Advanced Glycation End Product Receptor-Mediated Cellular Dysfunction

: Advanced glycation end products (AGEs), S100/calgranulins, and HMGB1 proteins supposedly play a pivotal role in diabetes mellitus and other chronic inflammatory diseases by promoting cellular dysfunction via binding to cellular surface receptors. Particularly, engagement of the receptor for AGEs (...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 2005-06, Vol.1043 (1), p.676-680
Main Authors: BIERHAUS, ANGELIKA, HUMPERT, PER M., STERN, DAVID M., ARNOLD, BERND, NAWROTH, PETER P.
Format: Article
Language:English
Subjects:
Activation
Age
AGE receptors
Animals
Cellular
diabetes
Diabetes Complications - genetics
Diabetes Complications - physiopathology
Diseases
Humans
inflammation
Ligands
Mice
Mice, Knockout
Models, Biological
RAGE
Receptor for Advanced Glycation End Products
Receptors
Receptors, Immunologic - deficiency
Receptors, Immunologic - genetics
Receptors, Immunologic - physiology
sRAGE
Surface chemistry
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Summary:: Advanced glycation end products (AGEs), S100/calgranulins, and HMGB1 proteins supposedly play a pivotal role in diabetes mellitus and other chronic inflammatory diseases by promoting cellular dysfunction via binding to cellular surface receptors. Particularly, engagement of the receptor for AGEs (RAGE) has gained major attention because it converts short‐lasting cellular activation in sustained cellular dysfunction. Consistently, blockade of ligand‐RAGE interaction with soluble RAGE (sRAGE) suppresses chronic cellular activation and dysfunction in animal models of chronic diseases. RAGE−/− mice, however, demonstrate that the protection conferred by RAGE deficiency is lower than that mediated by sRAGE. Furthermore, RAGE−/− mice can be protected by sRAGE in certain settings of the adaptive immune response. This finding implies that abounding RAGE ligands overworking the RAGE pathway might also activate other receptors.
ISSN:0077-8923
1749-6632
DOI:10.1196/annals.1333.077