Search results for "INTEGRIN"

showing 10 items of 286 documents

Model of a six immunoglobulin-like domain fragment of filamin A (16-21) built using residual dipolar couplings.

2012

Filamins are actin-binding proteins that participate in a wide range of cell functions, including cell morphology, locomotion, membrane protein localization, and intracellular signaling. The three filamin isoforms found in humans, filamins A, B, and C, are highly homologous, and their roles are partly complementary. In addition to actin, filamins interact with dozens of other proteins that have roles as membrane receptors and channels, enzymes, signaling intermediates, and transcription factors. Filamins are composed of an N-terminal actin-binding domain and 24 filamin-type immunoglobulin-like domains (FLN) that form tail-to-tail dimers with their C-terminal FLN domain. Many of the filamin …

Gene isoformModels Molecularanimal structuresMagnetic Resonance SpectroscopyProtein ConformationFilaminsIntegrinBiomolecular structuremacromolecular substances010402 general chemistryFilaminCell morphologyCrystallography X-Ray01 natural sciencesBiochemistryCatalysis03 medical and health sciencesColloid and Surface ChemistryContractile ProteinsHumansTranscription factorImmunoglobulin FragmentsActin030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryMicrofilament ProteinsGeneral Chemistry0104 chemical sciencesCell biologybody regionsbiology.proteinGlycoproteinJournal of the American Chemical Society
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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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Increased Expression of β6-Integrin in Skin Leads to Spontaneous Development of Chronic Wounds

2004

Integrin alphavbeta6 is an epithelial cell-specific receptor that is not normally expressed by resting epithelium but its expression is induced during wound healing. The function of alphavbeta6-integrin in wound repair is not clear. In the present study, we showed that beta6-integrin expression was strongly up-regulated in the epidermis in human chronic wounds but not in different forms of skin fibrosis. To test whether increased beta6-integrin expression plays a role in abnormal wound healing we developed four homozygous transgenic mouse lines that constitutively expressed human beta6-integrin in the epithelium. The mice developed normally and did not show any histological abnormalities in…

Genetically modified mousePathologymedicine.medical_specialtyIntegrin beta ChainsMice TransgenicBiologyPolymerase Chain ReactionPathology and Forensic MedicineCicatrixMice03 medical and health sciences0302 clinical medicineTransforming Growth Factor betaFibrosismedicineAnimalsHumansIn Situ HybridizationSkin030304 developmental biologyWound Healing0303 health sciencesintegumentary systemEpidermis (botany)Transforming growth factor betamedicine.diseaseFibrosisImmunohistochemistryEpithelium3. Good healthBlotting Southernmedicine.anatomical_structure030220 oncology & carcinogenesisChronic Diseasebiology.proteinImmunohistochemistryWound healingRegular ArticlesTransforming growth factorThe American Journal of Pathology
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Role of the Netrin-like Domain of Procollagen C-Proteinase Enhancer-1 in the Control of Metalloproteinase Activity

2010

The netrin-like (NTR) domain is a feature of several extracellular proteins, most notably the N-terminal domain of tissue inhibitors of metalloproteinases (TIMPs), where it functions as a strong inhibitor of matrix metalloproteinases and some other members of the metzincin superfamily. The presence of a C-terminal NTR domain in procollagen C-proteinase enhancers (PCPEs), proteins that stimulate the activity of astacin-like tolloid proteinases, raises the possibility that this might also have inhibitory activity. Here we show that both long and short forms of the PCPE-1 NTR domain, the latter beginning at the N-terminal cysteine known to be critical for TIMP activity, show no inhibition, at …

Glycobiology and Extracellular MatricesMatrix metalloproteinaseBiochemistryBONE MORPHOGENETIC PROTEIN-1AdamalysinFIBRILLAR PROCOLLAGENSTolloid ProteinaseExtracellular Matrix Proteins0303 health sciencesADAMTSFRIZZLED-RELATED PROTEINS030302 biochemistry & molecular biologyTissue Inhibitor of Metalloproteinases11 Medical And Health SciencesALPHA-CONVERTING-ENZYMEI PROCOLLAGENADAM ProteinsExtracellular MatrixPLASMINOGEN ACTIVATIONBiochemistryCollagen03 Chemical SciencesLife Sciences & BiomedicineProcollagenBiochemistry & Molecular BiologyTERMINAL DOMAINTolloid-Like MetalloproteinasesADAMTSBiologyBone morphogenetic protein 1Cell Line03 medical and health sciencesDisintegrinHumansHUMAN TISSUE INHIBITORMatrix MetalloproteinaseMolecular BiologyGlycoproteins030304 developmental biologyThrombospondinScience & TechnologyHeparinADAMCell Biology06 Biological SciencesMATRIX-METALLOPROTEINASESProtein Structure TertiaryADAM ProteinsProcollagen peptidaseSULFATED GLYCOSAMINOGLYCANSEnzymologybiology.proteinJournal of Biological Chemistry
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Towards an understanding of the molecular basis of immune responses in sponges: The marine demospongeGeodia cydonium as a model

