Search results for "Integrin alpha Chains"

showing 10 items of 10 documents

Ultrastructure of regions containing homologous loci in polytene chromosomes of Drosophila melanogaster and Drosophila subobscura.

1998

We have used a new approach involving in situ hybridisation and electron microscopy to establish ultrastructural homologies between polytene chromosome regions of Drosophila melanogaster and Drosophila subobscura. Twelve probes were chosen to cover all the chromosomal elements: the myospheroid gene, the collagen type IV gene, the collagen-like gene, the w26 homeobox gene, the beta3 tubulin gene, the kinesin heavy chain gene, the tryptophan hydrolase gene, the Hsp82, Hsp22-26 and Hsp23-28, Hsp68, Hsp70 genes and the beta unit of the F0-F1 ATPase gene. Most of these loci were previously undescribed in D. subobscura and imprecisely located in D. melanogaster. We have demonstrated here, by an u…

0106 biological sciencesIntegrinsHSP30 Heat-Shock ProteinsKinesinsMuscle ProteinsLocus (genetics)Genes InsectTryptophan Hydroxylase010603 evolutionary biology01 natural sciencesHomology (biology)Chromosomes03 medical and health sciencesTubulinSequence Homology Nucleic AcidGeneticsMelanogasterAnimalsDrosophila ProteinsHSP20 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsGeneGenetics (clinical)Heat-Shock Proteins030304 developmental biologyGenetics0303 health sciencesPolytene chromosomebiologyMembrane Proteinsbiology.organism_classificationDrosophila subobscuraChromosome BandingProton-Translocating ATPasesDrosophila melanogasterChromosomal regionCollagenDrosophila melanogasterDNA ProbesIntegrin alpha ChainsChromosoma
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Cleavage of endometrial α-integrins into their functional forms is mediated by proprotein convertase 5/6.

2012

Background Proprotein convertases (PCs) post-translationally activate a large number of protein precursors through limited cleavage. PC5/6 (PC6) in the human endometrium is tightly regulated during receptivity for embryo implantation. Integrins are transmembrane glycoproteins, some of which play an important role in the adhesive interactions between the trophoblast (blastocyst) and uterine epithelium at implantation. Integrins require PC cleavage for post-translational modification. We hypothesize that pro-integrin-αs in the endometrial epithelium are post-translationally cleaved by PC6 into functional subunits for the binding of blastocyst and adhesion of extracellular matrix proteins. Met…

BiopsyIntegrinCleavage (embryo)Gene Expression Regulation EnzymologicEndometriumPregnancymedicineCell AdhesionHumansBlastocystEmbryo ImplantationCell adhesionCells CulturedGlycoproteinsbiologyRehabilitationObstetrics and GynecologyTrophoblastTransfectionMolecular biologyFibronectinsFibronectinmedicine.anatomical_structureBlastocystReproductive Medicinebiology.proteinProprotein Convertase 5CalciumFemaleProprotein ConvertasesIntegrin alpha ChainsProtein Processing Post-TranslationalHuman reproduction (Oxford, England)
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β-Catenin Signaling Drives Differentiation and Proinflammatory Function of IRF8-Dependent Dendritic Cells

2014

Abstract β-Catenin signaling has recently been tied to the emergence of tolerogenic dendritic cells (DCs). In this article, we demonstrate a novel role for β-catenin in directing DC subset development through IFN regulatory factor 8 (IRF8) activation. We found that splenic DC precursors express β-catenin, and DCs from mice with CD11c-specific constitutive β-catenin activation upregulated IRF8 through targeting of the Irf8 promoter, leading to in vivo expansion of IRF8-dependent CD8α+, plasmacytoid, and CD103+CD11b− DCs. β-Catenin–stabilized CD8α+ DCs secreted elevated IL-12 upon in vitro microbial stimulation, and pharmacological β-catenin inhibition blocked this response in wild-type cells…

CD8 AntigensCellular differentiationImmunologyReceptors Cell SurfaceVaccinia virusPyrimidinonesCD8-Positive T-LymphocytesBiologyParasite LoadArticleProinflammatory cytokineMiceAntigens CDVacciniaAnimalsImmunology and AllergyPromoter Regions Geneticbeta CateninInflammationMice KnockoutCell DifferentiationDendritic CellsT lymphocyteTh1 CellsBridged Bicyclo Compounds HeterocyclicInterleukin-12CD11c AntigenCell biologyEnzyme ActivationMice Inbred C57BLInterferon Regulatory FactorsInterleukin 12FemaleIRF8Signal transductionIntegrin alpha ChainsToxoplasmaSpleenToxoplasmosisCD8Signal TransductionInterferon regulatory factorsThe Journal of Immunology
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Mammary-derived growth inhibitor (MDGI) interacts with integrin α-subunits and suppresses integrin activity and invasion

