Mouse Na<sup>+</sup>/K<sup>+</sup>-ATPase β1-subunit has a K<sup>+</sup>-dependent cell adhesion activity for β-GlcNAc-terminating glycans

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  • Noriaki Kitamura
    Departments of Biosignal Research and Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan; Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan; Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan
  • Masahiko Ikekita
    Departments of Biosignal Research and Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan; Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan; Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan
  • Takeshi Sato
    Departments of Biosignal Research and Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan; Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan; Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan
  • Yoshihiro Akimoto
    Departments of Biosignal Research and Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan; Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan; Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan
  • Yasumaru Hatanaka
    Departments of Biosignal Research and Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan; Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan; Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan
  • Hayato Kawakami
    Departments of Biosignal Research and Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan; Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan; Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan
  • Mitsushi Inomata
    Departments of Biosignal Research and Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan; Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan; Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan
  • Kiyoshi Furukawa
    Departments of Biosignal Research and Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan; Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan; Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan

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<jats:p>A 48-kDa β-<jats:italic>N</jats:italic>-acetylglucosamine (GlcNAc)-binding protein was isolated from mouse brain by GlcNAc-agarose column chromatography. The N-terminal amino acid residues showed the protein to be a mouse Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>-ATPase β1-subunit. When the recombinant FLAG-β1-subunit expressed in Sf-9 cells was applied to a GlcNAc-agarose column, only the glycosylated 38- and 40-kDa proteins bound to the column. In the absence of KCl, little of the proteins bound to a GlcNAc-agarose column, but the 38- and 40-kDa proteins bound in the presence of KCl at concentrations above 1 mM. Immunohistochemical study showed that the β1-subunit and GlcNAc-terminating oligosaccharides are at the cell contact sites. Inclusion of anti-β1-subunit antibody or chitobiose in cell aggregation assays using mouse neural cells resulted in inhibition of cell aggregation. These results indicate that the Na<jats:sup>+</jats:sup>/K<jats:sup>+</jats:sup>-ATPase β1-subunit is a potassium-dependent lectin that binds to GlcNAc-terminating oligosaccharides: it may be involved in neural cell interactions.</jats:p>

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