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Age-related Asp Isomerizations in Lens Alpha-crystallin

Research Project

Project/Area Number 15K16514
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeMulti-year Fund
Research Field Applied health science
Research InstitutionKyoto University (2016)
Tokyo University of Pharmacy and Life Science (2015)

Principal Investigator

Takata Takumi  京都大学, 原子炉実験所, 特定准教授 (80379007)

Project Period (FY) 2015-04-01 – 2017-03-31
Project Status Completed (Fiscal Year 2016)
Budget Amount *help
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
KeywordsD-アミノ酸 / クリスタリン / 白内障 / 加齢 / タンパク質異常凝集 / 質量分析 / D-Asp / 水晶体 / crystallin / タンパク質
Outline of Final Research Achievements

The lens α-crystallin is composed of two subunits αA- and αB-crystallin (αA-Crys and αB-Crys), which form various oligomers and complexes. Recent studies have shown that many aspartyl residues (Asp) in αA-Crys inverted to isomers (Lβ-Asp, Dα-Asp, Dβ-Asp) with age. It has not been well understood whether Asp isomers in native polymeric αA-Crys are different from those in dissociated αA-Crys or those in aggregated complexes. We therefore examined to clarify the distribution of Asp isomers in dissociated αA-Crys and those in aggregated αA-Crys. The results showed that the isomerization of Asp 58 in αA-Crys were highly detectable from the monomeric fraction. In addition, age-dependent Asp 58 isomerization in α-Crys is similar to the ratio from lens insoluble fraction. The isomerization of Asp as well as many other modifications would reduce the normal subunit-subunit interaction of α-Crys with aging, result in senile cataract formation.

Report

(3 results)
  • 2016 Annual Research Report   Final Research Report ( PDF )
  • 2015 Research-status Report
  • Research Products

    (11 results)

All 2017 2016 2015

All Journal Article (6 results) (of which Int'l Joint Research: 2 results,  Peer Reviewed: 6 results,  Open Access: 3 results,  Acknowledgement Compliant: 2 results) Presentation (5 results) (of which Int'l Joint Research: 4 results,  Invited: 2 results)

  • [Journal Article] Ferulic Acid Suppresses Amyloid β Production in the Human Lens Epithelial Cell Stimulated with Hydrogen Peroxide.2017

    • Author(s)
      Nagai N, Kotani S, Mano Y, Ueno A, Ito Y, Kitaba T, Takata T and Fujii N.
    • Journal Title

      Biomed. Res. Int.

      Volume: - Pages: 1-9

    • DOI

      10.1155/2017/5343010

    • Related Report
      2016 Annual Research Report
    • Peer Reviewed / Open Access
  • [Journal Article] Isomeric Replacement of a Single Aspartic Acid Induces a Marked Change in Protein Function: The Example of Ribonuclease A2017

    • Author(s)
      Sakaue H, Kinouchi T, Fujii N, Takumi T, Fujii N.
    • Journal Title

      ACS Omega

      Volume: 2 Issue: 1 Pages: 260-267

    • DOI

      10.1021/acsomega.6b00346

    • Related Report
      2016 Annual Research Report
    • Peer Reviewed / Open Access
  • [Journal Article] Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.2016

    • Author(s)
      Serebryany E, Takata T, Erickson E, Schafheimer N, Wang Y, King JA.
    • Journal Title

      Protein science.

      Volume: 6 Issue: 6 Pages: 1115-1128

    • DOI

      10.1002/pro.2924

    • Related Report
      2016 Annual Research Report
    • Peer Reviewed / Int'l Joint Research
  • [Journal Article] New insight into the dynamical system of αB-crystallin oligomers2016

    • Author(s)
      R. Inoue, T. Takata, N. Fujii, K. Ishii, S. Uchiyama, N. Sato, Y. Oba, K. Wood, K. Kato, N. Fujii, and M. Sugiyama
    • Journal Title

      Scientific Reports

      Volume: 6 Issue: 1 Pages: 29208-29208

    • DOI

      10.1038/srep29208

    • NAID

      120006323745

    • Related Report
      2016 Annual Research Report
    • Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
  • [Journal Article] Isomerization of Asp residues plays an important role in αA-crystallin dissociation.2016

    • Author(s)
      Takata T, Fujii N.
    • Journal Title

      FEBS J.

      Volume: 283 Issue: 5 Pages: 850-859

    • DOI

      10.1111/febs.13635

    • Related Report
      2015 Research-status Report
    • Peer Reviewed / Acknowledgement Compliant
  • [Journal Article] Effect of Asp 96 isomerization on the properties of a lens αB-crystallin-derived short peptide.2015

    • Author(s)
      Takata T, Fujii N.
    • Journal Title

      J Pharm Biomed Anal.

      Volume: 116 Pages: 139-144

    • DOI

      10.1016/j.jpba.2015.06.017

    • Related Report
      2015 Research-status Report
    • Peer Reviewed
  • [Presentation] Age-related abnormal Asp isomers distribution in lens specific αA-crystallin monomeric and polymeric state2017

    • Author(s)
      Takumi Takata and Noriko Fujii
    • Organizer
      The 3rd International Conference of D-Amino Acid Research
    • Place of Presentation
      Varese, Italy
    • Year and Date
      2017-07-10
    • Related Report
      2016 Annual Research Report
    • Int'l Joint Research / Invited
  • [Presentation] Age-related abnormal Asp isomers distribution in lens specific αA-crystallin monomeric and polymeric state2016

    • Author(s)
      Takumi Takata, Takashi Sato, Hiroshi Sasaki and Noriko Fujii
    • Organizer
      XXII Biennial Meeting of the International Society for Eye Research
    • Place of Presentation
      Tokyo, Japan
    • Year and Date
      2016-09-25
    • Related Report
      2016 Annual Research Report
    • Int'l Joint Research / Invited
  • [Presentation] Age-related Asp Isomerization in Dissociated Alpha-crystallin from Aged Lens2016

    • Author(s)
      Takumi Takata, Takashi Sato, Noriko Fujii
    • Organizer
      ARVO 2016
    • Place of Presentation
      Seattle, USA
    • Year and Date
      2016-04-30
    • Related Report
      2015 Research-status Report
    • Int'l Joint Research
  • [Presentation] Isomerization of Asp residues is different between monomer and hetero-polymer of alpha-crystallin in aged human lens.2015

    • Author(s)
      T. Takata and N Fujii.
    • Organizer
      International Conference on the Lens 2015.
    • Place of Presentation
      Kona, USA
    • Year and Date
      2015-12-06
    • Related Report
      2015 Research-status Report
    • Int'l Joint Research
  • [Presentation] 加齢後のヒト水晶体内におけるαA-クリスタリン単量体内と会合体内のAsp異性化率の相違2015

    • Author(s)
      高田匠, 藤井紀子
    • Organizer
      第11回D-アミノ酸学会
    • Place of Presentation
      長岡
    • Year and Date
      2015-09-14
    • Related Report
      2015 Research-status Report

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Published: 2015-04-16   Modified: 2018-03-22  

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