Histone functions as a cell-surface receptor for AGEs

Masanori Itakura, Kosuke Yamaguchi, Roma Kitazawa, Sei-Young Lim, Yusuke Anan, Jun Yoshitake, Takahiro Shibata, Lumi Negishi, Hikari Sugawa, Ryoji Nagai and Koji Uchida ()
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Masanori Itakura: The University of Tokyo
Kosuke Yamaguchi: The University of Tokyo
Roma Kitazawa: The University of Tokyo
Sei-Young Lim: The University of Tokyo
Yusuke Anan: The University of Tokyo
Jun Yoshitake: Nagoya University
Takahiro Shibata: Nagoya University
Lumi Negishi: The University of Tokyo
Hikari Sugawa: Tokai University
Ryoji Nagai: Tokai University
Koji Uchida: The University of Tokyo

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: Abstract Reducing sugars can covalently react with proteins to generate a heterogeneous and complex group of compounds called advanced glycation end products (AGEs). AGEs are generally considered as pathogenic molecules, mediating a pro-inflammatory response and contributing to the development of a number of human diseases. However, the intrinsic function of AGEs remains to be elucidated. We now provide multiple lines of evidence showing that AGEs can specifically bind histone localized on the cell surface as an AGE-binding protein, regulate the function of histone as a plasminogen receptor, and result in the regulation of monocytes/macrophage recruitment to the site of inflammation. Our finding of histone as a cell-surface receptor for AGEs suggests that, beside our common concept of AGEs as danger-associated molecular patterns mediating a pro-inflammatory response, they may also be involved in the homeostatic response via binding to histone.

Date: 2022
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DOI: 10.1038/s41467-022-30626-8

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