The C‐terminus of the amelogenin peptide influences the proliferation of human bone marrow mesenchymal stem cells

  • Ryo Kunimatsu
    Department of Orthodontics Applied Life Sciences Hiroshima University Institute of Biomedical & Health Sciences Kasumi, Minami‐ku Hiroshima Japan
  • Tetsuya Awada
    Department of Orthodontics Applied Life Sciences Hiroshima University Institute of Biomedical & Health Sciences Kasumi, Minami‐ku Hiroshima Japan
  • Yuki Yoshimi
    Department of Orthodontics Applied Life Sciences Hiroshima University Institute of Biomedical & Health Sciences Kasumi, Minami‐ku Hiroshima Japan
  • Kazuyo Ando
    Department of Orthodontics Applied Life Sciences Hiroshima University Institute of Biomedical & Health Sciences Kasumi, Minami‐ku Hiroshima Japan
  • Naoto Hirose
    Department of Orthodontics Applied Life Sciences Hiroshima University Institute of Biomedical & Health Sciences Kasumi, Minami‐ku Hiroshima Japan
  • Yuki Tanne
    Department of Orthodontics Applied Life Sciences Hiroshima University Institute of Biomedical & Health Sciences Kasumi, Minami‐ku Hiroshima Japan
  • Keisuke Sumi
    Department of Orthodontics Applied Life Sciences Hiroshima University Institute of Biomedical & Health Sciences Kasumi, Minami‐ku Hiroshima Japan
  • Kotaro Tanimoto
    Department of Orthodontics Applied Life Sciences Hiroshima University Institute of Biomedical & Health Sciences Kasumi, Minami‐ku Hiroshima Japan

書誌事項

公開日
2018-04
資源種別
journal article
権利情報
  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1002/jper.17-0087
公開者
Wiley

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説明

<jats:title>Abstract</jats:title><jats:sec><jats:title>Background</jats:title><jats:p>Amelogenins are a family of enamel matrix proteins that are important for formation of enamel. Amelogenins may induce division of mesenchymal stem cells (MSCs), among others. Recently, the C‐terminus of the amelogenin peptide (AMG‐CP) has been shown to enhance the proliferation of cementoblast lineage cells. The role of the amelogenin peptide on the proliferation of human MSCs and related alterations in the intracellular signaling pathway were studied.</jats:p></jats:sec><jats:sec><jats:title>Methods</jats:title><jats:p>MSCs were exposed to AMG‐CP in vitro. The MTS and 5‐bromo‐2′‐deoxyuridine (BrdU) assays were used to determine proliferation. Expression of the amelogenin receptor, lysosomal‐associated membrane protein 1 (LAMP1), was examined in MSCs with western blotting. Binding of AMG‐CP to LAMP1 was inhibited with anti‐LAMP1 antibody. Components of the mitogen‐activated protein kinase (MAPK)–extracellular signal‐regulated kinase (ERK) pathway were studied with western blotting and enzyme‐linked immunosorbent assay, and U0126, an MAPK inhibitor, was used to inhibit ERK activity.</jats:p></jats:sec><jats:sec><jats:title>Results</jats:title><jats:p>MSC proliferation was significantly increased in the presence of AMG‐CP and significantly inhibited by anti‐LAMP1 antibody or U0126. Increased phosphorylated ERK1/2 was observed in the presence of AMG‐CP, and decreased phosphorylated ERK1/2 was seen in the presence of anti‐LAMP1 antibody or U0126.</jats:p></jats:sec><jats:sec><jats:title>Conclusion</jats:title><jats:p>A C‐terminal amelogenin variant increased the proliferation of MSCs via an interaction with LAMP1 and the MAPK–ERK signaling pathway, indicating the possibility of using MSCs for tissue regeneration in the craniofacial region.</jats:p></jats:sec>

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