リソソーム酵素選別シグナルの解析 : DNase Iを用いた研究を中心に Study on the Lysosomal Enzyme Selection System

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著者

    • 西河 淳 NISHIKAWA Atsushi
    • 東京農工大学農学部応用生物科学科 Department of Applied Biological Science, Tokyo University of Agriculture and Technology

抄録

In many cell types, newly synthesized acid hydrolases acquire mannose 6-phosphate residues which serve as high affinity ligands for binding to Man-6-P receptors and targeting to lysosomes. A key step in this pathway is the ability of the enzyme UDP-G1cNAc: Lysosomal enzyme acetylglucosaminyl phosphotransferase to selective recognize and phosphorylate acid hydrolases. We have previously demonstrated that phosphotransferase recognizes conformational dependent protein determinants present on the acid hydrolases and absent in most nonlysosomal glycoproteins. It was recently reported that the secretory glycoprotein DNase I contains Man-6-P residues and we found that the human, bovine and mouse forms of this enzyme are phosphorylated to a low extent when expressed in COS cells. The poor phosphorylation of human and bovine DNase I is due to the lack of two critical lysines (position 27 and 74) present in the mouse enzyme whereas the poor phosphorylation of mouse DNase I appears to be due to the presence of "inhibitory" amino acid (Val23) that block the phosphotransferase recognition domain and the disappear of two critical amino acids (Tyr54 and Ser190). Then, we also report the substrate specificity of GPT for the oligosaccharides using variety of fluorescence labeled high mannose type oligosaccharides. As a point to be noticed, GPT can transfer the G1cNAc-phosphate to the G1cMan9GlcNAc2 that still remains glucose.

収録刊行物

  • 応用糖質科学 : oyo toshitsu kagaku = Journal of applied glycoscience

    応用糖質科学 : oyo toshitsu kagaku = Journal of applied glycoscience 49(2), 205-210, 2002-04-01

    The Japanese Society of Applied Glycoscience

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各種コード

  • NII論文ID(NAID)
    10008253728
  • NII書誌ID(NCID)
    AN10453916
  • 本文言語コード
    JPN
  • 資料種別
    REV
  • ISSN
    13403494
  • NDL 記事登録ID
    6142489
  • NDL 雑誌分類
    ZP24(科学技術--化学・化学工業--糖・澱粉)
  • NDL 請求記号
    Z17-15
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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