Search results for "INTEGRIN"

showing 10 items of 286 documents

Characterization of a putative extracellular matrix protein from the beetle Tenebrio molitor: hormonal regulation during metamorphosis.

2004

0949-944X (Print) Journal Article Research Support, Non-U.S. Gov't; We used differential display to isolate epidermis cDNAs corresponding to juvenile-hormone analog-regulated mRNA from the beetle Tenebrio molitor. One of them encodes a putative extracellular matrix (ECM) protein, named Tenebrin. Indeed, the deduced protein sequence contains ECM typical features like the presence of a signal peptide, internal repeats, a RGD tripeptide sequence motif known to bind integrins and von Willebrand factor type c domains involved in protein-protein interactions. Northern blot analysis reveals a single transcript of about 11 kb with an expression pattern correlated to 20-hydroxyecdysone fluctuations …

Signal peptideIntegrinMolecular Sequence DataCycloheximideBiologyExtracellular matrixchemistry.chemical_compoundExtracellular Matrix Proteins/*genetics/metabolismGeneticsAnimalsDevelopmentalHormones/physiologyNorthern blotAmino Acid SequenceTenebrioTenebrio/*geneticsDifferential displayMessenger RNAExtracellular Matrix ProteinsMetamorphosisMetamorphosis BiologicalGene Expression Regulation DevelopmentalBiological/*physiologyHormoneschemistryBiochemistryGene Expression RegulationJuvenile hormonebiology.proteinDevelopmental BiologyDevelopment genes and evolution
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Tetraspanin CD151 Mediates Papillomavirus Type 16 Endocytosis

2013

ABSTRACT Human papillomavirus type 16 (HPV16) is the primary etiologic agent for cervical cancer. The infectious entry of HPV16 into cells occurs via a so-far poorly characterized clathrin- and caveolin-independent endocytic pathway, which involves tetraspanin proteins and actin. In this study, we investigated the specific role of the tetraspanin CD151 in the early steps of HPV16 infection. We show that surface-bound HPV16 moves together with CD151 within the plane of the membrane before they cointernalize into endosomes. Depletion of endogenous CD151 did not affect binding of viral particles to cells but resulted in reduction of HPV16 endocytosis. HPV16 uptake is dependent on the C-termina…

Small interfering RNAEndosomevirusesmedia_common.quotation_subjectDNA Mutational AnalysisImmunologyEndocytic cycleIntegrinTetraspanin 24EndocytosisMicrobiologyClathrinCell LineTetraspaninVirologyHumansInternalizationmedia_commonHuman papillomavirus 16integumentary systembiologyvirus diseasesVirus InternalizationMolecular biologyEndocytosisfemale genital diseases and pregnancy complicationsVirus-Cell InteractionsCell biologyGene Knockdown TechniquesInsect Sciencebiology.proteinMutant ProteinsJournal of Virology
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Internalization of coxsackievirus A9 is mediated by {beta}2-microglobulin, dynamin, and Arf6 but not by caveolin-1 or clathrin.

2010

ABSTRACT Coxsackievirus A9 (CAV9) is a member of the human enterovirus B species within the Enterovirus genus of the family Picornaviridae . It has been shown to utilize αV integrins, particularly αVβ6, as its receptors. The endocytic pathway by which CAV9 enters human cells after the initial attachment to the cell surface has so far been unknown. Here, we present a systematic study concerning the internalization mechanism of CAV9 to A549 human lung carcinoma cells. The small interfering RNA (siRNA) silencing of integrin β6 subunit inhibited virus proliferation, confirming that αVβ6 mediates the CAV9 infection. However, siRNAs against integrin-linked signaling molecules, such as Src, Fyn, R…

Small interfering RNAmedia_common.quotation_subjectImmunologyEndocytic cycleIntegrinCaveolin 1CoxsackievirusEndocytosisCaveolaeMicrobiologyClathrinAmilorideDynamin IIVirologyCell Line TumorHumansRNA Small InterferingInternalizationmedia_commonDynaminbiologyADP-Ribosylation FactorsVirus Internalizationbiology.organism_classificationMolecular biologyClathrinEndocytosisCell biologyEnterovirus B HumanVirus-Cell InteractionsADP-Ribosylation Factor 6Insect Sciencebiology.proteinPinocytosisbeta 2-MicroglobulinJournal of virology
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Molecular mechanism of T-cell protein tyrosine phosphatase (TCPTP) activation by mitoxantrone.

2013

T-cell protein tyrosine phosphatase (TCPTP) is a ubiquitously expressed non-receptor protein tyrosine phosphatase. It is involved in the negative regulation of many cellular signaling pathways. Thus, activation of TCPTP could have important therapeutic applications in diseases such as cancer and inflammation. We have previously shown that the α-cytoplasmic tail of integrin α1β1 directly binds and activates TCPTP. In addition, we have identified in a large-scale high-throughput screen six small molecules that activate TCPTP. These small molecule activators include mitoxantrone and spermidine. In this study, we have investigated the molecular mechanism behind agonist-induced TCPTP activation.…

