Search results for "Integrin beta1"

showing 10 items of 23 documents

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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The inhibitor of differentiation-1 (Id1) enables lung cancer liver colonization through activation of an EMT program in tumor cells and establishment…

2017

Abstract: Id1 promotes carcinogenesis and metastasis, and predicts prognosis of non-small cell lung cancer (NSCLC)-adenocarcionoma patients. We hypothesized that Id1 may play a critical role in lung cancer colonization of the liver by affecting both tumor cells and the microenvironment. Depleted levels of Id1 in LLC (Lewis lung carcinoma cells, LLC shId1) significantly reduced cell proliferation and migration in vitro. Genetic loss of Id1 in the host tissue (Id1(-/-) mice) impaired liver colonization and increased survival of Id1 animals. Histologically, the presence of Idl in tumor cells of liver metastasis was responsible for liver colonization. Microarray analysis comparing liver tumor n…

Inhibitor of Differentiation Protein 10301 basic medicineCancer ResearchPathologyLung NeoplasmsTime Factors10255 Clinic for Thoracic SurgeryVimentinmedicine.disease_causeMetastasisCarcinoma Lewis Lung0302 clinical medicineCell MovementCarcinoma Non-Small-Cell LungTumor Microenvironment1306 Cancer ResearchMice KnockoutTissue microarrayIntegrin beta1Liver NeoplasmsTumor BurdenGene Expression Regulation NeoplasticOncology030220 oncology & carcinogenesis2730 OncologySignal Transductionmedicine.medical_specialtyEpithelial-Mesenchymal TransitionLiver tumor610 Medicine & healthBiologyTransforming Growth Factor beta103 medical and health sciencesCell Line Tumor10049 Institute of Pathology and Molecular PathologymedicineAnimalsHumansVimentinEpithelial–mesenchymal transitionLung cancerCell ProliferationLewis lung carcinomamedicine.diseaseMice Inbred C57BL030104 developmental biologyCancer researchbiology.proteinHuman medicineSnail Family Transcription FactorsCarcinogenesisCancer Letters
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β1D Integrin Inhibits Cell Cycle Progression in Normal Myoblasts and Fibroblasts

1998

Integrins are alphabeta heterodimeric transmembrane receptors involved in the regulation of cell growth and differentiation. The beta1 integrin subunit is widely expressed in vivo and is represented by four alternatively spliced cytoplasmic domain isoforms. beta1D is a muscle-specific variant of beta1 integrin and a predominant beta1 isoform in striated muscles. In the present study we showed that expression of the exogenous beta1D integrin in C2C12 myoblasts and NIH 3T3 or REF 52 fibroblasts inhibited cell proliferation. Unlike the case of the common beta1A isoform, adhesion of beta1D-transfected C2C12 myoblasts specifically via the expressed integrin did not activate mitogen-activated pro…

IntegrinsRecombinant Fusion ProteinsMolecular Sequence DataIntegrinSignal transductionTransfectionCell adhesion; Integrins; Signal transduction; Alternative splicing isoforms; Cell proliferation; MyodifferentiationBiochemistryCD49cCell LineCollagen receptorMiceAlternative splicing isoformsCell surface receptorAnimalsAmino Acid SequenceMuscle SkeletalMolecular BiologyCell proliferationMyodifferentiationbiologyCell growthIntegrin beta1Cell CycleCell adhesionCell DifferentiationReceptors Interleukin-2Cell BiologyImmunohistochemistryMolecular biologyCell biologyEnzyme ActivationProto-Oncogene Proteins c-rafAlternative SplicingGenes rasIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6C2C12Journal of Biological Chemistry
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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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The impact of conventional and heavy ion irradiation on tumor cell migration in vitro.

