Search results for " Glycoproteins"

showing 10 items of 329 documents

Kininogen binding protein p33/gC1qR is localized in the vesicular fraction of endothelial cells

1996

AbstractThe endothelial protein p33/gC1qR is thought to mediate the assembly of components of the kinin-forming and complement-activating pathways on the surface of cardiovascular cells. FACS analysis of intact human umbilical vein endothelial cells using specific antibodies to p33 revealed a minor fluorescence on the cell surface whereas permeabilized cells showed a bright fluorescence indicative of an intracellular localization of p33. Immunostaining of fixed cells confirmed the predominant intracellular localization of p33. Fractionation studies demonstrated that the vesicular but not the membrane fraction of EA.hy926 cells is rich in p33. We conclude that externalization of p33 must pre…

Kininogen bindingp33Kininogen binding proteinCellBiophysicsComplementFluorescent Antibody TechniqueBiologyBiochemistryUmbilical veinMitochondrial ProteinsStructural BiologyGeneticsmedicineHumansMolecular BiologyCells CulturedMembrane GlycoproteinsImmune SeraCell BiologyKininFlow CytometryKininFluorescenceReceptors ComplementCell biologyEndothelial stem cellSpecific antibodyHyaluronan Receptorsmedicine.anatomical_structuregC1qREndothelium VascularCarrier ProteinsImmunostainingFEBS Letters
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Langerinneg conventional dendritic cells produce IL-23 to drive psoriatic plaque formation in mice.

2013

Psoriasis is an autoinflammatory skin disease of unknown etiology. Topical application of Aldara cream containing the Toll-like receptor (TLR)7 agonist Imiquimod (IMQ) onto patients induces flares of psoriasis. Likewise, in mice IMQ triggers pathological changes closely resembling psoriatic plaque formation. Key cytokines like IL-23 and type-I IFN (IFN-I), both being produced mainly by dendritic cells (DCs), have been implicated in psoriasis. Although plasmacytoid DCs (pDCs) are the main source of IFNα and thought to initiate disease, conventional DCs (cDCs) appear to maintain the psoriatic lesions. Any role of cDCs during lesion formation remains elusive. Here, we report that selective ac…

LangerinCD11c610 Medicine & healthInflammation10263 Institute of Experimental ImmunologyInterleukin-23Mice03 medical and health sciences0302 clinical medicinePsoriasismedicineInterleukin 23AnimalsPsoriasisLectins C-Type030304 developmental biologyMice Knockout1000 Multidisciplinary0303 health sciencesImiquimodMembrane GlycoproteinsMultidisciplinarybiologyintegumentary systemhemic and immune systemsDendritic cellTLR7Biological SciencesAcquired immune systemmedicine.disease3. Good healthDisease Models AnimalMannose-Binding LectinsToll-Like Receptor 7Langerhans Cells030220 oncology & carcinogenesisAntigens SurfaceMyeloid Differentiation Factor 88ImmunologyAminoquinolinesbiology.protein570 Life sciences; biologymedicine.symptom
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Interaction of TLR2 and TLR4 ligands with the N-terminal domain of Gp96 amplifies innate and adaptive immune responses.

2006

Activation of dendritic cells by ligands for Toll-like receptors (TLR) is a crucial event in the initiation of innate and adaptive immune responses. Several classes of TLR ligands have been identified that interact with distinct members of the TLR-family. TLR4 ligands include lipopolysaccharide derived from different Gram-negative bacteria and viral proteins. Recent reports have demonstrated the TLR-mediated activation of dendritic cells by heat shock proteins (HSPs). However, doubts were raised as to what extent this effect was due to lipopolysaccharide contaminations of the HSP preparations. We re-examined this phenomenon using Gp96 or its N-terminal domain, nominally endotoxin-free (0.5 …

LipopolysaccharidesLipopolysaccharideBiologyCD8-Positive T-LymphocytesBiochemistrychemistry.chemical_compoundMiceImmune systemDogsHeat shock proteinAnimalsHumansReceptorMolecular BiologyInflammationMice Inbred BALB CInnate immune systemMembrane GlycoproteinsCCL18Cell BiologyToll-Like Receptor 2Cell biologyEndotoxinsMice Inbred C57BLToll-Like Receptor 4TLR2BiochemistrychemistryTLR4The Journal of biological chemistry
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Regulation of T cells in asthma: implications for genetic manipulation

2004

PURPOSE OF THE REVIEW Allergic asthma is a disease characterized by airway hyperresponsiveness, inflammation and remodeling. In the past few decades it has become clear that the pathogenesis and development of this disease is controlled by cytokines released by CD4 T helper type 2 lymphocytes that develop under the influence of natural killer lymphocytes. At birth, T cell priming exhibits a T helper type 2 bias and the development of the T helper phenotype is determined in the first year of life by environmental exposure to virus or bacterial substances or environmental allergens in genetically predisposed individuals. Decreased exposure to infection in early childhood has thus been linked …

