Search results for "Receptor for Advanced Glycation End Products"

showing 10 items of 10 documents

Genome-wide association study identifies five loci associated with lung function

2009

Pulmonary function measures are heritable traits that predict morbidity and mortality and define chronic obstructive pulmonary disease (COPD). We tested genome-wide association with forced expiratory volume in 1 s (FEV(1)) and the ratio of FEV(1) to forced vital capacity (FVC) in the SpiroMeta consortium (n = 20,288 individuals of European ancestry). We conducted a meta-analysis of top signals with data from direct genotyping (n < or = 32,184 additional individuals) and in silico summary association data from the CHARGE Consortium (n = 21,209) and the Health 2000 survey (n < or = 883). We confirmed the reported locus at 4q31 and identified associations with FEV(1) or FEV(1)/FVC and co…

OncologySpirometryMalemedicine.medical_specialtyVital capacityPopulationReceptor for Advanced Glycation End ProductsVital CapacityGenome-wide association studyBiologyPolymorphism Single NucleotideArticlePulmonary function testing03 medical and health sciencesFEV1/FVC ratioPulmonary Disease Chronic Obstructive0302 clinical medicineMeta-Analysis as TopicInternal medicineTensinsForced Expiratory VolumeGeneticsmedicineHumansRNA MessengerReceptors ImmunologiceducationLung030304 developmental biologyGlutathione Transferase0303 health scienceseducation.field_of_studyCOPDmedicine.diagnostic_testGenome HumanGene Expression ProfilingMicrofilament Proteinsrespiratory systemmedicine.disease3. Good healthRespiratory Function Tests030228 respiratory systemSpirometryImmunologyFemaleReceptors Serotonin 5-HT4Hedgehog interacting proteinThrombospondinsGenome-Wide Association Study
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The sodium-glucose co-transporter 2 inhibitor empagliflozin improves diabetes-induced vascular dysfunction in the streptozotocin diabetes rat model b…

2014

Objective In diabetes, vascular dysfunction is characterized by impaired endothelial function due to increased oxidative stress. Empagliflozin, as a selective sodium-glucose co-transporter 2 inhibitor (SGLT2i), offers a novel approach for the treatment of type 2 diabetes by enhancing urinary glucose excretion. The aim of the present study was to test whether treatment with empagliflozin improves endothelial dysfunction in type I diabetic rats via reduction of glucotoxicity and associated vascular oxidative stress. Methods Type I diabetes in Wistar rats was induced by an intravenous injection of streptozotocin (60 mg/kg). One week after injection empagliflozin (10 and 30 mg/kg/d) was adminis…

Blood GlucoseMalemedicine.medical_treatmentReceptor for Advanced Glycation End Productslcsh:MedicineGene ExpressionType 2 diabetesmedicine.disease_causeVascular MedicineGlucosidesMedicine and Health SciencesMedicineInsulinEndothelial dysfunctionReceptors Immunologiclcsh:ScienceMultidisciplinaryType 1 DiabetesCytokinesInflammation Mediatorsmedicine.drugSignal TransductionResearch Articlemedicine.medical_specialtyCardiologyBlood sugarStreptozocinCardiovascular PharmacologyDiabetes Mellitus ExperimentalDiabetes ComplicationsInternal medicineDiabetes mellitusEmpagliflozinDiabetes MellitusAnimalsRNA MessengerVascular DiseasesBenzhydryl CompoundsSodium-Glucose Transporter 2 InhibitorsPharmacologybusiness.industryInsulinlcsh:RHemodynamicsStreptozotocinmedicine.diseaseRatsOxidative StressEndocrinologyGlucoseMetabolic Disorderslcsh:QbusinessOxidative stressDiabetic AngiopathiesPloS one
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Posttranslationally modified proteins as mediators of sustained intestinal inflammation.

