Journal article


N -(Carboxymethyl)lysine adducts of proteins are ligands for RAGE (receptor for AGE) that activate cell signalling pathways and modulate gene expression


Publication Details
Author(s): Kislinger T, Fu C, Huber B, Qu W, Taguchi A, Yan SD, Hofmann MA, Yan SF, Pischetsrieder M, Stern DM, Schmidt AM
Publisher: American Society for Biochemistry and Molecular Biology
Publication year: 1999
Volume: 274
Pages range: 31740-31749
ISSN: 1083-351X

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.



How to cite
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. The 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." The Journal of biological chemistry 274 (1999): 31740-31749.

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