LipopolysaccharidesT-LymphocytesT cellImmunologyPriming (immunology)Receptors Cell SurfaceInflammationBiologyType 2 immune responseImmune systemAntigenHygiene hypothesismedicineHumansImmunology and AllergyGeneticsMembrane GlycoproteinsToll-Like ReceptorsT-Lymphocytes Helper-InducerEnvironmental exposureAsthmamedicine.anatomical_structureImmunologyCytokinesmedicine.symptomT-Box Domain ProteinsTranscription FactorsCurrent Opinion in Allergy and Clinical Immunology
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IL-10 down-regulates T cell activation by antigen-presenting liver sinusoidal endothelial cells through decreased antigen uptake via the mannose rece…

1998

SUMMARYOur study demonstrates that antigen-presenting liver sinusoidal endothelial cells (LSEC) induce production of interferon-gamma (IFN-γ) from cloned Th1 CD4+ T cells. We show that LSEC used the mannose receptor for antigen uptake, which further strengthened the role of LSEC as antigen-presenting cell (APC) population in the liver. The ability of LSEC to activate cloned CD4+ T cells antigen-specifically was down-regulated by exogenous prostaglandin E2 (PGE2) and by IL-10. We identify two separate mechanisms by which IL-10 down-regulated T cell activation through LSEC. IL-10 decreased the constitutive surface expression of MHC class II as well as of the accessory molecules CD80 and CD86 …

Liver cytologyT cellT-LymphocytesImmunologyAntigen presentationAntigen-Presenting CellsDown-RegulationReceptors Cell SurfaceBiologyLymphocyte ActivationDinoprostoneMiceAntigenAntigens CDmedicineImmunology and AllergyAnimalsLectins C-TypeCD86Antigen PresentationMice Inbred BALB CMembrane GlycoproteinsHistocompatibility Antigens Class IIOriginal ArticlesInterleukin-10Interleukin 10medicine.anatomical_structureMannose-Binding LectinsLiverImmunologyB7-1 AntigenCytokinesFemaleB7-2 AntigenEndothelium VascularMannoseCD80Mannose receptorMannose ReceptorClinical and experimental immunology
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Gp91phox-containing NAD(P)H oxidase increases superoxide formation by doxorubicin and NADPH

2006

Doxorubicin is a highly effective antineoplastic drug associated with a dose-dependent cardiotoxicity that may result in irreversible cardiomyopathy and heart failure. Gene variants of the superoxide-generating enzyme NAD(P)H oxidase have recently been associated with this phenotype. We investigated the mechanism of this association using lucigenin-enhanced chemiluminescence, spectrophotometry, electrochemical sensor, and electron paramagnetic resonance spectroscopy. Superoxide production was measured in female wild-type and NAD(P)H oxidase-deficient (gp91phox knockout) mice. The magnitude of the increase in superoxide production on the addition of doxorubicin was much higher in hearts of w…

LuminescenceGene ExpressionAntineoplastic AgentsPolymerase Chain ReactionBiochemistryMicechemistry.chemical_compoundSuperoxidesPhysiology (medical)medicineAnimalsDoxorubicinNADPH-Ferrihemoprotein ReductaseMice Knockoutchemistry.chemical_classificationCardiotoxicityOxidase testMembrane GlycoproteinsDose-Response Relationship DrugSuperoxideMyocardiumNADPH OxidasesMolecular biologyMice Inbred C57BLEnzymechemistryBiochemistryDoxorubicinNAD(P)H oxidaseNADPH Oxidase 2Knockout mouseNAD+ kinaseNADPmedicine.drugFree Radical Biology and Medicine
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Random, asynchronous, and asymmetric transcriptional activity of enhancer-flanking major immediate-early genes ie1/3 and ie2 during murine cytomegalo…

2001

ABSTRACT The lungs are a major organ site of cytomegalovirus (CMV) pathogenesis, latency, and recurrence. Previous work on murine CMV latency has documented a high load and an even distribution of viral genomes in the lungs after the resolution of productive infection. Initiation of the productive cycle requires expression of the ie1/3 transcription unit, which is driven by the immediate-early (IE) promoter P 1/3 and generates IE1 and IE3 transcripts by differential splicing. Latency is molecularly defined by the absence of IE3 transcripts specifying the essential transactivator protein IE3. In contrast, IE1 transcripts were found to be generated focally and randomly, reflecting sporadic P …

Lung DiseasesMuromegalovirusTranscription GeneticvirusesImmunologyReplicationEnhancer RNAsBiologyMicrobiologyImmediate early proteinImmediate-Early ProteinsTransactivationMiceViral ProteinsViral Envelope ProteinsTranscription (biology)VirologyVirus latencymedicineAnimalsEnhancerTranscription factorGenes Immediate-EarlyLungGeneticsMice Inbred BALB CMembrane Glycoproteinsvirus diseasesHerpesviridae Infectionsmedicine.diseaseUpstream EnhancerVirus LatencyEnhancer Elements GeneticInsect ScienceTrans-ActivatorsFemaleJournal of virology
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Targeted Repolarization of Tumor‐Associated Macrophages via Imidazoquinoline‐Linked Nanobodies

