Search results for "Integrin"

showing 10 items of 286 documents

Talin1 sets the stage for dendritic cell activation

2020

In dendritic cells, talin1 links integrin binding to efficient TLR downstream signaling through interaction with MyD88 and PIP5K.

TalinCellular differentiationImmunologyIntegrinInsightsMiceConditional gene knockoutImmune ToleranceImmunology and AllergyAnimalsSkinMice KnockoutMembrane GlycoproteinsbiologyChemistryChemotaxisToll-Like ReceptorsNF-kappa BReceptors Interleukin-1Dendritic cellCell biologyPhosphotransferases (Alcohol Group Acceptor)Langerhans CellsMyeloid Differentiation Factor 88biology.proteinCytokinesSignal transductionSignal TransductionThe Journal of Experimental Medicine
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Binding properties and stability of the Ras-association domain of Rap1-GTP interacting adapter molecule (RIAM).

2012

The Rap1-GTP interacting adapter protein (RIAM) is an important protein in Rap1-mediated integrin activation. By binding to both Rap1 GTPase and talin, RIAM recruits talin to the cell membrane, thus facilitating talin-dependent integrin activation. In this article, we studied the role of the RIAM Ras-association (RA) and pleckstrin-homology (PH) domains in the interaction with Rap1. We found that the RA domain was sufficient for GTP-dependent interaction with Rap1B, and the addition of the PH domain did not change the binding affinity. We also detected GTP-independent interaction of Rap1B with the N-terminus of RIAM. In addition, we found that the PH domain stabilized the RA domain both in …

TalinIntegrinsGTP'lcsh:MedicineGTPaseSignal transductionBiochemistryProtein structureMolecular cell biologyRIAMlcsh:Science0303 health sciencesMultidisciplinarybiologyProtein Stability030302 biochemistry & molecular biologySignal transducing adaptor proteinrap1 GTP-Binding ProteinssitoutuminenCell biologyPleckstrin homology domainRap1Research Articleendocrine systemvuorovaikutusProtein domainIntegrinSignaling in cellular processesPhosphoinositide Signal TransductionSignaling Pathways03 medical and health sciencesCell AdhesionHumansProtein InteractionsBiologyGTPase signaling030304 developmental biologyRas signalingAdaptor Proteins Signal Transducingintegriinitlcsh:RProteinsMembrane ProteinsRegulatory ProteinsProtein Structure TertiaryCytoskeletal Proteinsenzymes and coenzymes (carbohydrates)rap GTP-Binding ProteinsCell movement signalingbiology.proteinta1181lcsh:QPLoS ONE
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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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A Raft-derived, Pak1-regulated Entry Participates in α2β1 Integrin-dependent Sorting to Caveosomes

2008

We have previously shown that a human picornavirus echovirus 1 (EV1) is transported to caveosomes during 2 h together with its receptor alpha2beta1 integrin. Here, we show that the majority of early uptake does not occur through caveolae. alpha2beta1 integrin, clustered by antibodies or by EV1 binding, is initially internalized from lipid rafts into tubulovesicular structures. These vesicles accumulate fluid-phase markers but do not initially colocalize with caveolin-1 or internalized simian virus 40 (SV40). Furthermore, the internalized endosomes do not contain glycosylphosphatidylinositol (GPI)-anchored proteins or flotillin 1, suggesting that clustered alpha2beta1 integrin does not enter…

Time FactorsEndosomeAntigens Polyomavirus TransformingIntegrinCaveolaeClathrinCaveolinsModels BiologicalAmilorideMembrane MicrodomainsCaveolaeCell Line TumorCaveolinHumansMolecular BiologyDynaminMicroscopy ConfocalbiologyCell BiologyArticlesClathrinCell biologyEnterovirus B HumanIntegrin alpha Mp21-Activated KinasesType C Phospholipasesbiology.proteinIntegrin beta 6Integrin alpha2beta1
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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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Pharmacologic Inhibition of ADAM10 Attenuates Brain Tissue Loss, Axonal Injury and Pro-inflammatory Gene Expression Following Traumatic Brain Injury …

2021

The α-secretase A disintegrin and metalloprotease 10 (ADAM10) regulates various physiological and pathophysiological processes. Despite its broad functional implications during development, plasticity, and disease, no pharmacological approaches to inhibit ADAM10 in acute brain injury have been reported. Here, we examined the effects of the ADAM10 inhibitor GI254023X on the neurological and histopathological outcome after experimental traumatic brain injury (TBI). C57BL/6N mice were subjected to the controlled cortical impact (CCI) model of TBI or sham procedure and received GI254023X or vehicle during the acute phase of injury (n = 40, 100 mg/kg, 25% DMSO, 0.1 M Na2CO3, intraperitoneal, 30 …

