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Analysis of functional domains within adhesive proteins with the aim of controlling the interaction between cells and collagens

Research Project

Project/Area Number 03454498
Research Category

Grant-in-Aid for General Scientific Research (B)

Allocation TypeSingle-year Grants
Research Field 医学一般
Research InstitutionTokyo Institute of Technology

Principal Investigator

SAITO Yuji  Tokyo Institute of Technology, Department of Biological Sciences, Associate Professor, 生命理工学部, 助教授 (30134810)

Co-Investigator(Kenkyū-buntansha) TAKAGI Junichi  Tokyo Institute of Technology, Department of Biological Sciences, Assistant Prof, 生命理工学部, 助手 (90212000)
Project Period (FY) 1991 – 1993
Project Status Completed (Fiscal Year 1993)
Budget Amount *help
¥6,400,000 (Direct Cost: ¥6,400,000)
Fiscal Year 1993: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1992: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1991: ¥4,700,000 (Direct Cost: ¥4,700,000)
Keywordscollagen / von Willebrand factor / propolypeptide / blood coagulation factor XIIIa / laminin / thrombospondin / トロンボスポンジン / 血小板凝集 / ホスホリパーゼA_2 / Fc受容体 / デカペプチド / コラ-ゲン / 単クロ-ン抗体 / リシルエンドペプチダ-ゼ
Research Abstract

Collagen is one of the most common proteins found in extra-cellular matrix (ECM). In ECM there are proteins like collagen which are inherently present there as ECM proteins, and there are proteins which are associated with these ECM proteins and exert respective functions in the associated state. We have been interested in the latter kind of proteins and have been trying to locate the functional domains within these proteins. Followings are the main findings we have made from the research carried out during the last three years using this research grant.
(1). We isolated a protein from platelets bound to type I collagen. We identified this protein by N-terminal amino acid sequence analyses as propolypeptide of von Willebrand factor (pp-vWF) which had been called von Willebrand antigen II.
(2). We succeeded in narrowing down the collagen binding domain to a ten-residue portion Trp620-Ser629 out of 843 amino acid residues.
(3). As the mature von Willebrand factor which is derived from the c … More ommon precursor for pp-vWF is also known to bind to type I collagen, we made a comparison between these two proteins in terms of binding characteristics to the collagen. We came to a conclusion that they recognize different sites in the collagen molecule for the binding.
(4). We found that pp-vWF was present not only in alpha-granules but also on the surface of platelets. This may indicate that it plays a role during the adhesion of platelets to collagen present in subendothelium.
(5). We found pp-vWF cross-linked to an ECM protein laminin via blood coagulation factor XIIIa or tissue transglutaminase.
(6). We then investigated another collagen-binding protein thrombospondin (TSP). TSP was different from pp-vWF in that it preferentially bound to native type V collagen, rather than type I collagen unlike pp-vWF.As we have a future plan of making a comparison between these two collagen binding domains, we studied the type V collagen-binding domain of TSP.We were able to locate the domain to a portion comprised of 80 amino acid residues out of the 450-kDa molecule. Less

Report

(4 results)
  • 1993 Annual Research Report   Final Research Report Summary
  • 1992 Annual Research Report
  • 1991 Annual Research Report
  • Research Products

    (17 results)

All Other

All Publications (17 results)

  • [Publications] T.Usui: "Propolypeptide and mature portions of von Willebrand factor recognize different sites of type I collagen" European Journal of Biochemistry. 205. 363-367 (1992)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] J.Takagi: "A collagen/gelatin-binding decapeptide derived from bovine propolypeptide of von Willebrand factor" Biochemistry. 31. 8530-8534 (1992)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] K.Hashimoto: "Activation of phospholipases in platelets by polyclonal antibodies against a surface membrane protein" Biochimica Biophysica Acta. 1165. 27-31 (1992)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] T.Usui: "Propolypeptide of von Willebrand factor serves as a substrate for Factor XIIIa and is cross-linked to laminin" Journal of Biological Chemistry. 268. 12311-12316 (1993)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] J.Takagi: "A single chain 19-kDa fragment from bovine thrombospondin binds to type V collagen and heparin" Journal of Biological Chemistry. 268. 15544-15549 (1993)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] T.Usui, T.Fujisawa, J.Takagi and Y.Saito: "Propolypeptide and mature portions of von Willebrand factor recognize different sites of type I collagen." Eur. J.Biochem.205. 363-367 (1992)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] J.Takagi, H.Asai and Y.Saito: "A collagen/gelatinbinding decapeptide derived from bovine propolypeptide of von Willebrand Factor." Biochemistry. 31. 8530-8534 (1992)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] K.Hashimoto, F.Sekiya, J.Takagi, T.Tsukada, F.Sato and Y.Saito: "Activation of phospholipases in platelets by polyclonal antibodies against a surface membrane pro" Biochem. Biophys. Acta. 1165. 27-31 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] T.Usui, J.Takagi and Y.Saito: "Propolypeptide of von Willebrand factor serves as a substrate for factor XIIIa and is cross-linked to laminin." J.Biol. Chem.268. 12311-12316 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] J.Takagi, T.Fujisawa, T.Usui, T.Aoyama and Y.Saito: "A single chain 19-kDa fragment from bovine thrombospondin binds to type V collagen and heparin." J.Biol. Chem.268. 15544-15549 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1993 Final Research Report Summary
  • [Publications] J.Takagi: "A single chain 19-kDa fragment from bovine thrombospondin binds to type V collagen and heparin." The Journal of Biological Chemistry. 268. 15544-15549 (1993)

    • Related Report
      1993 Annual Research Report
  • [Publications] T.Usui: "Propolypeptide of von Willebrand factor serves as a substrate for factor XIIIa and is cross-linked to laminin." The Journal of Biological Chemistry. 268. 12311-12316 (1993)

    • Related Report
      1993 Annual Research Report
  • [Publications] Tomoko Usui: "Propolypetide and mature portions of von Wellebrand factor of bovine origin recognize different sites on type-I collagen obtained from bovine tendon" European Journal of Biochemistry. 205. 363-367 (1992)

    • Related Report
      1992 Annual Research Report
  • [Publications] Keiko Hashimoto: "Activation of phospholipases in platelets by polyclonal antibodies against a surface membrane protein" Biochimica et Biopysica Acta. 1165. 27-31 (1992)

    • Related Report
      1992 Annual Research Report
  • [Publications] Junichi Takagi: "A collagen/gelatin-binding decapeptide from bovine propolypeptide of von Willebrand factor" Biochemistry. 31. 8530-8534 (1992)

    • Related Report
      1992 Annual Research Report
  • [Publications] Junichi Takagi: "Collagenーbinding Domain within Bovine Propolypeptide of von Willebrand Factor" Journal of Biological Chemistry. 266. 5575-5579 (1991)

    • Related Report
      1991 Annual Research Report
  • [Publications] Tomoyuki Fujisawa: "Monoclonal antibodies that inhibit binding of propolypetide of von Willebrand factor to collagenーLocalization of epitopesー" European Journal of Biochehemistry. 196. 673-677 (1991)

    • Related Report
      1991 Annual Research Report

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Published: 1991-04-01   Modified: 2016-04-21  

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