2007

The influence of X-ray and (12)C heavy ion irradiation on tumor cell migration and of beta(3) and beta(1) integrin expression was investigated.Two different tumor cell lines (U87 glioma and HCT116 colon carcinoma cells) were irradiated with 1, 3, or 10 Gy X-rays or (12)C heavy ions. 24 h after irradiation a standardized Boyden Chamber assay for migration analysis was performed and cells were lysed for Western blotting.Radiation-induced influences were cell line- and radiation type-dependent. X-rays decreased HCT116 migration at higher doses and appear to increase U87 migration after 3 Gy. Heavy ions decreased migration of both cell lines dose-dependently. A trend of increased beta(3) and be…

LysisHeavy Ion RadiotherapyCell MovementGliomaCell Line TumorNeoplasmsmedicineTumor Cell MigrationHumansRadiology Nuclear Medicine and imagingIrradiationNeoplasm MetastasisneoplasmsRadiological and Ultrasound TechnologyChemistryIntegrin beta1RadiochemistryIntegrin beta3Dose-Response Relationship RadiationGliomaHeavy Ion Radiotherapymedicine.diseaseMolecular biologyIn vitroDose–response relationshipCell cultureColonic NeoplasmsInternational journal of radiation biology
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Three-dimensional invasion of human glioblastoma cells remains unchanged by X-ray and carbon ion irradiation in vitro.

2012

Purpose Cell invasion represents one of the major determinants that treatment has failed for patients suffering from glioblastoma. Contrary findings have been reported for cell migration upon exposure to ionizing radiation. Here, the migration and invasion capability of glioblastoma cells on and in collagen type I were evaluated upon irradiation with X-rays or carbon ions. Methods and Materials Migration on and invasion in collagen type I were evaluated in four established human glioblastoma cell lines exposed to either X-rays or carbon ions. Furthermore, clonogenic radiation survival, proliferation (5-bromo-2-deoxyuridine positivity), DNA double-strand breaks (γH2AX/53BP1-positive foci), a…

MAPK/ERK pathwayCancer ResearchCell signalingMMP2MAP Kinase Kinase 4p38 Mitogen-Activated Protein KinasesCollagen Type IExtracellular matrixHistonesPhosphatidylinositol 3-KinasesCell MovementMedicineHumansRadiology Nuclear Medicine and imagingDNA Breaks Double-StrandedNeoplasm InvasivenessClonogenic assayPI3K/AKT/mTOR pathwayCell ProliferationRadiationbusiness.industryCell growthBrain NeoplasmsIntegrin beta1Intracellular Signaling Peptides and ProteinsCell migrationCarbonOncologyBromodeoxyuridineImmunologyCancer researchbusinessCell Migration AssaysGlioblastomaTumor Suppressor p53-Binding Protein 1International journal of radiation oncology, biology, physics
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β1 integrin signaling promotes neuronal migration along vascular scaffolds in the post-stroke brain

2017

Cerebral ischemic stroke is a main cause of chronic disability. However, there is currently no effective treatment to promote recovery from stroke-induced neurological symptoms. Recent studies suggest that after stroke, immature neurons, referred to as neuroblasts, generated in a neurogenic niche, the ventricular-subventricular zone, migrate toward the injured area, where they differentiate into mature neurons. Interventions that increase the number of neuroblasts distributed at and around the lesion facilitate neuronal repair in rodent models for ischemic stroke, suggesting that promoting neuroblast migration in the post-stroke brain could improve efficient neuronal regeneration. To move t…

Male0301 basic medicineChain migrationlcsh:MedicineExtracellular matrixNeural Stem CellsCell MovementLamininCells CulturedMice KnockoutNeuronslcsh:R5-920Mice Inbred ICRMicroscopy ConfocalTissue ScaffoldsbiologyIntegrin beta1BrainCell migrationGeneral MedicineCell biologyStrokeVasculature-guided migrationFemaleBlood vesselmedicine.symptomlcsh:Medicine (General)Signal TransductionResearch Paperanimal structuresIntegrinMice TransgenicGeneral Biochemistry Genetics and Molecular BiologyLesion03 medical and health sciencesNeuroblastβ1 integrinNeuroblast migrationmedicineAnimalsRegeneration (biology)lcsh:RCoculture TechniquesMicroscopy Electron030104 developmental biologynervous systemAstrocytesImmunologybiology.proteinBlood VesselsLamininEBioMedicine
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The effect of detergents on the basement membrane complex of a biologic scaffold material

2013

The basement membrane complex (BMC) is a critical component of the extracellular matrix (ECM) that supports and facilitates the growth of cells. This study investigates four detergents commonly used in the process of tissue decellularization and their effect upon the BMC. The BMC of porcine urinary bladder was subjected to 3% Triton-X 100, 8 mM 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate (CHAPS), 4% sodium deoxycholate or 1% sodium dodecyl sulfate (SDS) for 24 h. The BMC structure for each treatment group was assessed by immunolabeling, scanning electron microscopy (SEM) and second harmonic generation (SHG) imaging of the fiber network. The composition was assessed by quantif…

