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2006 Fiscal Year Final Research Report Summary

Studies on the mechanism of amyloid fibril formation using yeast expression system of amyloidogenic proteins and the search of food components to prevent the formation of amyloid fibril

Research Project

Project/Area Number 17380080
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field Food science
Research InstitutionYamaguchi University

Principal Investigator

KATO Akio  Yamaguchi University, Professor Emeritus, 名誉教授 (00035114)

Co-Investigator(Kenkyū-buntansha) AZAKAMI Hiroyuki  Yamaguchi University, Faculty of Agriculture, Associate Professor, 農学部, 助教授 (40263850)
Project Period (FY) 2005 – 2006
Keywordsamyloidosis / amyloidogenic lysozyme / amyloidogenic cystatin / Pichia pastoris expression / PQQ / catechin / エピガロカテキン
Research Abstract

We are successful to secrete amyloidogenic proteins such as mutant lysozyme and cystatin in yeast expression system. Therefore, it is easy to search the effective food components to prevent amyloid fibril formation of these amyloidogenic proteins. Thus, we found that catechin, epigarocatechin and PQQ (pyrroloquinoline quinine) are efficiently prevent the amyloid fibril formation using yeast expression system of amyloidogenic cystatin. In addition, the yeast secretion system of amyloidogenic proteins enabled to address how to prevent amyloidosis using various mutants of amyloidogenic proteins such as lysozyme and cystatin. To address the role of glycosylation on the fibrillogenecity of cystatin, the consensus sequence for N-linked glycosylation was introduced by site-directed mutagenesis into the amyloidogenic cystatin. The glycosylation of amyroidogenic cystatin inhibited the formation of cystain dimmer. This finding suggests that the mechanism causing the prevention of amyloidogenic fibril formation may be the suppression of three-dimensional domain-swapped dimmers and oligomers. In addition, attempt to elucidate the mechanism of the amyloid fibril formation was carried out using various mutant amyloidogenic lysozymes. The helix-stabilizing mutant lysozyme suppressed the amyloidogenic fibril formation and increase inβ-structure. This suggests that a-helix of lysozyme converts into β-structure during amyloidosis of lysozyme.

  • Research Products

    (6 results)

All 2006 2005

All Journal Article (6 results)

  • [Journal Article] Prevention of amyloid fibril formation of amyloidogenic chicken cystatin by site-specific glycosylation in yeast.2006

    • Author(s)
      J.W.He et al.
    • Journal Title

      Protein Science 15

      Pages: 213-222

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Preparation of bio active and surface functional oligomannosyl neoglycoprotein in yeast2006

    • Author(s)
      S.Nakamura et al.
    • Journal Title

      Bioconjugate Chem. 17

      Pages: 1170-1177

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Preparation of bio active and surface functional oligomannosyl neoglycoprotein in Yeast2006

    • Author(s)
      S.Nakamura et al.
    • Journal Title

      Bioconjugate Chem. 17

      Pages: 1170-1177

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Characterization of recombinant amyloidogenic chicken cystatin mutant I66Q expressed in yeast.2005

    • Author(s)
      J.W.He et al.
    • Journal Title

      J. Biochem. 137

      Pages: 477-485

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Effect of EPS1 gene deletion in S. cerevisiae on the secretion of foreign proteins which have disulfide bridges.2005

    • Author(s)
      J.W.He et al.
    • Journal Title

      FEBS Letters 579

      Pages: 2277-2283

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Characterization of recombinant amyloidogenic chicken cystatin mutant I66Q expressed in yeast.2005

    • Author(s)
      J.W.He et al.
    • Journal Title

      J.Biochem. 137

      Pages: 477-485

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 2008-05-27  

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