1999

The phylogenetic position of the phylum Porifera (sponges) is near the base of the kingdom Metazoa. During the last few years, not only rRNA sequences but, more importantly, cDNA/genes that code for proteins have been isolated and characterized from sponges, in particular from the marine demosponge Geodia cydonium. The analysis of the deduced amino acid sequences of these proteins allowed a molecular biological approach to the question of the monophyly of the Metazoa. Molecules of the extracellular matrix/basal lamina, with the integrin receptor, fibronectin, and galectin as prominent examples, and of cell-surface receptors (tyrosine kinase receptor), elements of sensory systems (crystallin…

HistologybiologyCell adhesion moleculeIntegrinbiology.organism_classificationReceptor tyrosine kinaseFibronectinMedical Laboratory TechnologySpongeDemospongeBiochemistrybiology.proteinAnatomySignal transductionInstrumentationGalectinMicroscopy Research and Technique
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Impact of therapeutically induced reactive oxygen species and radical scavenging by α-tocopherol on tumor cell adhesion

2007

Many tumor treatment modalities such as ionizing radiation or some chemotherapy induce reactive oxygen species (ROS) resulting in therapeutic cell damage. The aim of this study was to analyze whether such ROS induction may affect the mechanical stability of solid tumor tissue by degradation of the extracellular matrix proteins or by a loss of cell adhesion molecules. Additionally, the protective impact of alpha-tocopherol treatment on these processes was studied. Experimental DS-sarcomas in rats were treated with a combination of localized 44 degrees C hyperthermia, inspiratory hyperoxia and xanthine oxidase in order to induce pronounced oxidative stress. A second group of animals were pret…

Hyperoxiachemistry.chemical_classificationCancer ResearchReactive oxygen speciesbiologyCell adhesion moleculeIntegrinGeneral Medicinemedicine.diseasemedicine.disease_causeExtracellular matrixchemistry.chemical_compoundOncologyBiochemistrychemistrymedicinebiology.proteinCancer researchmedicine.symptomXanthine oxidaseCell damageOxidative stressOncology Reports
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Polymorphonuclear leukocyte rheology, cytosolic Ca2+ content, beta2-integrin expression and oxidative stress in hypertension.

2008

Hypertension Leukocyte rheology beta2-integrin oxidative stress.
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Human papillomavirus infection requires cell surface heparan sulfate.

2001

ABSTRACT Using pseudoinfection of cell lines, we demonstrate that cell surface heparan sulfate is required for infection by human papillomavirus type 16 (HPV-16) and HPV-33 pseudovirions. Pseudoinfection was inhibited by heparin but not dermatan or chondroitin sulfate, reduced by reducing the level of surface sulfation, and abolished by heparinase treatment. Carboxy-terminally deleted HPV-33 virus-like particles still bound efficiently to heparin. The kinetics of postattachment neutralization by antiserum or heparin indicated that pseudovirions were shifted on the cell surface from a heparin-sensitive into a heparin-resistant mode of binding, possibly involving a secondary receptor. Alpha-6…

ImmunologyIntegrinIntegrin alpha6Microbiologychemistry.chemical_compoundSulfationAntigens CDVirologymedicineAnimalsHumansChondroitin sulfateReceptorNeural Cell Adhesion MoleculesPapillomaviridaeAntiserumHeparinaseMembrane GlycoproteinsbiologyHeparinVirionHeparan sulfateHeparinMolecular biologyVirus-Cell InteractionschemistryInsect ScienceCOS Cellsbiology.proteinHeparitin SulfateLeukocyte L1 Antigen Complexmedicine.drugJournal of virology
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Photoactivatable caged cyclic RGD peptide for triggering integrin binding and cell adhesion to surfaces.

2011

We report the synthesis and properties of a photoactivatable caged RGD peptide and its application for phototriggering integrin- and cell-binding to surfaces. We analysed in detail 1) the differences in the integrin-binding affinity of the caged and uncaged forms by quartz crystal microbalance (QCM) studies, 2) the efficiency and yield of the photolytic uncaging reaction, 3) the biocompatibility of the photolysis by-products and irradiation conditions, 4) the possibility of site, temporal and density control of integrin-binding and therefore human cell attachment, and 5) the possibility of in situ generation of cell patterns and cell gradients by controlling the UV exposure. These studies p…

In situIntegrinsBiocompatibilityStereochemistryUltraviolet RaysCellIntegrinBiochemistryPeptides CyclicmedicineCell AdhesionHumansCell adhesionMolecular BiologyCells CulturedIntegrin bindingMaterialesbiologyChemistryOrganic ChemistryQuímicaQuartz crystal microbalanceCyclic rgd peptidemedicine.anatomical_structureBiophysicsbiology.proteinQuartz Crystal Microbalance TechniquesMolecular MedicineProtein BindingChembiochem : a European journal of chemical biology
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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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