膜構造によるアポリポタンパク質の機能制御 Membrane Structure Modulates the Function of Apolipoproteins

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Apolipoprotein (apo) A-I and E are exchangeable proteins in plasma and play key roles in lipoprotein metabolism. Association of apoA-I and E with lipid is required for their functions; apoA-I functions as an acceptor of cell membrane cholesterol and apoE serves as a high-affinity ligand for cell surface receptors. To better understand apolipoprotein-lipid interactions on cell membranes and lipoprotein surfaces, thermodynamic approach using isothermal titration calorimetry, fluorescence measurements using fluorescent phospholipid analogue, and natural abundance <SUP>13</SUP>C NMR method were employed. ApoA-I binding to lipid membrane was found to be superficial and binding capacity was modulated by the degree of separation between the carbonyl groups at the surface. Cholesterol increased the head group space of phospholipids so as to allow more apoA-I to bind to the membrane surface, suggesting the interaction of apoA-I with cholesterol-enriched membrane domains. ApoE binds to the lipoprotein surface through the 10-kDa C-terminal domain that has a high-affinity for lipid. Our results showed that apoE bound to the spherical particles can adopt two distinct conformations with the N-terminal four-helix bundle either open or closed, suggesting that lipoprotein-associated apoE displays variable receptor binding activity depending upon the surface structure. Cholesterol may be the key component regulating such a conformational change of apoE on the lipoprotein surface.

収録刊行物

  • 膜 27(6), 317-323, 2002-11-01

    THE MEMBRANE SOCIETY OF JAPAN

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各種コード

  • NII論文ID(NAID)
    10010087706
  • NII書誌ID(NCID)
    AN0023215X
  • 本文言語コード
    JPN
  • 資料種別
    REV
  • ISSN
    03851036
  • NDL 記事登録ID
    6362395
  • NDL 雑誌分類
    ZR2(科学技術--生物学--生化学)
  • NDL 請求記号
    Z18-1127
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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