Search results for "Integrin alpha5"

showing 7 items of 7 documents

Genetic abrogation of the fibronectin-α5β1 integrin interaction in articular cartilage aggravates osteoarthritis in mice.

2018

The balance between synthesis and degradation of the cartilage extracellular matrix is severely altered in osteoarthritis, where degradation predominates. One reason for this imbalance is believed to be due to the ligation of the α5β1 integrin, the classic fibronectin (FN) receptor, with soluble FN fragments instead of insoluble FN fibrils, which induces matrix metalloproteinase (MMP) expression. Our objective was to determine whether the lack of α5β1-FN binding influences cartilage morphogenesis in vivo and whether non-ligated α5β1 protects or aggravates the course of osteoarthritis in mice. We engineered mice (Col2a-Cre;Fn1RGE/fl), whose chondrocytes express an α5β1 binding-deficient FN, …

Cartilage ArticularMale0301 basic medicineIntegrinsKnee JointGlycobiologylcsh:MedicineCartilage morphogenesisOsteoarthritisMatrix metalloproteinaseBiochemistryExtracellular matrixMice0302 clinical medicineAnimal CellsMedicine and Health Scienceslcsh:ScienceConnective Tissue CellsStainingMultidisciplinarybiologyChemistryExtracellular MatrixCell biologymedicine.anatomical_structureConnective TissueProteoglycansMatrix Metalloproteinase 3AnatomyCellular Structures and OrganellesCellular TypesResearch ArticleIntegrin alpha5beta1Signal TransductionIntegrinMice TransgenicResearch and Analysis Methods03 medical and health sciencesChondrocytesPhysical Conditioning AnimalMatrix Metalloproteinase 13OsteoarthritisCell AdhesionmedicineAnimalsHumansRegenerationCytoplasmic Staining030203 arthritis & rheumatologyCartilagelcsh:RBiology and Life SciencesProteinsCell Biologymedicine.diseaseFibronectinsFibronectinDisease Models AnimalBiological TissueCartilage030104 developmental biologyProteoglycanSpecimen Preparation and Treatmentbiology.proteinSafranin Staininglcsh:QCollagensArticular CartilagePLoS ONE
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β1-Integrin Cytoplasmic Subdomains Involved in Dominant Negative Function

1998

The beta1-integrin cytoplasmic domain consists of a membrane proximal subdomain common to the four known isoforms ("common" region) and a distal subdomain specific for each isoform ("variable" region). To investigate in detail the role of these subdomains in integrin-dependent cellular functions, we used beta1A and beta1B isoforms as well as four mutants lacking the entire cytoplasmic domain (beta1TR), the variable region (beta1COM), or the common region (beta1 deltaCOM-B and beta1 deltaCOM-A). By expressing these constructs in Chinese hamster ovary and beta1 integrin-deficient GD25 cells (Wennerberg et al., J Cell Biol 132, 227-238, 1996), we show that beta1B, beta1COM, beta1 deltaCOM-B, a…

Gene isoformTalinCytoplasmProtein ConformationIntegrinMolecular Sequence DataCHO CellsIntegrin alpha5Platelet Membrane GlycoproteinsArticleFocal adhesionchemistry.chemical_compoundMiceAntigens CDCricetinaeCell AdhesionAnimalsActininAmino Acid SequencePhosphorylationCell adhesionMolecular BiologyBinding SitesbiologyCell adhesion moleculeChinese hamster ovary cellIntegrin beta1Integrin beta3Tyrosine phosphorylationCell BiologyIntegrin alphaVProtein-Tyrosine KinasesRecombinant ProteinsCell biologyFibronectinsFibronectinchemistryFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesMutationbiology.proteinCell Adhesion MoleculesSignal Transduction
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Bone Metastasis in Renal Cell Carcinoma is Preprogrammed in the Primary Tumor and Caused by AKT and Integrin α5 Signaling

2015

Bone metastasis develops in 30% of all patients with renal cell carcinoma. We elucidated the mechanisms that lead to and predict bone metastasis of renal cell carcinoma.Nine renal cell carcinoma primary cell lines and 30 renal cell carcinoma tissue specimens (normal and tumor tissue) were collected from 3 patients with no metastasis and 10 with lung or bone metastasis within 5 years after nephrectomy. Cell migration was analyzed in a Boyden chamber and proliferation was assessed by bromodeoxyuridine incorporation. Adhesion to fibronectin, and collagen I and IV was determined after cell staining. The expression and/or activity of cellular signaling molecules was quantified by Western blot.Co…

Pathologymedicine.medical_specialtyUrologyBlotting WesternBone NeoplasmsIntegrin alpha5MetastasisExtracellular matrixCell MovementRenal cell carcinomaCell Line TumormedicineCarcinomaHumansCarcinoma Renal CellKidneybiologybusiness.industryTumor Suppressor ProteinsPTEN PhosphohydrolaseBone metastasisCell migrationDNA Neoplasmmedicine.diseaseKidney NeoplasmsGene Expression Regulation NeoplasticFibronectinmedicine.anatomical_structurebiology.proteinCancer researchbusinessProto-Oncogene Proteins c-aktSignal TransductionJournal of Urology
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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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EGFL7 enhances surface expression of integrin α5β1 to promote angiogenesis in malignant brain tumors

