

Irisinobesitymedicine.medical_specialtyIrisin; obesity; diabetesEndocrinology Diabetes and MetabolismMEDLINEEnergy metabolismType 2 diabetesMicePhysical Conditioning AnimalInternal medicineDiabetes mellitusAnimalsHumansMedicineHormone metabolismExercisediabetesPhysical conditioningbusiness.industrymedicine.diseaseObesityHormonesFibronectinsEndocrinologyDiabetes Mellitus Type 2Energy MetabolismbusinessHormoneJournal of Diabetes
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The cell adhesion domain of type XVII collagen promotes integrin-mediated cell spreading by a novel mechanism.

2001

Type XVII collagen (BP180) is a keratinocyte transmembrane protein that exists as the full-length protein in hemidesmosomes and as a 120-kDa shed ectodomain in the extracellular matrix. The largest collagenous domain of type XVII collagen, COL15, has been described previously as a cell adhesion domain (Tasanen, K., Eble, J. A., Aumailley, M., Schumann, H., Baetge, J, Tu, H., Bruckner, P., and Bruckner-Tuderman, L. (2000) J. Biol. Chem. 275, 3093-3099). In the present work, the integrin binding of triple helical, human recombinant COL15 was tested. Solid phase binding assays using recombinant integrin alpha(1)I, alpha(2)I, and alpha(10)I domains and cell spreading assays with alpha(1)beta(1)…

KeratinocytesIntegrinsDNA ComplementaryDystoninIntegrinAmino Acid MotifsNerve Tissue ProteinsCHO CellsBiochemistryAutoantigensCollagen receptorCell LineCell MovementCricetinaeCell AdhesionTumor Cells CulturedAnimalsHumansCloning MolecularCell adhesionMolecular BiologyIntegrin bindingbiologyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionHemidesmosomeCell BiologyNon-Fibrillar CollagensMolecular biologyRecombinant ProteinsProtein Structure TertiaryFibronectinHaCaTCytoskeletal ProteinsEctodomainbiology.proteinCollagenCarrier ProteinsPeptidesProtein BindingThe Journal of biological chemistry
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