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J Biol Chem, Vol. 274, Issue 44, 31740-31749, October 29, 1999
From the 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,
N
N
-(Carboxymethyl)Lysine Adducts
of Proteins Are Ligands for Receptor for Advanced Glycation End
Products That Activate Cell Signaling Pathways and Modulate Gene
Expression
,,
,,,,,,,, and
College of Physicians & Surgeons, Columbia
University, New York, New York 10032 and the Institut
für Pharmazie und Lebensmittelchemie, Abteilung
Lebensmittelchemie, Universitàt Erlangen-Nürnberg,
Schuhstrasse 19, Erlangen 91052, Germany
-(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-
B 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.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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