2018

Abstract Glioblastoma (GBM) is a typically lethal type of brain tumor with a median survival of 15 months postdiagnosis. This negative prognosis prompted the exploration of alternative treatment options. In particular, the reliance of GBM on angiogenesis triggered the development of anti‐VEGF (vascular endothelial growth factor) blocking antibodies such as bevacizumab. Although its application in human GBM only increased progression‐free periods but did not improve overall survival, physicians and researchers still utilize this treatment option due to the lack of adequate alternatives. In an attempt to improve the efficacy of anti‐VEGF treatment, we explored the role of the egfl7 gene in ma…

0301 basic medicineMedicine (General)Vascular Biology & AngiogenesisAngiogenesisEndothelial Growth FactorsQH426-470chemistry.chemical_compoundangiogenesisMice0302 clinical medicineAntineoplastic Agents ImmunologicalResearch ArticlesCancerNeovascularization PathologicBrain NeoplasmsEndothelial stem cellVascular endothelial growth factormedicine.anatomical_structureTreatment Outcome030220 oncology & carcinogenesisendothelial cellMolecular MedicineHeterograftsEGFL7PericyteEGFL7medicine.drugResearch ArticleIntegrin alpha5beta1EGF Family of ProteinsintegrinBrain tumor03 medical and health sciencesR5-920GliomamedicineGeneticsHuman Umbilical Vein Endothelial CellsAnimalsHumansddc:610Cell ProliferationTemozolomidebusiness.industryCalcium-Binding ProteinsglioblastomaEndothelial Cellsmedicine.diseaseSurvival AnalysisDisease Models Animal030104 developmental biologychemistryCancer researchbusinessNeoplasm TransplantationNeuroscienceEMBO Molecular Medicine
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Fibronectin-bound α5β1 integrins sense load and signal to reinforce adhesion in less than a second

2017

Integrin-mediated mechanosensing of the extracellular environment allows cells to control adhesion and signalling. Whether cells sense and respond to force immediately upon ligand-binding is unknown. Here, we report that during adhesion initiation, fibroblasts respond to mechanical load by strengthening integrin-mediated adhesion to fibronectin (FN) in a biphasic manner. In the first phase, which depends on talin and kindlin as well as on the actin nucleators Arp2/3 and mDia, FN-engaged α5β1 integrins activate focal adhesion kinase (FAK) and c-Src in less than 0.5 s to steeply strengthen α5β1- and αV-class integrin-mediated adhesion. When the mechanical load exceeds a certain threshold, fib…

Talin0301 basic medicineTime FactorsMaterials scienceIntegrinNanotechnologyMechanotransduction CellularActin-Related Protein 2-3 ComplexCSK Tyrosine-Protein KinaseFocal adhesionMice03 medical and health sciencesCell AdhesionAnimalsGeneral Materials ScienceMechanotransductionCell adhesionActinMice KnockoutbiologyCell adhesion moleculeMechanical EngineeringGeneral ChemistryAdhesionFibroblastsCondensed Matter PhysicsFibronectinsCell biologyFibronectinsrc-Family Kinases030104 developmental biologyMechanics of MaterialsFocal Adhesion Kinase 1biology.proteinApplications of AFM; integrins; Mechanotransduction; Microscopy; Nanoscale biophysicsIntegrin alpha5beta1Nature Materials
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Transcription of α2 Integrin Gene in Osteosarcoma Cells Is Enhanced by Tumor Promoters

1998

Integrin alpha2beta1 is a heterodimeric transmembrane receptor for collagens. In osteogenic cells the expression of alpha2beta1 integrin is induced by both Kirsten sarcoma virus and chemical transformation. The association of alpha2 integrin with transformed cell phenotype was studied further by testing the effects of two tumor promoters, 12-O-tetradecanoylphorbol 13-acetate (TPA) and okadaic acid (OA), on human MG-63 osteosarcoma cells. TPA, an activator of protein kinase C, increased the cell surface expression of alpha2 integrin and the corresponding mRNA levels. Nuclear run-on assays indicated that TPA activated the transcription of alpha2 integrin gene. TPA also slightly increased the …

IntegrinsTime FactorsTranscription GeneticIntegrin alpha3IntegrinIntegrin alpha2CD18Integrin alpha5CD49cCD49bCollagen receptorAntigens CDOkadaic AcidCell AdhesionTumor Cells CulturedHumansCollagenasesRNA MessengerOsteosarcomabiologyActivator (genetics)Integrin beta1Cell BiologyIntegrin alphaVBlotting NorthernFlow CytometryMolecular biologyUp-RegulationIntegrin alpha MCarcinogensbiology.proteinTetradecanoylphorbol AcetateIntegrin beta 6CollagenMatrix Metalloproteinase 1Experimental Cell Research
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