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Pathobiological role of 36 kDa microfibril-associated glycoprotein in Smith-Magenis syndrome.

Research Project

Project/Area Number 09470044
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field Pathological medical chemistry
Research InstitutionKagawa Medical University

Principal Investigator

KOBAYASHI Ryoji  Kagawa Medical University, Faculty of Medicine, Professor, 医学部, 教授 (00020917)

Co-Investigator(Kenkyū-buntansha) SUGANUMA Tatsuo  Miyazaki Medical College, Faculty of Medicine, Professor, 医学部, 教授 (60115350)
OKABE Akinobu  Kagawa Medical University, Faculty of Medicine, Professor, 医学部, 教授 (20093677)
MAETA Hajime  Kagawa Medical University, Faculty of Medicine, Professor, 医学部, 教授 (00075508)
前田 肇  香川医科大学, 医学部, 教授 (20294754)
Project Period (FY) 1997 – 1998
Project Status Completed (Fiscal Year 1998)
Budget Amount *help
¥8,300,000 (Direct Cost: ¥8,300,000)
Fiscal Year 1998: ¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 1997: ¥5,100,000 (Direct Cost: ¥5,100,000)
Keywordsextracellular matrix protein / Ca^<2+> binding protein / Smith-Magenis syndrome / elasith / EF hand protein / blood vessel / microfibril / inhibitor / 36kDa MAGP / Smith-Magenis症候群 / ミクロフィブリン
Research Abstract

A new extracellular matrix protein of 36 kDa has been purified from bovine and porcine aorta. The protein, 36 kDa microfibril associated glycoprotein (36kDa - MAGP), has a fibrinogen - like domain and contained the sequence Arg - Gly - Asp in the N - terminal region, which is the site for the association with cell and extracellular matrix. Immunoelection microscopy specified its location to elastin - microfibrils.
Using Ca^<2+> - dependent affinity chromatography on an isoquinoline sulfonamide (CKA 1303 ) coupled agarose, we obtained pure form of 36 kDa -MAGP.This compound should serve as a useful tool for clarifying the physiological roles of 36 kDa - MAGP.During the synthesis and selection of S - 100 protein antagonists derived from cinnamic acid and anthranilic acid, we discovered that N - acetyl anthranilic acid and O - (3', 4' - dimethoxy cinnamoyl) salicilic acid strongly bind to 36kDa-MAGP.

Report

(3 results)
  • 1998 Annual Research Report   Final Research Report Summary
  • 1997 Annual Research Report
  • Research Products

    (14 results)

All Other

All Publications (14 results)

  • [Publications] Jin L.: "Localization of calbindin-D28k in normal and incised mouse skin: immunohistochemical and immunoblot analysis" Arch.Derm.Res.289. 578-584 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Oyama Y.: "Two distinct anti-allergic drugs, amIexanox and cromolyn, bind to the same kinds of calcium binding proteins, except calmodulin, in bovine lung extract." Biochem.Biophys.Res.Commun.240. 341-347 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Shishibori T.: "Three distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein family." Biochem J.338. 583-589 (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Yamashita K.: "Purification of Bovine S100A12 from Recombinant Escherichia coli." Protein Expr.Purif.(in press). (1999)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Jin L, Miyamoto O, Toyoshima T, Kobayashi R, Murakami TH, Itano T: "Localization of calbindin-D28k in normal and incised mouse skin : immunohistochemical and immunoblot analysis." Arch.Derm.Res.289. 578-584 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Oyama.Y, Shishibori T, Yamashita K, Naya T, Nakagiri S, Maeta H, Kobayashi R: "Two distinct anti-allergic drugs, amlexanox and cromolyn, bind to the same kinds of calcium binding proteins, except calmodulin, in bovine lung extrat." Biochem.Biophys.Res.Commun.240. 341-347 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Shishibori T, Oyama Y, Matsushita O, Yamashita K, Furuichi H, Okabe A, Maeta H, Hata Y, Kobayashi R: "Three distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein family." Biochem.J.15 ; 338. 583-589 (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Yamashita K, Oyama Y, Shihibori T, Matsushita O, Okabe A, Kobayashi R: "Purification of Bovine S100A12 from Recombinant Escherichia coli." Protein Expr.Purif.(in press). (1999)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Shishibori T.: "Three distinct anti-allergic drugs,amlexanox,cromolyn and tranilast,bind to S100A12 and S100A13 of the S100 protein family." Biochem J.338. 583-589 (1999)

    • Related Report
      1998 Annual Research Report
  • [Publications] Yamashita K.: "Purification of Bovine S100A12 from Recombinant Escherichia coli." Protein Expr.Purif.(in press). (1999)

    • Related Report
      1998 Annual Research Report
  • [Publications] Jin L.: "Localization of calbindin-D28k in normal and incised mouse skinimmunohistochemical and immunoblot analysis." Arch.Derm.Res.289. 578-584 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] Oyama Y.: "Two distinct anti-allergic drugs,amlexanox and cromolyn,bind to the same kinds of calcium binding proteins,except calmodulin,in bovine lung extract." Biochem.Biophys.Res.Commun.240. 341-347 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] 小林良二: "レセプター・分子薬理学的アプローチ" 講談社サイエンティフィック, 19 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] 小林良二: "廣川タンパク質化学6巻-細胞骨格と筋肉のタンパク質" 廣川書店, 6 (1997)

    • Related Report
      1997 Annual Research Report

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Published: 1997-04-01   Modified: 2016-04-21  

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