2010

The majority of mortality associated with cancer is due to formation of metastases from the primary tumor. Adhesion mediated by different integrin heterodimers has an important role during cell migration and invasion. Protein interactions with the β1-integrin cytoplasmic tail are known to influence integrin affinity for extracellular ligands, but regulating binding partners for the α-subunit cytoplasmic tails have remained elusive. In this study, we show that mammary-derived growth inhibitor (MDGI) (also known as FABP-3 or H-FABP) binds directly to the cytoplasmic tail of integrin α-subunits and its expression inhibits integrin activity. In breast cancer cell lines, MDGI expression correlat…

Cancer Researchmedicine.disease_causemigrationCD49cCollagen receptor0302 clinical medicineCell Movement0303 health sciencesCell migrationMiddle Agedinvasion3. Good healthCell biologyExtracellular MatrixadhesionIntegrin alpha MMDGI030220 oncology & carcinogenesis/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingIntegrin beta 6FemaleFatty Acid Binding Protein 3Integrin alpha Chainsmedicine.medical_specialtyintegrinIntegrinMolecular Sequence DataBreast NeoplasmsBiologyFatty Acid-Binding ProteinsCollagen Type IDisease-Free Survival03 medical and health sciencesbreast cancerSDG 3 - Good Health and Well-beingInternal medicineCell Line TumorGeneticsmedicineHumansNeoplasm InvasivenessProtein Interaction Domains and MotifsAmino Acid SequenceMolecular Biology030304 developmental biologyFibronectinsFibronectinEndocrinologybiology.proteinCarcinogenesisOncogene
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IL-23-mediated mononuclear phagocyte crosstalk protects mice from Citrobacter rodentium-induced colon immunopathology.

2014

Gut homeostasis and mucosal immune defense rely on the differential contributions of dendritic cells (DC) and macrophages. Here we show that colonic CX3CR1+ mononuclear phagocytes are critical inducers of the innate response to Citrobacter rodentium infection. Specifically, the absence of IL-23 expression in macrophages or CD11b+ DC results in the impairment of IL-22 production and in acute lethality. Highlighting immunopathology as a death cause, infected animals are rescued by the neutralization of IL-12 or IFNγ. Moreover, mice are also protected when the CD103+ CD11b− DC compartment is rendered deficient for IL-12 production. We show that IL-12 production by colonic CD103+ CD11b− DC is r…

ChemokineColonCX3C Chemokine Receptor 1General Physics and Astronomychemical and pharmacologic phenomenaMice TransgenicInterleukin-23General Biochemistry Genetics and Molecular BiologyMonocytesArticleMicrobiologyInterferon-gammaMiceIntestinal mucosaAntigens CDImmunopathologyCitrobacter rodentiummedicineAnimalsHomeostasisInterferon gammaIntestinal MucosaImmunity MucosalMultidisciplinaryCD11b AntigenbiologyInterleukinsMacrophagesEnterobacteriaceae InfectionsGeneral ChemistryMononuclear phagocyte systemDendritic CellsInterleukin-12Survival AnalysisImmunity InnateIntegrin alpha MGene Expression RegulationImmunologyInterleukin 12biology.proteinCitrobacter rodentiumTh17 CellsReceptors ChemokineIntegrin alpha Chainsmedicine.drugSignal TransductionNature communications
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Dermal dendritic cells, but not Langerhans cells, are critical in murine single epicutaneous sensitization

2014

A murine repeated protein-patch model has been established to study epicutaneous sensitization in atopic dermatitis. This model has shown a predominant Th2 and a weak Th1 response in both BALB/c and C57BL/6 mice. However, Th responses induced in the repeated model are not consistent with the generally accepted theory that BALB/c and C57BL/6 mice are Th2 and Th1 prone and are representatives of human atopy and non-atopy, respectively. In this study, a single protein-patch model was established, which showed in addition to the Th2 response, a remarkable Th1 response in C57BL/6 mice, but not in BALB/c mice. Moreover, using muLangerin-DTR mice, we demonstrated that dermal dendritic cells, but n…

Dermal Dendritic CellsTh2 responseDermatologyBiochemistryDermatitis AtopicAtopyMiceTh2 CellsAntigens CDCell MovementmedicineAnimalsHumansEpicutaneous sensitizationMolecular BiologyCells CulturedSkinMice Inbred BALB Cbusiness.industryDendritic CellsAtopic dermatitisAllergensTh1 Cellsmedicine.diseaseMice Inbred C57BLLangerhans CellsImmunologyCytokinesTh1 responsebusinessIntegrin alpha ChainsExperimental Dermatology
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The Fibril-associated Collagen IX Provides a Novel Mechanism for Cell Adhesion to Cartilaginous Matrix

