Glycation reaction and the role of the receptor for advanced glycation end-products in immunity and social behavior
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COMPREHENSIVE REVIEW ARTICLE
Glycation reaction and the role of the receptor for advanced glycation end-products in immunity and social behavior Nontaphat Leerach 1 & Ai Harashima 1 & Seiichi Munesue 1 & Kumi Kimura 1 & Yu Oshima 1 & Hisanori Goto 1 & Hiroshi Yamamoto 1,2 & Haruhiro Higashida 3 & Yasuhiko Yamamoto 1 Received: 30 August 2020 / Revised: 30 August 2020 / Accepted: 15 October 2020 # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract The receptor for advanced glycation end-products (receptor for AGEs, RAGE) is a pattern recognition receptor. The interaction of RAGE with its ligands, such as AGEs, S100 proteins, high mobility group box-1 (HMGB1), and lipopolysaccharides (LPS), is known to play a pivotal role in the propagation of immune responses and inflammatory reactions. The ligand-RAGE interaction elicits cellular responses, for example, in myeloid and lymphoid cells, through distinct pathways by activating NF-κB and Rac1/cdc42, which lead to cytokine production, cell migration, phagocytosis, maturation, and polarization. Recently, oxytocin, a peptide hormone and neuropeptide, was identified as a novel binding molecule for the RAGE; however, it cannot compete with the interaction of RAGE with other ligands or induce RAGE intracellular signaling. The RAGE transports oxytocin from the blood into the brain and regulates brain functions. In this review, we summarize the current understanding of glycation reaction, AGEs, and the RAGE-mediated biological responses as well as the physiological role of RAGE in immunity and social behaviors, particularly, maternal bonding. Keywords Receptor for advanced glycation end-products . Inflammation . Oxytocin . Maternal bonding
Abbreviations RAGE receptor for advanced glycation end-products Rac1/cdc42 ras-related C3 botulinum toxin substrate 1 / Cell division control protein 42 homolog CEL Nε-carboxyethyllysine CML Nε-carboxymethyllysine MG methylglyoxal
* Yasuhiko Yamamoto [email protected] 1
Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences, 13-1 Takara-machi, Kanazawa 920-8640, Japan
2
Komatsu University, Komatsu 923-0921, Japan
3
Department of Basic Research on Social Recognition and Memory, Research Centre for Child Mental Development, Kanazawa University, Kanazawa 920-8640, Japan
Introduction Browning of food during processing was initially described in the early nineteenth century by a French chemist, Maillard LC, and was thereafter named as Maillard reaction [1]. The Maillard reaction occurs in living systems, and the in vivo reaction between proteins, amino groups, and nonreducing sugars, such as glucose without enzymes, is termed “nonenzymatic glycation”, which is different from enzymatic glycosylation. The glycation reaction can be preceded endogenously or exogenously in the body. Irreversibly formed advanced glycation end-products (AGEs) are generated from a series of chemical reactions and have been implicated in various diseases, such as infla
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