N -(Carboxymethyl)lysine adducts of proteins are ligands for RAGE (receptor for AGE) that activate cell signalling pathways and modulate gene expression
Kislinger T, Fu C, Huber B, Qu W, Taguchi A, Yan SD, Hofmann MA, Yan SF, Pischetsrieder M, Stern DM, Schmidt AM (1999)
Publication Type: Journal article
Publication year: 1999
Journal
Publisher: American Society for Biochemistry and Molecular Biology
Book Volume: 274
Pages Range: 31740-31749
Abstract
Recent studies suggested that interruption of the interaction of advanced glycation end products (AGEs), with the signal-transducing receptor receptor for AGE (RAGE), by administration of the soluble, extracellular ligand-binding domain of RAGE, reversed vascular hyperpermeability and suppressed accelerated atherosclerosis in diabetic rodents. Since the precise molecular target of soluble RAGE in those settings was not elucidated, we tested the hypothesis that predominant specific AGEs within the tissues in disorders such as diabetes
and renal failure, Ne-(carboxymethyl)lysine (CML) adducts, are ligands of RAGE. We demonstrate here that physiologically relevant CML modifications of proteins engage cellular RAGE, thereby activating key cell signaling pathways such as NF-kB and modulating gene
expression. Thus, CML-RAGE interaction triggers processes intimately linked to accelerated vascular and inflammatory complications that typify disorders in which inflammation is an established component.
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APA:
Kislinger, T., Fu, C., Huber, B., Qu, W., Taguchi, A., Yan, S.D.,... Schmidt, A.M. (1999). N -(Carboxymethyl)lysine adducts of proteins are ligands for RAGE (receptor for AGE) that activate cell signalling pathways and modulate gene expression. Journal of Biological Chemistry, 274, 31740-31749. https://dx.doi.org/10.1074/jbc.274.44.31740
MLA:
Kislinger, Thomas, et al. "N -(Carboxymethyl)lysine adducts of proteins are ligands for RAGE (receptor for AGE) that activate cell signalling pathways and modulate gene expression." Journal of Biological Chemistry 274 (1999): 31740-31749.
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