SpermidineProtein tyrosine phosphataseBiochemistryAnalytical Chemistry0302 clinical medicinePhosphorylationDatabases Protein0303 health sciencesProtein Tyrosine Phosphatase Non-Receptor Type 2biologyChemistrySmall molecule3. Good healthCell biologyisothermal titration calorimetryMolecular Docking Simulationmolecular dynamics simulation030220 oncology & carcinogenesis/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingThermodynamicsHydrophobic and Hydrophilic InteractionsProtein BindingSignal TransductionCell signalingintegrinIntegrinPhosphataseStatic ElectricityBiophysicsAntineoplastic AgentsMolecular Dynamics Simulationta3111mitoxantroneIntegrin alpha1beta1Small Molecule Libraries03 medical and health sciencesSDG 3 - Good Health and Well-beingdifferential scanning fluorimetryHumansBinding siteMolecular Biology030304 developmental biologyT-cell protein tyrosine phosphataseta1182ta3122In vitroProtein Structure TertiaryKineticsCytoplasmbiology.proteinMitoxantronePeptidesBiochimica et Biophysica Acta: Proteins and Proteomics
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Echovirus 1 Endocytosis into Caveosomes Requires Lipid Rafts, Dynamin II, and Signaling EventsV⃞

2004

Binding of echovirus 1 (EV1, a nonenveloped RNA virus) to the α2β1 integrin on the cell surface is followed by endocytic internalization of the virus together with the receptor. Here, video-enhanced live microscopy revealed the rapid uptake of fluorescently labeled EV1 into mobile, intracellular structures, positive for green fluorescent protein-tagged caveolin-1. Partial colocalization of EV1 with SV40 (SV40) and cholera toxin, known to traffic via caveosomes, demonstrated that the vesicles were caveosomes. The initiation of EV1 infection was dependent on dynamin II, cholesterol, and protein phosphorylation events. Brefeldin A, a drug that prevents SV40 transport, blocked the EV1 infection…

SucroseTime FactorsvirusesEndocytic cycleDynamin IIchemistry.chemical_compoundDynamin IIPhosphorylationInternalizationCytoskeletonIn Situ HybridizationIn Situ Hybridization Fluorescencemedia_commonGenes Dominant0303 health sciencesMicroscopy Videobiology030302 biochemistry & molecular biologyArticlesBrefeldin AEndocytosisCell biologyEnterovirus B HumanCholesterolRNA ViralElectrophoresis Polyacrylamide GelProtein BindingSignal TransductionCholera Toxinmedia_common.quotation_subjectIntegrinGreen Fluorescent ProteinsImmunoblottingEndocytosisTransfectionCell Line03 medical and health sciencesCapsidMembrane MicrodomainsViral entryCentrifugation Density GradientAnimalsMolecular Biology030304 developmental biologyBinding SitesBrefeldin ACell MembraneCell BiologyKineticschemistryViral replicationMicroscopy Fluorescencebiology.protein
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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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The role of the fibronectin synergy site in skin wound healing

2022

Upon skin barrier disruption, complex cellular and molecular events are activated to repair the damage and restore skin integrity. In adulthood, the outcome of this process can result in scarring and fibrosis, whereas complete tissue regeneration is observed in fetal wounds and wounds in lower vertebrates and invertebrates .Although there is abundant literature about the factors and mechanisms that determine the endpoint of either scarring/fibrosis or regeneration after tissue injury, the process is still poorly understood. After cutaneous injury, fibronectin (FN) is instantly released and deposited by cells, and represents a major ECM component in all stages of the wound healing process. F…

TGF-β1myofibroblastsUNESCO::CIENCIAS DE LA VIDAsynergy sitewound healingα5β1 integrinfibronecin
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Strategies to Target ADAM17 in Disease: From Its Discovery to the iRhom Revolution

2021

For decades, disintegrin and metalloproteinase 17 (ADAM17) has been the object of deep investigation. Since its discovery as the tumor necrosis factor convertase, it has been considered a major drug target, especially in the context of inflammatory diseases and cancer. Nevertheless, the development of drugs targeting ADAM17 has been harder than expected. This has generally been due to its multifunctionality, with over 80 different transmembrane proteins other than tumor necrosis factor α (TNF) being released by ADAM17, and its structural similarity to other metalloproteinases. This review provides an overview of the different roles of ADAM17 in disease and the effects of its ablation in a n…

TIMPsEGFRiRhomsTNFAnti-Inflammatory AgentsPharmaceutical ScienceInflammationContext (language use)Antineoplastic AgentsDiseaseComputational biologyReviewADAM17 ProteinmetalloproteinasesAnalytical Chemistrylcsh:QD241-44103 medical and health sciences0302 clinical medicineImmune systemlcsh:Organic chemistryIn vivoNeoplasmsDrug DiscoverymedicineDisintegrinTIMPADAM17 ProteinAnimalsHumansPhysical and Theoretical Chemistry030304 developmental biologyInflammation0303 health sciencesADAM17biologyOrganic ChemistryIntracellular Signaling Peptides and ProteinsiRhomChemistry (miscellaneous)030220 oncology & carcinogenesisbiology.proteinADAM17; Ectodomain shedding; EGFR; IRhoms; Metalloproteinases; TIMPs; TNF; ADAM17 Protein; Animals; Anti-Inflammatory Agents; Antineoplastic Agents; Humans; Inflammation; Intracellular Signaling Peptides and Proteins; NeoplasmsMolecular MedicineTumor necrosis factor alphametalloproteinaseectodomain sheddingmedicine.symptomMolecules
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Type-II transmembrane prolyl dipeptidases and matrix metalloproteinases in membrane vesicles of active endothelial cells.

2006

Conclusions: 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 mech…

TUMOR-CELLSCell MembraneBREAST-CARCINOMA CELLSEndothelial CellsUP-REGULATIONANGIOGENESISMatrix MetalloproteinasesExtracellular MatrixACTIVATIONEnzyme ActivationNEUROPEPTIDE-YCell MovementSEPRASESettore BIO/10 - BiochimicaMETASTASISPEPTIDASE-IVHumansDipeptidyl-Peptidases and Tripeptidyl-PeptidasesINTEGRINCells CulturedAdvances in experimental medicine and biology
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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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