2004

Collagen IX is the prototype fibril-associated collagen with interruptions in triple helix. In human cartilage it covers collagen fibrils, but its putative cellular receptors have been unknown. The reverse transcription-PCR analysis of human fetal tissues suggested that based on their distribution all four collagen receptor integrins, namely alpha1beta1, alpha2beta1, alpha10beta1, and alpha11beta1, are possible receptors for collagen IX. Furthermore primary chondrocytes and chondrosarcoma cells express the four integrins simultaneously. Chondrosarcoma cells, as well as Chinese hamster ovary cells transfected to express alpha1beta1, alpha2beta1, or alpha10beta1 integrin as their only collage…

Integrin alpha1Integrin alpha2LigandsPolymerase Chain ReactionBiochemistryCollagen receptorMiceCricetinaeReceptorbiologyReverse Transcriptase Polymerase Chain ReactionChemistryChinese hamster ovary cellRecombinant ProteinsCell biologyBiochemistryCollagenIntegrin alpha ChainsProtein BindingMolecular Sequence DataIntegrinChondrosarcomaCHO CellsFibrilCollagen Type IXCell LineChondrocytesMicroscopy Electron TransmissionCell Line TumorCell AdhesionEscherichia coliAnimalsHumansImmunoprecipitationAmino Acid SequenceRNA MessengerBinding siteCell adhesionMolecular BiologyBinding SitesSequence Homology Amino AcidCell BiologyProtein Structure TertiaryRatsMicroscopy ElectronCollagen type I alpha 1CartilageMutationMutagenesis Site-Directedbiology.proteinRNAPeptidesJournal of Biological Chemistry
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Negative regulators of integrin activity

2012

Integrins are heterodimeric transmembrane adhesion receptors composed of α- and β-subunits. They are ubiquitously expressed and have key roles in a number of important biological processes, such as development, maintenance of tissue homeostasis and immunological responses. The activity of integrins, which indicates their affinity towards their ligands, is tightly regulated such that signals inside the cell cruicially regulate the switching between active and inactive states. An impaired ability to activate integrins is associated with many human diseases, including bleeding disorders and immune deficiencies, whereas inappropriate integrin activation has been linked to inflammatory disorders…

IntegrinsIntegrin beta ChainsintegrinMolecular Sequence DataIntegrinCellActivationSHARPINta3111Collagen receptorMice03 medical and health sciences0302 clinical medicineImmune systemSDG 3 - Good Health and Well-beingCell AdhesionmedicineAnimalsHumansendocytosisAmino Acid SequenceTissue homeostasis030304 developmental biology0303 health sciencesbiologytalinta1182Cell BiologyTransmembrane proteinCell biologyadhesionmedicine.anatomical_structureIntegrin alpha Mbiology.protein/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingIntegrin beta 6Integrin alpha Chains030217 neurology & neurosurgerySignal TransductionJ Cell Sci
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Tenectin is a novel alphaPS2betaPS integrin ligand required for wing morphogenesis and male genital looping in Drosophila.

2010

International audience; Morphogenesis of the adult structures of holometabolous insects is regulated by ecdysteroids and juvenile hormones and involves cell-cell interactions mediated in part by the cell surface integrin receptors and their extracellular matrix (ECM) ligands. These adhesion molecules and their regulation by hormones are not well characterized. We describe the gene structure of a newly described ECM molecule, tenectin, and demonstrate that it is a hormonally regulated ECM protein required for proper morphogenesis of the adult wing and male genitalia. Tenectin's function as a new ligand of the PS2 integrins is demonstrated by both genetic interactions in the fly and by cell s…

MaleMESH: Extracellular Matrix ProteinsMESH: DrosophilaMESH : Immunohistochemistry[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionIntegrinLigandsLooping morphogenesisExtracellular matrixchemistry.chemical_compound0302 clinical medicineMESH: Genitalia MaleMorphogenesisMESH: LigandsDrosophila ProteinsWings AnimalMESH: AnimalsTransgenesIn Situ Hybridization0303 health sciencesExtracellular Matrix ProteinsMESH : Genitalia MaleMESH : LigandsIntegrin alpha ChainsCell adhesion moleculeMESH : In Situ HybridizationImmunohistochemistry3. Good healthCell biologyLarvaMESH : Integrin alpha ChainsAdhesionDrosophilaMESH : MutationMESH : TransgenesTenectinIntegrin alpha ChainsDrosophila ProteinEcdysoneEcdysoneMESH: MutationMESH: Drosophila ProteinsMESH : MaleIntegrinMorphogenesisMESH : WingMESH: TransgenesBiologyGenitalia MaleArticle03 medical and health sciencesMESH : Extracellular Matrix ProteinsMESH: In Situ HybridizationAnimalsMESH : DrosophilaCell adhesionMolecular Biology030304 developmental biologyMESH : LarvaMetamorphosisMESH: Integrin alpha ChainsLeft–right asymmetryMESH: ImmunohistochemistryCell BiologyMESH : Drosophila ProteinsMESH: WingMESH: MaleMESH: MorphogenesischemistryMESH : MorphogenesisMutationbiology.proteinMESH : AnimalsMESH: Larva[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition030217 neurology & neurosurgeryDevelopmental Biology
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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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