Sus scrofaFluorescent Antibody TechniqueBiochemistryBasement MembraneGlycosaminoglycanExtracellular matrixImmunolabelingchemistry.chemical_compoundTissue ScaffoldChapsSodium dodecyl sulfateDecellularizationGlycosaminoglycansMicrovesselEndothelial CellDecellularizationTissue ScaffoldsIntegrin beta1Extracellular matrixGeneral Medicinemedicine.anatomical_structureCollagenHumanBiotechnologyDetergentMaterials scienceDetergentsBiomedical EngineeringArticleBiomaterialsImaging Three-DimensionalRe-endothelizationIn Situ Nick-End LabelingmedicineAnimalsHumansMolecular BiologyOrgan engineeringBasement membraneStaining and LabelingAnimalBiologic scaffoldAntigens CD29Endothelial CellsDNABiomaterialMolecular biologyKi-67 AntigenGlycosaminoglycanchemistryTissue DecellularizationMicrovesselsActa Biomaterialia
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Promotion of osteogenic cell response using quasicovalent immobilized fibronectin on titanium surfaces: introduction of a novel biomimetic layer syst…

2012

Purpose Despite the undeniable potential of cell adhesion molecules such as fibronectin to support osteogenic cell responses and consecutive dental implant healing, the most beneficial mode of application onto titanium implant surfaces still requires investigation. Unspecific fibronectin adsorption on titanium dioxide (TiO2) surfaces can result in low-loading, high-desorption rates and protein–metal interactions with impaired biologic activity. The aim of the present study was to monitor the osteogenic cell responses (cell adhesion, proliferation, and differentiation) specifically to fibronectin biofunctionalized TiO2. Materials and Methods An innovative biomimetic streptavidin-biotin layer…

Time FactorsCellular differentiationOsteocalcinCell Culture TechniquesBiotinBiocompatible MaterialsCore Binding Factor Alpha 1 SubunitCell LineCyclin D1Biomimetic MaterialsOsteogenesisCell AdhesionMedicineHumansCyclin D1Cell adhesionCell ProliferationTitaniumOsteoblastsbiologyCell adhesion moleculebusiness.industryIntegrin beta1Cell DifferentiationAdhesionSilanesAlkaline PhosphataseFibronectinsFibronectinImmobilized ProteinsPhenotypeOtorhinolaryngologyBiotinylationVitamin B Complexbiology.proteinBiophysicsAlkaline phosphataseSurgeryAdsorptionStreptavidinOral SurgerybusinessJournal of oral and maxillofacial surgery : official journal of the American Association of Oral and Maxillofacial Surgeons
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Factor VIIa-induced interaction with integrin controls the release of tissue factor on extracellular vesicles from endothelial cells.

2019

Essentials Prothrombotic extracellular vesicles (EV) carry agonist pathway-specific proteomes Agonists for protease activated receptor (PAR) 2 signaling have distinct effects on EV composition PAR2 signaling rapidly generates prothrombotic EV and slowly EV with inactive tissue factor (TF) FVIIa integrin ligation restricts TF incorporation into EV from endothelial cells SUMMARY: Background Cell injury signal-induced activation and release of tissue factor (TF) on extracellular vesicles (EVs) from immune and vessel wall cells propagate local and systemic coagulation initiation. TF trafficking and release on EVs occurs in concert with the release of cell adhesion receptors, including integrin …

Time Factorsmedia_common.quotation_subjectIntegrinFactor VIIa030204 cardiovascular system & hematologyThromboplastin03 medical and health sciencesTissue factorchemistry.chemical_compoundExtracellular Vesicles0302 clinical medicineHumansReceptor PAR-2Protease-activated receptorintegrin traffickingInternalizationReceptorCell adhesionBlood CoagulationCells Culturedmedia_commonbiologyFactor VIIChemistryIntegrin beta1protease-activated receptorsEndothelial CellsHematologytissue factorCell biologyProtein Transportbiology.proteinOligopeptidesIntracellularSignal TransductionJournal of thrombosis and haemostasis : JTH
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