2006

Oxidative and carbonyl stress leads to generation of N(epsilon)-carboxymethyllysine-modified proteins (CML-mps), which are known to bind the receptor for advanced glycation end products (RAGE) and induce nuclear factor (NF)-kappaB-dependent proinflammatory gene expression. To determine the impact of CML-mps in vivo, RAGE-dependent sustained NF-kappaB activation was studied in resection gut specimens from patients with inflammatory bowel disease. Inflamed gut biopsy tissue demonstrated a significant up-regulation of RAGE and increased NF-kappaB activation. Protein extracts from the inflamed zones, but not from noninflamed resection borders, caused perpetuated NF-kappaB activation in cultured…

AdultCell ExtractsMaleReceptor for Advanced Glycation End ProductsInflammationBiologyInflammatory bowel diseasep38 Mitogen-Activated Protein KinasesPathology and Forensic MedicineProinflammatory cytokineRAGE (receptor)MiceGlycationhemic and lymphatic diseasesGene expressionmedicineAnimalsCalgranulin BHumansCalgranulin AIntestinal MucosaReceptors ImmunologicReceptorProtein Kinase InhibitorsMice KnockoutMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3LysineNF-kappa Bnutritional and metabolic diseasesEndothelial Cellsmedicine.diseaseNFKB1Inflammatory Bowel DiseasesIntestinesDisease Models AnimalImmunologyCancer researchFemalemedicine.symptomProtein Processing Post-TranslationalRegular ArticlesThe American journal of pathology
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Effects of glycation of the model food allergen ovalbumin on antigen uptake and presentation by human dendritic cells.

2010

Advanced glycation endproducts (AGEs) of food proteins resulting from the Maillard reaction after cooking or heating may have particular importance in food allergy. The underlying immunological mechanisms are only poorly understood. The aim of the study was to examine the effects of AGE derived from the model food allergen ovalbumin (AGE-OVA) on dendritic cells (DCs), their immunostimulatory capacity and the T-cell response compared with regular OVA. For this purpose, human immature DCs were exposed to fluorescein isothiocyanate (FITC)-labelled AGE-OVA and FITC-labelled regular OVA and uptake was analysed by flow cytometry and fluorescence microscopy. Furthermore, autologous CD4(+) T-cell p…

CD4-Positive T-LymphocytesGlycation End Products AdvancedOvalbuminmedicine.medical_treatmentImmunologyReceptor for Advanced Glycation End ProductsLymphocyte ActivationAntibodiesRAGE (receptor)chemistry.chemical_compoundTh2 CellsAntigenGlycationmedicineImmunology and AllergyHumansScavenger receptorPhosphorylationReceptors ImmunologicFluorescein isothiocyanateCell ProliferationAntigen PresentationbiologyInterleukin-6Transcription Factor RelADendritic CellsOriginal Articlesrespiratory systemAllergensTh1 CellsEndocytosisCell biologyOvalbuminCytokinechemistryImmunologybiology.proteinCytokinesMannose receptorFood HypersensitivityImmunology
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Regulated Proteolysis of RAGE and AβPP as Possible Link Between Type 2 Diabetes Mellitus and Alzheimer's Disease

2009

Epidemiological studies have linked type 2 diabetes mellitus (T2DM) with an increased risk of developing Alzheimer's disease (AD). In T2DM, the elevated blood glucose level promotes formation of advanced glycation end products (AGEs). The receptor for AGEs (RAGE) is a type I membrane-protein and is also able to import amyloid-beta (Abeta) from the blood across the blood-brain-barrier into the brain. Oligomeric Abeta peptides disturb synaptic function in the brain and are believed to contribute to the development of AD. Abeta peptides are released from the amyloid-beta protein precursor (AbetaPP) after sequential proteolysis by beta- and gamma-secretases but alpha-secretase-mediated cleavage…

medicine.medical_specialtyendocrine system diseasesProteolysisReceptor for Advanced Glycation End ProductsAmyloid beta-Protein PrecursorAlzheimer DiseaseGlycationInternal medicinemental disordersmedicineAnimalsHumansReceptors ImmunologicProtein precursorProtein kinase AReceptorAmyloid beta-Peptidesmedicine.diagnostic_testChemistryGeneral Neurosciencenutritional and metabolic diseasesGeneral MedicinePsychiatry and Mental healthClinical PsychologyCholesterolEndocrinologyDiabetes Mellitus Type 2EctodomainPeptide transportAmyloid Precursor Protein SecretasesGeriatrics and GerontologySignal transductionJournal of Alzheimer's Disease
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Induction of RAGE Shedding by Activation of G Protein-Coupled Receptors