Traumatic brain injuryADAM10PharmacologyBlood–brain barrierNeuroprotectionneuroinflammationaxonal injuryCell and Developmental Biologymedicinelcsh:QH301-705.5NeuroinflammationOriginal ResearchMicrogliabiologybusiness.industrytraumatic brain injuryADAM10 (a disintegrin and metalloprotease 10)Glutamate receptorCell Biologymedicine.diseaseGI254023Xmedicine.anatomical_structurelcsh:Biology (General)biology.proteinneuroprotectionGRIN2BbusinessDevelopmental BiologyFrontiers in Cell and Developmental Biology
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Il ruolo dei leucociti polimorfonucleati in patologia venosa

2009

Trombosi venosa profonda sindrome post-flebitica ulcere venose beta2-integrine
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Selective Binding of Collagen Subtypes by Integrin α1I, α2I, and α10I Domains

2001

Four integrins, namely alpha(1)beta(1), alpha(2)beta(1), alpha(10)beta(1), and alpha(11)beta(1), form a special subclass of cell adhesion receptors. They are all collagen receptors, and they recognize their ligands with an inserted domain (I domain) in their alpha subunit. We have produced the human integrin alpha(10)I domain as a recombinant protein to reveal its ligand binding specificity. In general, alpha(10)I did recognize collagen types I-VI and laminin-1 in a Mg(2+)-dependent manner, whereas its binding to tenascin was only slightly better than to albumin. When alpha(10)I was tested together with the alpha(1)I and alpha(2)I domains, all three I domains seemed to have their own collag…

Type IV collagenIntegrin alpha2Integrin alpha ChainsAlpha (ethology)Cell BiologyBiologyMolecular BiologyBiochemistryMolecular biologyType I collagenBinding domainCollagen receptorG alpha subunitJournal of Biological Chemistry
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ASTROCYTES SHED EXTRACELLULAR VESICLES THAT CONTAIN FIBROBLAST GROWTH FACTOR-2 AND VASCULAR ENDOTHELIAL GROWTH FACTOR.

2007

An important component of the pathogenic process of multiple sclerosis (MS) is the blood-brain barrier (BBB) damage. We recently set an in vitro model of BBB, based on a three-cell-type co-culture system, in which rat neurons and astrocytes synergistically induce brain capillary endothelial cells to form a monolayer with permeability properties resembling those of the physiological BBB. Herein we report that the serum from patients with secondary progressive multiple sclerosis (SPMS) has a damaging effect on isolated neurons. This finding suggests that neuronal damaging in MS could be a primary event and not only secondary to myelin damage, as generally assumed. SPMS serum affects the perme…

Vascular Endothelial Growth Factor ACellFluorescent Antibody TechniqueBiologyFibroblast growth factorCulture Media Serum-Freechemistry.chemical_compoundWestern blotSettore BIO/10 - BiochimicaGlial Fibrillary Acidic ProteinGeneticsmedicineAnimalsSecretionFibroblastCells Culturedmedicine.diagnostic_testVesicleIntegrin beta1Secretory VesiclesGeneral MedicineCell biologyRatsVascular endothelial growth factorastrocytesextracellular vesicle sheddingfibroblastic growth factors-2Protein Transportmedicine.anatomical_structureMembrane proteinchemistryAstrocytesFibroblast Growth Factor 2
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NEURONS PRODUCE FGF-2 AND VEGF SECRETE THEM AT LEST IN PART BY SHEDDING EXTRACELLULAR VESCICLES

2007

Abstract We previously found that neurons are able to affect the ability of brain capillary endothelial cells to form in vitro a monolayer with properties resembling the blood-brain barrier. We then looked, by immunofluorescence and western analysis, for factors, produced by neurons, with the potential to influence growth and differentiation of endothelial cells. In the present paper, we report that neurons produce both vascular endothelial growth factor and fibroblast growth factor 2, two well-known angiogenic factors. More interestingly, we gained evidence that both factors are released by neurons, at least in part, by shedding of extracellular vesicles, that contain β1 integrin, a membra…

Vascular Endothelial Growth Factor AFGF-2BiologyFibroblast growth factorchemistry.chemical_compoundsheddingNeurofilament ProteinsGlial Fibrillary Acidic ProteinExtracellularAnimalsSecretionRats WistarCells CulturedNeuronsVesicleIntegrin beta1Secretory VesiclesCell BiologyArticlesVEGFTransport proteinCell biologyRatsVascular endothelial growth factorVascular endothelial growth factor AProtein TransportMembrane proteinchemistryAstrocytesMolecular Medicineneurons vesicles fibroblastic growth factor-2 vascular endothelial growth factorCamptothecinFibroblast Growth Factor 2Extracellular Spaceextracellular vesicles
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