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Mol. Cells 2011; 31(2): 91-97

Published online February 28, 2011

https://doi.org/10.1007/s10059-011-0030-x

© The Korean Society for Molecular and Cellular Biology

RAGE: The Beneficial and Deleterious Effects by Diverse Mechanisms of Actions

Sun-Ho Han, Yoon Hee Kim, and Inhee Mook-Jung*

Department of Biochemistry and Biomedical Sciences, Seoul National University, College of Medicine, Seoul 110-799, Korea

Correspondence to : *Correspondence: inhee@snu.ac.kr

Received: December 15, 2010; Accepted: December 22, 2010

Abstract

Receptor for advanced glycation endproducts (RAGE) is a transmembrane protein that belongs to the immunoglobulin superfamily. RAGE is expressed ubiquitously-high in lung and moderate to low in a wide range of cells-in a tightly regulated manner at various stages of development. RAGE is a pattern recognition receptor that binds to multiple ligands, including amphoterin, members of the S100/ calgranulin family, the integrin Mac-1, and amyloid β-pep-tide (Aβ). RAGE-ligand engagement effects the activation of diverse cascades that initiate and stimulate chronic stress pathways and repair, depending on the ligand, envi-ronment, and developmental stage. Further, RAGE-ligand interaction and the consequent upregulation of RAGE through a positive feedback loop are often associated with various diseases, including vascular disease, diabetes, cancer, and neurodegenerative disease. It is unknown how RAGE mediates these events, but such phenomena appear to be linked to the inflammatory re-sponse. In this review, we summarize the findings on RAGE from published reports and ongoing studies. Also, the implication of RAGE in Alzheimer disease, the most common neurodegenerative disease in the elderly population, will be discussed, with a focus on Aβ-RAGE interactions with regard to signaling pathways and their impact on cellular activity.

Keywords Alzheimer disease, Amyloid β, NF-κB, p38 MARK, RAGE

Article

Minireview

Mol. Cells 2011; 31(2): 91-97

Published online February 28, 2011 https://doi.org/10.1007/s10059-011-0030-x

Copyright © The Korean Society for Molecular and Cellular Biology.

RAGE: The Beneficial and Deleterious Effects by Diverse Mechanisms of Actions

Sun-Ho Han, Yoon Hee Kim, and Inhee Mook-Jung*

Department of Biochemistry and Biomedical Sciences, Seoul National University, College of Medicine, Seoul 110-799, Korea

Correspondence to:*Correspondence: inhee@snu.ac.kr

Received: December 15, 2010; Accepted: December 22, 2010

Abstract

Receptor for advanced glycation endproducts (RAGE) is a transmembrane protein that belongs to the immunoglobulin superfamily. RAGE is expressed ubiquitously-high in lung and moderate to low in a wide range of cells-in a tightly regulated manner at various stages of development. RAGE is a pattern recognition receptor that binds to multiple ligands, including amphoterin, members of the S100/ calgranulin family, the integrin Mac-1, and amyloid β-pep-tide (Aβ). RAGE-ligand engagement effects the activation of diverse cascades that initiate and stimulate chronic stress pathways and repair, depending on the ligand, envi-ronment, and developmental stage. Further, RAGE-ligand interaction and the consequent upregulation of RAGE through a positive feedback loop are often associated with various diseases, including vascular disease, diabetes, cancer, and neurodegenerative disease. It is unknown how RAGE mediates these events, but such phenomena appear to be linked to the inflammatory re-sponse. In this review, we summarize the findings on RAGE from published reports and ongoing studies. Also, the implication of RAGE in Alzheimer disease, the most common neurodegenerative disease in the elderly population, will be discussed, with a focus on Aβ-RAGE interactions with regard to signaling pathways and their impact on cellular activity.

Keywords: Alzheimer disease, Amyloid β, NF-κB, p38 MARK, RAGE

Mol. Cells
Nov 30, 2022 Vol.45 No.11, pp. 763~867
COVER PICTURE
Naive (cyan) and axotomized (magenta) retinal ganglion cell axons in Xenopus tropicalis (Choi et al., pp. 846-854).

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