© 1999 American Heart Association, Inc.
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Activation of Receptor for Advanced Glycation End Products
A Mechanism for Chronic Vascular Dysfunction in Diabetic Vasculopathy and Atherosclerosis
From the Division of Surgical Science, Departments of Surgery (A.M.S., D.S.), Medicine (A.M.S.), Pathology (S.D.Y.), and Physiology (D.S.) and Cellular Biophysics (A.M.S., S.D.Y, D.S.), College of Physicians & Surgeons of Columbia University, New York, NY, and Laboratoire de Biologie Vasculaire et Cellulaire (J-L.W.), UFR Lariboisiere St Louis, Paris, France.
Correspondence to Dr Ann Marie Schmidt, Department of Surgery, P&S 17-501, College of Physicians & Surgeons of Columbia University, 630 W 168th St, New York, NY 10032.
Abstract
Abstract—Receptor for advanced glycation end products (RAGE) is a member of the immunoglobulin superfamily of cell surface molecules and engages diverse ligands relevant to distinct pathological processes. One class of RAGE ligands includes glycoxidation products, termed advanced glycation end products, which occur in diabetes, at sites of oxidant stress in tissues, and in renal failure and amyloidoses. RAGE also functions as a signal transduction receptor for amyloid ß peptide, known to accumulate in Alzheimer disease in both affected brain parenchyma and cerebral vasculature. Interaction of RAGE with these ligands enhances receptor expression and initiates a positive feedback loop whereby receptor occupancy triggers increased RAGE expression, thereby perpetuating another wave of cellular activation. Sustained expression of RAGE by critical target cells, including endothelium, smooth muscle cells, mononuclear phagocytes, and neurons, in proximity to these ligands, sets the stage for chronic cellular activation and tissue damage. In a model of accelerated atherosclerosis associated with diabetes in genetically manipulated mice, blockade of cell surface RAGE by infusion of a soluble, truncated form of the receptor completely suppressed enhanced formation of vascular lesions. Amelioration of atherosclerosis in these diabetic/atherosclerotic animals by soluble RAGE occurred in the absence of changes in plasma lipids or glycemia, emphasizing the contribution of a lipid- and glycemia-independent mechanism(s) to atherogenesis, which we postulate to be interaction of RAGE with its ligands. Future studies using mice in which RAGE expression has been genetically manipulated and with selective low molecular weight RAGE inhibitors will be required to definitively assign a critical role for RAGE activation in diabetic vasculopathy. However, sustained receptor expression in a microenvironment with a plethora of ligand makes possible prolonged receptor stimulation, suggesting that interaction of cellular RAGE with its ligands could be a factor contributing to a range of important chronic disorders.
Key Words: glycoxidation • diabetes • nuclear factor-
B • inflammation • amyloid
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 M. M. Sousa, S. Du Yan, R. Fernandes, A. Guimaraes, D. Stern, and M. J. Saraiva Familial Amyloid Polyneuropathy: Receptor for Advanced Glycation End Products-Dependent Triggering of Neuronal Inflammatory and Apoptotic Pathways J. Neurosci., October 1, 2001; 21(19): 7576 - 7586. [Abstract] [Full Text] [PDF]
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T. Kislinger, N. Tanji, T. Wendt, W. Qu, Y. Lu, L. J. Ferran Jr, A. Taguchi, K. Olson, L. Bucciarelli, M. Goova, et al. Receptor for Advanced Glycation End Products Mediates Inflammation and Enhanced Expression of Tissue Factor in Vasculature of Diabetic Apolipoprotein E-Null Mice Arterioscler. Thromb. Vasc. Biol., June 1, 2001; 21(6): 905 - 910. [Abstract] [Full Text] [PDF]
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C.-H. Yeh, L. Sturgis, J. Haidacher, X.-N. Zhang, S. J. Sherwood, R. J. Bjercke, O. Juhasz, M. T. Crow, R. G. Tilton, and L. Denner Requirement for p38 and p44/p42 Mitogen-Activated Protein Kinases in RAGE-Mediated Nuclear Factor-{kappa}B Transcriptional Activation and Cytokine Secretion Diabetes, June 1, 2001; 50(6): 1495 - 1504. [Abstract] [Full Text]
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B. I. Hudson, M. H. Stickland, T. S. Futers, and P. J. Grant Effects of Novel Polymorphisms in the RAGE Gene on Transcriptional Regulation and Their Association With Diabetic Retinopathy Diabetes, June 1, 2001; 50(6): 1505 - 1511. [Abstract] [Full Text]
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S. M. Twigg, M. M. Chen, A. H. Joly, S. D. Chakrapani, J. Tsubaki, H.-S. Kim, Y. Oh, and R. G. Rosenfeld Advanced Glycosylation End Products Up-Regulate Connective Tissue Growth Factor (Insulin-Like Growth Factor-Binding Protein-Related Protein 2) in Human Fibroblasts: A Potential Mechanism for Expansion of Extracellular Matrix in Diabetes Mellitus Endocrinology, May 1, 2001; 142(5): 1760 - 1769. [Abstract] [Full Text]
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 M.-P. Wautier, O. Chappey, S. Corda, D. M. Stern, A. M. Schmidt, and J.-L. Wautier Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE Am J Physiol Endocrinol Metab, May 1, 2001; 280(5): E685 - E694. [Abstract] [Full Text] [PDF]
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 B. Degryse, T. Bonaldi, P. Scaffidi, S. Muller, M. Resnati, F. Sanvito, G. Arrigoni, and M. E. Bianchi The High Mobility Group (HMG) Boxes of the Nuclear Protein HMG1 Induce Chemotaxis and Cytoskeleton Reorganization in Rat Smooth Muscle Cells J. Cell Biol., March 19, 2001; 152(6): 1197 - 1206. [Abstract] [Full Text] [PDF]
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S. G. ROSTAND Coronary Heart Disease in Chronic Renal Insufficiency: Some Management Considerations J. Am. Soc. Nephrol., October 1, 2000; 11(10): 1948 - 1956. [Full Text]
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 E. Abraham, J. Arcaroli, A. Carmody, H. Wang, and K. J. Tracey Cutting Edge: HMG-1 as a Mediator of Acute Lung Inflammation J. Immunol., September 15, 2000; 165(6): 2950 - 2954. [Abstract] [Full Text] [PDF]
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S. D. Yan, A. Roher, A. M. Schmidt, and D. M. Stern Cellular Cofactors for Amyloid {beta}-Peptide-Induced Cell Stress : Moving from Cell Culture to in Vivo Am. J. Pathol., November 1, 1999; 155(5): 1403 - 1411. [Full Text] [PDF]
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 C. Renard, O. Chappey, M. P. Wautier, M. Nagashima, J. Morser, J. M. Scherrmann, and J. L. Wautier The Human and Rat Recombinant Receptors for Advanced Glycation End Products Have a High Degree of Homology but Different Pharmacokinetic Properties in Rats J. Pharmacol. Exp. Ther., September 1, 1999; 290(3): 1458 - 1466. [Abstract] [Full Text]
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N. Tanaka, H. Yonekura, S.-i. Yamagishi, H. Fujimori, Y. Yamamoto, and H. Yamamoto The Receptor for Advanced Glycation End Products Is Induced by the Glycation Products Themselves and Tumor Necrosis Factor-alpha through Nuclear Factor-kappa B, and by 17beta -Estradiol through Sp-1 in Human Vascular Endothelial Cells J. Biol. Chem., August 11, 2000; 275(33): 25781 - 25790. [Abstract] [Full Text] [PDF]
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