2011

The multiligand Receptor for Advanced Glycation End products (RAGE) is involved in various pathophysiological processes, including diabetic inflammatory conditions and Alzheimers disease. Full-length RAGE, a cell surface-located type I membrane protein, can proteolytically be converted by metalloproteinases ADAM10 and MMP9 into a soluble RAGE form. Moreover, administration of recombinant soluble RAGE suppresses activation of cell surface-located RAGE by trapping RAGE ligands. Therefore stimulation of RAGE shedding might have a therapeutic value regarding inflammatory diseases. We aimed to investigate whether RAGE shedding is inducible via ligand-induced activation of G protein-coupled recep…

MaleReceptors Vasopressinendocrine system diseasesReceptor for Advanced Glycation End Productslcsh:MedicineHydroxamic Acids570 Life sciencesRAGE (receptor)Adenylyl cyclaseADAM10 ProteinMicePhosphatidylinositol 3-Kinaseschemistry.chemical_compoundMolecular Cell BiologyNeurobiology of Disease and RegenerationSignaling in Cellular ProcessesMembrane Receptor SignalingReceptors Immunologiclcsh:ScienceReceptorLungCellular Stress ResponsesCalcium signalingMultidisciplinaryKinaseDipeptidesHormone Receptor SignalingCell biologyMatrix Metalloproteinase 9NeurologyReceptors OxytocinGene Knockdown Techniquescardiovascular systemMatrix Metalloproteinase 2Pituitary Adenylate Cyclase-Activating PolypeptideMedicineRNA InterferenceAdenylyl CyclasesResearch ArticleSignal Transduction570 Biowissenschaftenmedicine.medical_specialtyMAP Kinase Signaling SystemADAM17 ProteinBiologyAlzheimer DiseaseCa2+/calmodulin-dependent protein kinaseInternal medicinemedicineAnimalsHumansProtease InhibitorsCalcium Signalingcardiovascular diseasesBiologyG protein-coupled receptorlcsh:RHEK 293 cellsMembrane Proteinsnutritional and metabolic diseasesCyclic AMP-Dependent Protein KinasesADAM ProteinsG-Protein SignalingHEK293 CellsEndocrinologychemistryProteolysisDementialcsh:QAmyloid Precursor Protein SecretasesMolecular Neurosciencehuman activitiesReceptors Pituitary Adenylate Cyclase-Activating Polypeptide Type INeurosciencePLoS ONE
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Receptor for advanced glycation end products is subjected to protein ectodomain shedding by metalloproteinases.

2008

The receptor for advanced glycation end products (RAGE) is a 55-kDa type I membrane glycoprotein of the immunoglobulin superfamily. Ligand-induced up-regulation of RAGE is involved in various pathophysiological processes, including late diabetic complications and Alzheimer disease. Application of recombinant soluble RAGE has been shown to block RAGE-mediated pathophysiological conditions. After expression of full-length RAGE in HEK cells we identified a 48-kDa soluble RAGE form (sRAGE) in the culture medium. This variant of RAGE is smaller than a 51-kDa soluble version derived from alternative splicing. The release of sRAGE can be induced by the phorbol ester PMA and the calcium ionophore c…

endocrine system diseasesADAM10Receptor for Advanced Glycation End ProductsMatrix Metalloproteinase InhibitorsHydroxamic AcidsBiochemistryProtein biotinylationCell LineDiabetes ComplicationsADAM10 ProteinGlycationAlzheimer DiseaseHumansProtein IsoformsProtease Inhibitorscardiovascular diseasesRNA Small InterferingReceptors ImmunologicReceptorMolecular BiologyProtein kinase CCalcimycinIonophoresChemistryHEK 293 cellsCell Membranenutritional and metabolic diseasesMembrane ProteinsCell BiologyProtein Structure TertiaryADAM ProteinsAlternative SplicingEctodomainBiochemistryMatrix Metalloproteinase 9cardiovascular systemCarcinogensImmunoglobulin superfamilyTetradecanoylphorbol AcetateAmyloid Precursor Protein Secretaseshuman activitiesThe Journal of biological chemistry
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Statins stimulate the production of a soluble form of the receptor for advanced glycation end products

