Rage: A Novel Cellular Receptor for Advanced Glycation End Products

Author:

Schmidt Ann Marie1,Hori Osamu1,Cao Rong1,Yan Shi Du1,Brett Jerold1,Wautier Jean-Luc2,Ogawa Satoshi3,Kuwabara Keisuke3,Matsumoto Masayasu3,Stern David1

Affiliation:

1. Departments of Medicine, Physiology and Surgery, Columbia University, College of Physicians and Surgeons New York, New York

2. Laboratoire de Recherche en Biologie Vasculaire et Cellulaire, Unite d'Immunohematologie, Hopital Lariboisiere, Universie Paris 7 Faculte de Medecine, Paris, France

3. First Department of Medicine, Osaka University School of Medicine Osaka, Japan

Abstract

Exposure of proteins to reducing sugars results in nonenzymatic glycation with the ultimate formation of advanced glycation end products (AGEs). One means through which AGEs modulate cellular functions is through binding to specific cell surface acceptor molecules. The receptor for AGEs (RAGE) is such a receptor and is a newly identified member of the immunoglobulin superfamily expressed on endothelial cells (ECs), mononuclear phagocytes (MPs), and vascular smooth muscle cells (SMCs) in both vivo and in vitro. Binding of AGEs to RAGE results in induction of cellular oxidant stress, as exemplified by the generation of thiobarbituric acid-reactive substances, expression of heme oxygenase type I, and activation of the transcription factor NF-kB, with consequences for a range of cellular functions. AGEs on the surface of diabetic red cells enhance binding to endothelial RAGE and result in enhanced oxidant stress in the vessel wall. By using reagents to selectively block access to RAGE, the role of this receptor in AGE-mediated perturbation of cellular properties can be dissected in detail.

Publisher

American Diabetes Association

Subject

Endocrinology, Diabetes and Metabolism,Internal Medicine

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