2021

Abstract Tumor‐associated macrophages (TAMs) promote the immune suppressive microenvironment inside tumors and are, therefore, considered as a promising target for the next generation of cancer immunotherapies. To repolarize their phenotype into a tumoricidal state, the Toll‐like receptor 7/8 agonist imidazoquinoline IMDQ is site‐specifically and quantitatively coupled to single chain antibody fragments, so‐called nanobodies, targeting the macrophage mannose receptor (MMR) on TAMs. Intravenous injection of these conjugates result in a tumor‐ and cell‐specific delivery of IMDQ into MMRhigh TAMs, causing a significant decline in tumor growth. This is accompanied by a repolarization of TAMs to…

Lung NeoplasmsGeneral Chemical Engineeringmedicine.medical_treatmentGeneral Physics and AstronomyMedicine (miscellaneous)TLR 7/8 agonist02 engineering and technology01 natural scienceschemistry.chemical_compoundCancer immunotherapyTumor-Associated MacrophagesTumor MicroenvironmentMacrophageM2 macrophagesGeneral Materials ScienceReceptorResearch ArticlesMice KnockoutMembrane GlycoproteinsChemistrytumor associated macrophagesQGeneral EngineeringImidazoles021001 nanoscience & nanotechnologynanobodiesmedicine.anatomical_structureDrug deliveryQuinolines0210 nano-technologyMannose ReceptorResearch ArticleT cellScience010402 general chemistryBiochemistry Genetics and Molecular Biology (miscellaneous)Immune systemmedicineAnimalsrepolarizationcancer immunotherapyCancerSingle-Domain Antibodiesmedicine.disease0104 chemical sciencesImidazoquinolineMice Inbred C57BLDisease Models AnimalToll-Like Receptor 6Toll-Like Receptor 7drug deliveryCancer research
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Measles virus enhances the expression of cellular immediate-early genes and DNA-binding of transcription factor AP-1 in lung epithelial A549 cells.

2002

In this work we investigated the effect of measles virus (MV) infection on the expression of immediate-early genes junB, c-jun and c-fos mRNA as well as AP-1 DNA-binding activity in the lung epithelial-like adenocarcinoma cell line A549. The transcription factor AP-1, which is a group of dimeric complexes of the Fos and Jun family proteins, is an important regulator in many cellular responses to different extracellular stimuli. Membrane cofactor protein CD46, which acts as a receptor for laboratory-adapted and vaccine strains of MV, has been reported to associate with beta1 integrin molecules, which are known to trigger signaling events and activate immediate-early genes. The expression of …

Lung NeoplasmsJUNBBiologyMeasles virusMembrane Cofactor Protein03 medical and health sciencesAntigens CDVirologyGene expressionTumor Cells CulturedHumansMononegaviralesTranscription factorGenes Immediate-Early030304 developmental biologyA549 cell0303 health sciencesMembrane GlycoproteinsCD46Interleukin-6030302 biochemistry & molecular biologyGeneral MedicineDNAbiology.organism_classificationVirology3. Good healthTranscription Factor AP-1Gene Expression RegulationMeasles virusImmediate early geneArchives of virology
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Down-regulation of human CYP3A4 by the inflammatory signal interleukin-6: molecular mechanism and transcription factors involved.

2002

The hepatic drug-metabolizing cytochrome P-450 (CYP) enzymes are down-regulated during inflammation. In vitro studies with hepatocytes have shown that the cytokines released during inflammatory responses are largely responsible for this CYP repression. However, the signaling pathways and the cytokine-activated factors involved remain to be properly identified. Our research has focused on the negative regulation of CYP3A4 (the major drug-metabolizing human CYP) by interleukin 6 (IL-6) (the principal regulator of the hepatic acute-phase response). CYP3A4 down-regulation by IL-6 requires activation of the glycoprotein receptor gp130; however, it does not proceed through the JAK/STAT pathway, a…

MAPK/ERK pathwaySTAT3 Transcription FactorMAP Kinase Signaling Systemp38 mitogen-activated protein kinasesDown-RegulationBiologyBiochemistryTransactivationCytochrome P-450 Enzyme SystemAntigens CDGeneticsCCAAT-Enhancer-Binding Protein-alphaCytokine Receptor gp130Tumor Cells CulturedCytochrome P-450 CYP3AHumansRNA MessengerSTAT3Molecular BiologyTranscription factorCells CulturedMembrane GlycoproteinsDose-Response Relationship DrugInterleukin-6Reverse Transcriptase Polymerase Chain ReactionCCAAT-Enhancer-Binding Protein-betaJAK-STAT signaling pathwayProtein-Tyrosine KinasesGlycoprotein 130Molecular biologyDNA-Binding ProteinsGene Expression Regulationbiology.proteinHepatocytesTrans-ActivatorsSignal transductionBiotechnologyAcute-Phase ProteinsSignal TransductionTranscription FactorsFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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