2013

The beneficial effects of statin therapy in the reduction of cardiovascular pathogenesis, atherosclerosis, and diabetic complications are well known. The receptor for advanced glycation end products (RAGE) plays an important role in the progression of these diseases. In contrast, soluble forms of RAGE act as decoys for RAGE ligands and may prevent the development of RAGE-mediated disorders. Soluble forms of RAGE are either produced by alternative splicing [endogenous secretory RAGE (esRAGE)] or by proteolytic shedding mediated by metalloproteinases [shed RAGE (sRAGE)]. Therefore we analyzed whether statins influence the production of soluble RAGE. Lovastatin treatment of either mouse alveol…

medicine.medical_specialtyendocrine system diseasesADAM10Receptor for Advanced Glycation End ProductsBeta-CyclodextrinsQD415-436PharmacologyBiochemistryCell LineRAGE (receptor)MiceEndocrinologyGlycationInternal medicinediabetic complicationsmedicineAnimalsHumansSecretionLovastatincardiovascular diseasesReceptors ImmunologicReceptorResearch ArticlesDose-Response Relationship DrughypercholesterolemiaChemistrybeta-CyclodextrinsHEK 293 cellsTricarboxylic Acidsnutritional and metabolic diseasesCell BiologyBridged Bicyclo Compounds HeterocyclicADAM 10CholesterolFarnesyl-Diphosphate FarnesyltransferaseEndocrinologySolubilitycardiovascular systemLovastatinHydroxymethylglutaryl-CoA Reductase Inhibitorsatherosclerosishuman activitiesmedicine.drugJournal of Lipid Research
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Decreased plasma soluble RAGE in patients with hypercholesterolemia: Effects of statins

2007

The receptor for advanced glycation endproducts (RAGE) is overexpressed at sites of vascular pathology. A soluble RAGE isoform (sRAGE) neutralizes the ligand-mediated damage by acting as a decoy. We hypothesized that in hypercholesterolemia up-regulation of the ligand-RAGE axis may bridge impairment of nitric oxide biosynthesis with oxidative stress. We measured in 60 hypercholesterolemic patients and 20 controls plasma total sRAGE levels, urinary 8-iso-prostaglandin (PG) F(2alpha) excretion, and plasma levels of asymmetric dimethylarginine (ADMA). The effects of two structurally different statins (pravastatin and atorvastatin) on these parameters were analyzed in 20 hypercholesterolemic su…

Malemedicine.medical_specialtySettore MED/09 - Medicina InternaStatinmedicine.drug_classAtorvastatinHypercholesterolemiaReceptor for Advanced Glycation End ProductsFree radicalsArginineDinoprostNitric Oxidemedicine.disease_causeBiochemistrychemistry.chemical_compoundDouble-Blind MethodPhysiology (medical)Internal medicineHyperlipidemiaAtorvastatinmedicineHumansPyrrolesReceptors ImmunologicEndothelial dysfunctionPravastatinChemistryVascular diseaseAnticholesteremic AgentsStatinnutritional and metabolic diseasesMiddle AgedAtherosclerosismedicine.diseaseADMACross-Sectional StudiesHyperlipidemiaEndocrinologyHeptanoic AcidsOxidative streFemalelipids (amino acids peptides and proteins)Hydroxymethylglutaryl-CoA Reductase InhibitorsNitric Oxide SynthaseAsymmetric dimethylarginineOxidative stressPravastatinsRAGEmedicine.drugFree Radical Biology and Medicine
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Advanced Glycation End Products: Do They Impair Bone Health in Diabetes?

2022

AbstractIn diabetes mellitus (DM), there is increased formation and accumulation of advanced glycation end products (AGEs), which represent a heterogeneous class of molecules produced by non-enzymatic glycation of various molecules during long-term hyperglycaemia. Several studies have examined the role of AGEs in DM complications. Accumulating evidence suggests that AGEs affect bone metabolism. New knowledge indicates that they may play a role in bone disease among DM subjects. More data are now needed to clarify their role and to explore new AGEs-based therapeutic options for optimal bone health in DM.

Glycation End Products AdvancedDiabetes ComplicationsEndocrinologyBone Densityadvanced glycation end products bone formation complications diabetes mellitusEndocrinology Diabetes and MetabolismReceptor for Advanced Glycation End ProductsDiabetes MellitusInternal MedicineHumansGeneral Medicine
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