Search results for "collage"

showing 10 items of 638 documents

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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Integrin alpha(2)I domain recognizes type I and type IV collagens by different mechanisms.

2000

The collagens are recognized by the alphaI domains of the collagen receptor integrins. A common structural feature in the collagen-binding alphaI domains is the presence of an extra helix, named helix alphaC. However, its participation in collagen binding has not been shown. Here, we have deleted the helix alphaC in the alpha(2)I domain and tested the function of the resultant recombinant protein (DeltaalphaCalpha(2)I) by using a real-time biosensor. The DeltaalphaCalpha(2)I domain had reduced affinity for type I collagen (430 +/- 90 nM) when compared with wild-type alpha(2)I domain (90 +/- 30 nM), indicating both the importance of helix alphaC in type I collagen binding and that the collag…

IntegrinsIntegrinIntegrin alpha2CHO CellsBiochemistryCollagen receptorType IV collagenIntegrin alpha2Antigens CDCricetinaeAnimalsBinding siteMolecular BiologyBinding SitesbiologyChemistryChinese hamster ovary cellCell BiologyMolecular biologyRecombinant ProteinsCollagen type I alpha 1biology.proteinMutagenesis Site-DirectedCollagenType I collagenProtein BindingThe Journal of biological chemistry
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Cholesterol Dependence of Collagen and Echovirus 1 Trafficking along the Novel α2β1 Integrin Internalization Pathway

2013

We have previously shown that soluble collagen and a human pathogen, echovirus 1 (EV1) cluster α2β1 integrin on the plasma membrane and cause their internalization into cytoplasmic endosomes. Here we show that cholesterol plays a major role not only in the uptake of α2β1 integrin and its ligands but also in the formation of α2 integrin-specific multivesicular bodies (α2-MVBs) and virus infection. EV1 infection and α2β1 integrin internalization were totally halted by low amounts of the cholesterol-aggregating drugs filipin or nystatin. Inhibition of cholesterol synthesis and accumulation of lanosterol after ketoconazole treatment inhibited uptake of collagen, virus and clustered integrin, an…

IntegrinsNystatinFluorescent Antibody TechniqueBiochemistryCollagen receptorchemistry.chemical_compoundBINDINGMolecular Cell BiologyInternalizationLipid raftREQUIRESmedia_common0303 health sciencesMicroscopy ConfocalMultidisciplinarybiologyQRIMMUNODEFICIENCY-VIRUS TYPE-1RNA REPLICATIONCellular StructuresExtracellular MatrixEnterovirus B Human3. Good healthCell biologyProtein TransportCholesterolENTRYCytochemistryMedicineMembranes and Sortinglipids (amino acids peptides and proteins)CollagenIntegrin alpha2beta1Research ArticleSignal TransductionViral EntryEndosomeSciencemedia_common.quotation_subjecteducationIntegrinLOW-DENSITY-LIPOPROTEINMicrobiologyFilipinClathrinGPI-ANCHORED PROTEINS03 medical and health sciencesVirologyCell Line TumorCell AdhesionHumansFilipinBiology030304 developmental biology030306 microbiologyCell MembraneVirus Uncoatingta1182TRANSPORTLIPID RAFTSMicroscopy ElectronSubcellular Organelleschemistrybiology.protein3111 BiomedicineChromatography Thin LayerCELL-MEMBRANESViral Transmission and InfectionPLoS ONE
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The Selective Regulation of αVβ1 Integrin Expression Is Based on the Hierarchical Formation of αV-containing Heterodimers

2002

The integrin beta1 subunit can form a heterodimer with 12 different alpha subunits. According to the present model, the expression level of any alphabeta complex is regulated by the availability of the specific alpha subunit, whereas beta1 subunit is constantly present in a large excess. The expression of several heterodimers containing the alphaV subunit seems to be regulated by an identical mechanism. The fact that many cells express alphaVbeta1 heterodimer, and that this fibronectin/vitronectin receptor may be selectively regulated, compromises the present model of the regulation of beta1 and alphaV integrins. We have tried to solve this problem by assuming that distinct alphabeta hetero…

IntegrinsProtein subunitCellIntegrinBiologyModels BiologicalBiochemistryAntigens CDComplementary DNATumor Cells CulturedmedicineHumansReceptors VitronectinMelanomaMolecular BiologyCell MembraneCell BiologyTransfectionIntegrin alphaVFibronectinsCell biologyGene Expression Regulation NeoplasticFibronectinmedicine.anatomical_structurebiology.proteinVitronectinCollagenDimerizationIntracellularProtein BindingJournal of Biological Chemistry
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Internalization of Echovirus 1 in Caveolae

