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Histone functions as a cell-surface receptor for AGEs

Author

Listed:
  • 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
    Japan Agency for Medical Research and Development, CREST)

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.

Suggested Citation

  • Masanori Itakura & Kosuke Yamaguchi & Roma Kitazawa & Sei-Young Lim & Yusuke Anan & Jun Yoshitake & Takahiro Shibata & Lumi Negishi & Hikari Sugawa & Ryoji Nagai & Koji Uchida, 2022. "Histone functions as a cell-surface receptor for AGEs," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-30626-8
    DOI: 10.1038/s41467-022-30626-8
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    References listed on IDEAS

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    1. Fei Xiao & Denian Wang & Lingmiao Kong & Min Li & Zhongxue Feng & Bingxing Shuai & Lijun Wang & Yong’gang Wei & Hongyu Li & Sisi Wu & Chun Tan & Huan Zhao & Xuejiao Hu & Jin Liu & Yan Kang & Xuelian L, 2018. "Intermedin protects against sepsis by concurrently re-establishing the endothelial barrier and alleviating inflammatory responses," Nature Communications, Nature, vol. 9(1), pages 1-15, December.
    2. Landin Boring & Jennifa Gosling & Michael Cleary & Israel F. Charo, 1998. "Decreased lesion formation in CCR2−/− mice reveals a role for chemokines in the initiation of atherosclerosis," Nature, Nature, vol. 394(6696), pages 894-897, August.
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