0000000000084448

AUTHOR

Angelika Bierhaus

showing 4 related works from this author

RAGE Mediates a Novel Proinflammatory Axis

1999

S100/calgranulin polypeptides are present at sites of inflammation, likely released by inflammatory cells targeted to such loci by a range of environmental cues. We report here that receptor for AGE (RAGE) is a central cell surface receptor for EN-RAGE (extracellular newly identified RAGE-binding protein) and related members of the S100/calgranulin superfamily. Interaction of EN-RAGEs with cellular RAGE on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Blockade of EN-RAGE/RAGE quenches delayed-type hypersensitivity and inflammatory colitis in murine models by arresting activation of central signaling pathw…

endocrine system diseasesbiologyBiochemistry Genetics and Molecular Biology(all)nutritional and metabolic diseasesInflammationS100A12 ProteinGeneral Biochemistry Genetics and Molecular BiologyCell biologyRAGE (receptor)Proinflammatory cytokineCell surface receptorImmunologycardiovascular systembiology.proteinmedicineCalgranulincardiovascular diseasesmedicine.symptomSignal transductionReceptorhuman activitiesCell
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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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Association of reduced glyoxalase 1 activity and painful peripheral diabetic neuropathy in type 1 and 2 diabetes mellitus patients

2013

Abstract Aims The present study was undertaken to investigate the relationship between glyoxalase 1 (Glo1) enzyme activity and painful diabetic neuropathy (DN) in patients with diabetes mellitus. Methods Glo1 activity and biochemical markers were determined in blood samples from 108 patients with type 1 diabetes, 109 patients with type 2 diabetes, and 132 individuals without diabetes as a control. Painful and painless peripheral DN was assessed and multivariate regression analysis was used to determine independent association of Glo1 activity with occurrence of painful DN. Results In patients with type 1 and type 2 diabetes mellitus and painful DN compared to patients with painless DN, Glo1…

AdultMalemedicine.medical_specialtyMultivariate analysisEndocrinology Diabetes and MetabolismPainType 2 diabetesSeverity of Illness IndexGastroenterologyEndocrinologyDiabetic NeuropathiesInternal medicineDiabetes mellitusInternal MedicinemedicineHumansPain MeasurementGlycated HemoglobinType 1 diabetesbusiness.industryConfoundingLactoylglutathione LyasePeripheral Nervous System DiseasesType 2 Diabetes MellitusMiddle Agedmedicine.diseasePeripheralDiabetes Mellitus Type 1EndocrinologyDiabetes Mellitus Type 2Painful diabetic neuropathyDisease ProgressionFemalebusinessBiomarkersJournal of Diabetes and its Complications
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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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