2002

ABSTRACT Echovirus 1 (EV1) is a human pathogen which belongs to the Picornaviridae family of RNA viruses. We have analyzed the early events of infection after EV1 binding to its receptor α2β1 integrin and elucidated the route by which EV1 gains access to the host cell. EV1 binding onto the cell surface and subsequent entry resulted in conformational changes of the viral capsid as demonstrated by sucrose gradient sedimentation analysis. After 15 min to 2 h postinfection (p.i.) EV1 capsid proteins were seen in vesicular structures that were negative for markers of the clathrin-dependent endocytic pathway. In contrast, immunofluorescence confocal microscopy showed that EV1, α2β1 integrin, and …

IntegrinsReceptors CollagenEchovirusmedia_common.quotation_subjectCaveolin 1ImmunologyIntegrinCaveolaemedicine.disease_causeCaveolinsMicrobiologyClathrin03 medical and health sciencesCapsidVirologyCaveolaeCaveolinEnterovirus InfectionsTumor Cells CulturedmedicineAnimalsHumansInternalization030304 developmental biologymedia_common0303 health sciencesMicroscopy Confocalbiology030302 biochemistry & molecular biologyMolecular biologyClathrinEnterovirus B HumanVirus-Cell InteractionsCell biologyMicroscopy ElectronViral replicationInsect ScienceCaveolin 1biology.proteinRabbitsbeta 2-MicroglobulinJournal of Virology
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Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2A and dephosphorylation of Akt and glycogen synthase kinase 3 beta.

2002

The integrins are a large family of heterodimeric transmembrane receptors composed of α and β subunits (22). In addition to mediating cell-matrix interactions, integrins have been shown to activate intracellular signaling pathways which, in collaboration with growth factor-induced signals, regulate cellular functions (46). Some integrin signaling cascades are activated via the β subunit cytoplasmic domain, and they are therefore triggered by several integrin heterodimers. These signals include the activation of protein tyrosine kinases of the Src and focal adhesion kinase (FAK) families (9, 47). More-recent studies have revealed signaling events that are activated specifically by an α subun…

IntegrinsReceptors CollagenIntegrinProtein Serine-Threonine KinasesCD49cp38 Mitogen-Activated Protein KinasesCollagen receptorGlycogen Synthase Kinase 3Proto-Oncogene ProteinsCell AdhesionPhosphoprotein PhosphatasesHumansIntegrin-linked kinaseProtein Phosphatase 2cdc42 GTP-Binding ProteinMolecular BiologyCell Growth and DevelopmentCells CulturedbiologyAkt/PKB signaling pathwayCell adhesion moleculeGlycogen Synthase KinasesCell BiologyCell biologyEnzyme ActivationBiochemistryIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6CollagenMitogen-Activated Protein KinasesProto-Oncogene Proteins c-aktProtein BindingSignal TransductionMolecular and cellular biology
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The collagen receptor subfamily of the integrins

2003

The four collagen receptor integrins, alpha1beta1, alpha2beta1, alpha10beta1 and alpha11beta1, form a structurally and functionally distinct subgroup when compared to other members of the integrin family. In this review, we discuss the structures of these receptors and their differences in collagen binding and signalling function.

IntegrinsReceptors CollagenSubfamilybiologyChemistryIntegrinCell BiologyPlasma protein bindingLigandsBiochemistryProtein Structure TertiaryCollagen receptorCell biologyIntegrin alpha Mbiology.proteinAnimalsHumansSignal transductionReceptorFunction (biology)Protein BindingSignal TransductionThe International Journal of Biochemistry & Cell Biology
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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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Endomicroscopy of Colon Pathology

2007

Colorectal cancer is still one of the leading causes of cancer-related death in the Western world. Screening colonoscopy is widely accepted as the gold standard for early diagnosis of cancer. The prognosis for patients with colonic neoplasms is strictly dependent on the depth of infiltration and therefore depends on early detection of pre-invasive and neoplastic changes. Early detection makes it possible to cure the patient by means of immediate endoscopic resection.

Intraepithelial neoplasiamedicine.medical_specialtyCollagenous colitisbusiness.industryColorectal cancerEarly detectionScreening colonoscopymedicine.diseaseUlcerative colitisMicroscopic colitismedicineEndomicroscopyRadiologybusiness
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