Identification of heparin-binding sites in midkine and their role in neurite-promotion

Toshinobu Asai, Kiichi Watanabe, Keiko Ichihara-Tanaka, Norio Kaneda, Soichi Kojima, Akihisa Iguchi, Fuyuhiko Inagaki, Takashi Muramatsu

研究成果: ジャーナルへの寄稿学術論文査読

43 被引用数 (Scopus)

抄録

Midkine (MK) is a heparin-binding growth factor, which promotes neurite outgrowth in embryonic neurons and enhances their survival. The three dimensional structure of MK clarified by NMR spectroscopy indicates that several basic amino acids are exposed on the surface of the C-terminal half domain, which retains heparin-binding and neurite-promoting activity. We performed site-directed mutagenesis of these amino acids, and found that mutation of arginine78 reduced the heparin-binding activity. Mutation of either lysine83 or lysine84 scarcely affected heparin-binding activity, while the double mutant involving both lysine residues showed reduction in the activity. Neurite-promoting activity of mutant MKs always correlated with their heparin-binding activity, illustrating the close relationship of the two activities. Thus, the present result verifies the occurrence of two distinct heparin-binding sites involved in neurite-promoting activity of MK molecule.

本文言語英語
ページ(範囲)66-70
ページ数5
ジャーナルBiochemical and Biophysical Research Communications
236
1
DOI
出版ステータス出版済み - 09-07-1997
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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