• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to project page

2006 Fiscal Year Final Research Report Summary

Molecular basis for transglutaminase reaction in cornified layer of skin epidermis

Research Project

Project/Area Number 17580077
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Applied biochemistry
Research InstitutionNagoya University

Principal Investigator

KIYOTAKA Hitomi  Nagoya Univ., Graduate Sch.Bioagric Sci., Associate Prof., 大学院生命農学研究科, 助教授 (00202276)

Project Period (FY) 2005 – 2006
Keywordstransglutaminase / calcium / epidermis / cornified layer
Research Abstract

Transglutaminase (TGase) is a family of enzymes that catalyzes cross-linking reaction between two or identical proteins. In formation of skin epidermis, several structural proteins are cross-linked by TGase during differentiation. These reaction products are essential for cornification of the mature keratinocytes. For this cross-linking reaction, the mechanisms that TGase isozymes (TGase 1, TGase 3, and TGase 5) are activated in differentiated keratinocytes remained unclarified. Furthermore, how target substrate proteins are catalyzed by each enzyme is unknown. In this study, I searched the responsible enzyme for activation of TGase 3, a main cross-linking enzyme located in cytoplasm, using recombinant protein expressed in baculovirus-infected insect cells. As a result, two lysosome-proteases, cathepsins S and L appeared as activating protease (Chen et al. J.Biol.Chem., 2006). Since this activation is confirmed as in vitro reaction, in vivo mechanism for activation is necessary as future works. However, the acknowledgements contribute to identify substrate proteins for TGase 3. Additionally, I established the system to identify the substrate sequence by TGase (Sugimura et al. J.Biol.Chem., 2006). For establishment of the system, TGase 2 (tissue-type) and Factor XIII (TGase for blood coagulation) were used as target TGase. I successfully identified the motifs for each preferred substrate sequence. This system enables to provide information of substrate proteins that cross-linked by each TGase isozyme.

  • Research Products

    (12 results)

All 2006 2005 Other

All Journal Article (11 results) Patent(Industrial Property Rights) (1 results)

  • [Journal Article] Cystatin M/E is a high affinity inhibitor of cathepsin V and the short chain form of cathepsin L by a reactive site that is distinct from the legumain-binding site.2006

    • Author(s)
      Chen.et al.
    • Journal Title

      Journal of Biological Chemistry 281

      Pages: 15893-15899

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library2006

    • Author(s)
      Sugimura et al.
    • Journal Title

      Journal of Biological Chemistry 281

      Pages: 17699-17706

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Immunological Analysis of Epidermal-type Transglutaminase (TGase 3) in Epithelium.2006

    • Author(s)
      Hitomi et al.
    • Journal Title

      Animal Cell technology 14

      Pages: 339-345

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Cystatin M/E is a high affinity inhibitor of cathepsin V and the short chain form of cathepsin L by a reactive site that is distinct from the legumain-binding site2006

    • Author(s)
      Chen.et al.
    • Journal Title

      Journal of Biological Chemistry 281

      Pages: 15893-15899

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library2006

    • Author(s)
      Sugimura. et al.
    • Journal Title

      Journal of Biological Chemistry 281

      Pages: 17699-17706

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Transglutaminases in skin epidermis2005

    • Author(s)
      Hitomi
    • Journal Title

      European Journal of Dermatology 15/5

      Pages: 313-319

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] トランスグルタミナーゼによるタンパク質修飾2005

    • Author(s)
      人見清隆
    • Journal Title

      生化学 77巻6号

      Pages: 552-558

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] トランスグルタミナーゼによる低分子量Gタンパク質の機能制御2005

    • Author(s)
      和田文孝ら
    • Journal Title

      化学と生物 43巻10号

      Pages: 630-632

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Protein modification by transglutaminase (Japanese)2005

    • Author(s)
      Hitomi
    • Journal Title

      Journal of Biochemistry (Seikagaku) 77

      Pages: 552-558

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Regulation of G-protein by transglutaminases (Japanese)2005

    • Author(s)
      Wada
    • Journal Title

      Kagaku to Seibutsu 43

      Pages: 630-632

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Transglutaminases in skin epidermis

    • Author(s)
      Hitomi
    • Journal Title

      European Journal of Dermatology 5

      Pages: 313-319

    • Description
      「研究成果報告書概要(欧文)」より
  • [Patent(Industrial Property Rights)] トランスグルタミナーゼ基質反応性を有するペプチド及びその利用2006

    • Inventor(s)
      人見清隆, 杉村禎昭, 牧正敏
    • Industrial Property Rights Holder
      名古屋大学
    • Industrial Property Number
      2005-380040および2006-352448(優先権主張に伴う)
    • Filing Date
      2006-12-26
    • Description
      「研究成果報告書概要(和文)」より

URL: 

Published: 2008-05-27  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi