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Elucidation of molecular mechanisms of lipid metabolism regulation and amyloidogenesis by serum amyloid A.

Research Project

Project/Area Number 20790045
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeSingle-year Grants
Research Field Physical pharmacy
Research InstitutionKobe Pharmaceutical University

Principal Investigator

TANAKA Masafumi  Kobe Pharmaceutical University, 薬学部, 講師 (40411904)

Project Period (FY) 2008 – 2009
Project Status Completed (Fiscal Year 2009)
Budget Amount *help
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2008: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Keywords血清アミロイドA / 脂質代謝 / アポリポ蛋白質
Research Abstract

Human serum amyloid A (SAA) protein is an apolipoprotein predominantly present in the high-density lipoprotein fraction of plasma. Despite its critical roles in lipid metabolism, especially in acute phases, systematic understanding of the lipid interaction of this protein is limited. SAA shares certain structural features with other apolipoproteins including amphipathic helices, a motif that appears to be responsible for lipid binding. Previously, we examined the lipid-binding properties of the putative amphipathic α-helices in apoA-I molecule using its fragment peptides. In the present study, lipid-binding properties of synthetic fragment peptides corresponding to the N-terminal (region spanning residues 1-27), central (residues 43-63), and C-terminal (residues 77-104) parts of human SAA molecule were examined. SAA (1-27) peptide binds to lipid forming an α-helical structure, whereas SAA (43-63) and (77-104) peptides do not display binding to lipid with any conformational changes. These results indicate that the N-terminal region of SAA is important for lipid interaction. In addition, the finding that proline substitution at 7th residue in the most N-terminal region markedly decreased the binding to lipid indicates that the α-helical structure in this region is essential for lipid binding of SAA. Furthermore, binding competition assay suggests that the replacement of apoA-I in HDL might be caused by membrane disruption by insertion of the N-terminal helix of SAA.

Report

(3 results)
  • 2009 Annual Research Report   Final Research Report ( PDF )
  • 2008 Annual Research Report
  • Research Products

    (11 results)

All 2009 2008 Other

All Journal Article (4 results) (of which Peer Reviewed: 4 results) Presentation (5 results) Remarks (2 results)

  • [Journal Article] Evaluation of Lipid-Binding Properties of the N-Terminal Helical Segments in Human Apolipoprotein A-I Using Fragment Peptides2009

    • Author(s)
      Tanaka M., Tanaka T., Ohta S., Kawakami T., Konno H., Akaji K., Aimoto S., Saito H.
    • Journal Title

      J. Pept. Sci. 15(1)

      Pages: 36-42

    • Related Report
      2009 Final Research Report
    • Peer Reviewed
  • [Journal Article] Defining Lipid-Binding Regions of Human Serum Amyloid A Using Its Fragment Peptides2009

    • Author(s)
      Ohta S., Tanaka M., Sakakura K., Kawakami T., Aimoto S., Saito H.
    • Journal Title

      Chem. Phys. Lipids 162(1-2)

      Pages: 62-68

    • Related Report
      2009 Final Research Report
    • Peer Reviewed
  • [Journal Article] Defining Lipid-Binding Regions of Human Serum Amyloid A Using Its Fragment Peptides2009

    • Author(s)
      Ohta S., Tanaka M., Sakakura K., Kawakami T., Aimoto S., Saito H.
    • Journal Title

      Chemistry and Physics of Lipids 162

      Pages: 62-68

    • Related Report
      2009 Annual Research Report
    • Peer Reviewed
  • [Journal Article] Evaluation of Lipid-Binding Properties of the N-Terminal Helical Segments in Human Apolipoprotein A-I Using Fragment Peptides2009

    • Author(s)
      Tanaka M., Tanaka T., Ohta S., Kawakami T., Konno H., Akaji K., Aimoto S., Saito H.
    • Journal Title

      Journal of Peptide Science 15(1)

      Pages: 36-42

    • Related Report
      2008 Annual Research Report
    • Peer Reviewed
  • [Presentation] 脂質代謝異常に関与する血清アミロイドAの脂質膜結合機構の解明2009

    • Author(s)
      田中将史、大田慎也、坂倉広大、川上徹、相本三郎、斎藤博幸
    • Organizer
      膜シンポジウム
    • Place of Presentation
      広島
    • Year and Date
      2009-11-18
    • Related Report
      2009 Final Research Report
  • [Presentation] 脂質代謝異常に関与する血清アミロイドAの脂質膜結合機構の解明2009

    • Author(s)
      田中将史、大田慎也、坂倉広大、川上徹、相本三郎、斎藤博幸
    • Organizer
      膜シンポジウム2009
    • Place of Presentation
      広島
    • Year and Date
      2009-11-18
    • Related Report
      2009 Annual Research Report
  • [Presentation] ヒトSerum Amyloid AのN末端領域は脂質結合に重要な役割を果たす2008

    • Author(s)
      大田慎也, 田中将史, 川上徹, 相本三郎, 斎藤博幸
    • Organizer
      第45回ペプチド討論会
    • Place of Presentation
      東京
    • Year and Date
      2008-10-29
    • Related Report
      2009 Final Research Report 2008 Annual Research Report
  • [Presentation] 急性期タンパク質血清アミロイドA (SAA)の脂質結合部位の特定2008

    • Author(s)
      大田慎也, 田中将史, 川上徹, 相本三郎, 斎藤博幸
    • Organizer
      第58回日本薬学会近畿支部大会
    • Place of Presentation
      神戸
    • Year and Date
      2008-10-25
    • Related Report
      2009 Final Research Report
  • [Presentation] 急性期タンパク質血清アミロイドA(SAA)の脂質結合部位の特定2008

    • Author(s)
      大田慎也, 田中将史, 川上徹, 相本三郎, 斎藤博幸
    • Organizer
      第58回日本薬学会近畿支部大会
    • Place of Presentation
      神戸
    • Year and Date
      2008-10-25
    • Related Report
      2008 Annual Research Report
  • [Remarks]

    • URL

      http://www.kobepharma-u.ac.jp/~biophys/

    • Related Report
      2009 Annual Research Report
  • [Remarks]

    • URL

      http://www.kobepharma-u.acjp/~biophys/

    • Related Report
      2008 Annual Research Report

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Published: 2008-04-01   Modified: 2016-04-21  

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