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Analyses of Physiological Functions of Protein-Modifying Enzyme Trabsglutaminase

Research Project

Project/Area Number 15580077
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Applied biochemistry
Research InstitutionKyoto Institute of Technology

Principal Investigator

IKURA Koji  Kyoto Institute of Technology, Faculty of textile Science, Professor, 繊維学部, 教授 (00101246)

Project Period (FY) 2003 – 2004
Project Status Completed (Fiscal Year 2004)
Budget Amount *help
¥3,900,000 (Direct Cost: ¥3,900,000)
Fiscal Year 2004: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 2003: ¥2,300,000 (Direct Cost: ¥2,300,000)
KeywordsProtein-modifying enzyme / Transglutaminase / Betaine-homocysteine methyltransferase / Homocysteine metabolism / 生理機能解析
Research Abstract

In order to elucidate physiological functions of protein-modifying enzyme transglutaminase at the molecular level, analyses of its protein substrates and interacting proteins were done, and ectopic gene expressing experiments using Drosophila as a model system were designed.
1.It was conmirmed that betaine-homocysteine S-methyltransferase(BHMT) can be a substrate of tissue-type transglutaminase by in vitro experiments using porcine liver BHMT and guinea pig liver transglutaminase. Primary amines were incorporated into BHMT by transglutaminase. In the absence of the primary amines, BHMT subunits were cross-linked intra- and intermolecularly. Glutamine residues of BHMT which are reactive for transglutaminase reaction were located in the region near the carboxyl terminal of BHMT subunit, BHMT activity was regulated repressively by the transglutaminase modification, specially by the cross-linking. This regulatory reaction might be involved in the regulation of homocysteine metabolism in the liver.
2.The experiments using immuno-affinity gel beads with monoclonal antibody to guinea pig liver transglutaminase suggested that a 55 kDa protein is a candidate of an interacting protein of tissue-type transglutaminase. Yeast two-hybrid experiments using Sos/Ras-relay system were done to detect proteins interacting with tissue-type transglutaminase in mouse liver. The results suggested that various proteins including enzymes and proteinase inhibitor can be candidates of interacting proteins. We also prepared materials to apply the two-hybrid experiments on human brain.
3.A search on the data-base of Drosophila gene (Fly Base) indicated that Drosophila has one transglutaminase gene and two splicing variants are transcribed from the gene. To make the GAL4-UAS expression system of transglutaminase in Drosophila, we are now subcloning the cDNA of Drosophila transglutaminase into pUASP vector.

Report

(3 results)
  • 2004 Annual Research Report   Final Research Report Summary
  • 2003 Annual Research Report

Research Products

(4 results)

All 2004 Other

All Journal Article (3 results) Publications (1 results)

  • [Journal Article] In vitro modification betaine-homocysteine S-methyltransferase by tissue-type transglutaminase2004

    • Author(s)
      Akira Ichikawa et al.
    • Journal Title

      The International Journal of Biochemistry and Cell Biology 36

      Pages: 1981-1992

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] In vitro modification betaine-homocysteine S-methyltransferase by tissue-type transglutaminase2004

    • Author(s)
      Akira Ichikawa et al.
    • Journal Title

      The International Journal of Biochemistry and Cell Biology Vol.36, No.10

      Pages: 1981-1992

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] In vitro modification betaine-homocysteine S-methyltransferase by tissue-type transglutaminase2004

    • Author(s)
      Akira Ichikawa et al.
    • Journal Title

      The International Journal of Biochemistry and Cell Biology 36・10

      Pages: 1981-1992

    • Related Report
      2004 Annual Research Report
  • [Publications] Akira Ichikawa et al.: "In Vitro Modification of Betaine-Homocysteine S-Methyltransferase by Tissue-Type Transglutaminase"International Journal of Biochemistry and Cell Biology. (印刷中). (2004)

    • Related Report
      2003 Annual Research Report

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Published: 2003-03-31   Modified: 2016-04-21  

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