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Keratan sulphate proteoglycans associated with the bone formation of embryonic chick femurs

Research Project

Project/Area Number 08672099
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Morphological basic dentistry
Research InstitutionNihon University

Principal Investigator

TAKAGI Minoru  Nihon University School of Dentistry Professor, 歯学部, 教授 (90060061)

Co-Investigator(Kenkyū-buntansha) SHIGEMASA Kayoko  Nihon University School of Dentistry Research Associate, 歯学部, 助手 (30059604)
MAENO Masao  Nihon University School of Dentistry Associate Professor, 歯学部, 助教授 (60147618)
Project Period (FY) 1996 – 1997
Project Status Completed (Fiscal Year 1997)
Budget Amount *help
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1997: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1996: ¥900,000 (Direct Cost: ¥900,000)
Keywordsbone / chick embryo / glycosaminoglycan / proteoglycan / keratan sulphate / immunohistochemistry / Western blot / 骨 / 鶏胚 / グリコサミノグリカン / ケラタン硫酸 / プロテオグリカン
Research Abstract

The type and sistribution of sulphated proteoglycans (PGs) in the midshaft subperiosteal bone of 15-18-day embryonic chick femurs were studied immunocytochemically and biochemically, using four monoclonal antibodies (MAb 2B6, 3B3, 1B5, and 5D4). These MAb specifically recognize epitopes in chondroitin 4-sulphate (C4-S) and dermatan sulphate (DS) ; chondroitin 6-sulphate (C6-S) and unsulphated chondroitin (C0-S) ; C0-S ; and keratan sulphate (KS) respectively. Immunohistochemistry showed that staining of C4-S, DS, and KS, but not of C6-S and C0-S, was limited to osteoid, the cell surface of osteocytes, and to the walls of osteocytic lacunae and bone canaliculi in 15-18-day embryonic specimens. However, no significant difference in the distribution and intensity of immunostaining was observed in these specimens. Bone proteins were extracted from fresh 18-day embryonic specimens with a three extraction procedure, 4 M guanidine HCl (GdnCl, G-1 extract), 0.4M EDTA (E-ectract), followed by GdnCl (G-2extract), to characterize mineral binding and collagenous matrix associated PGs in E-and G2-extracts respectively. Western blot analysis of E-and G2-extracts demonstrated that chondroitinase ABC-digested PGs with a molecular weight (M_r) approximately of 45,000 containing GAGs predominantly corresponding to C4-S and/or DS, with no detectable C6-S or C0-S present in the mineral and matrix phase, whereas KSPGs having an M_r of approximately 72,000 are only present in the mineral phase. These results indicate that embryonic chick bone contains small PGs having C4-S, DS, and KS chains with preferential localization to osteoid, the cell surface of osteocytes, and to the walls of osteocytic lacunac and bone canaliculi.

Report

(3 results)
  • 1997 Annual Research Report   Final Research Report Summary
  • 1996 Annual Research Report
  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] Minoru Takagi et al.: "Immunohistochemical and biochemical characterization of sulphated proteoglycans in embryonic chick bone" Journal of Nihon University School of Dentsitry. 39・3. 156-163 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Minoru Takagi, Yohan Ono, Masao Maeno, Kunihiro Miyashita, and Kazuhiro Omiya.: "Immunohistochemical and biochemical characterization of sulphated proteoglycans in embryonic chick bone." J Nihon Univ Sch Dent. 39-3. 156-163 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] Minoru Takagi et al.: "Immunohistochemical and biochemical characterization of sulphated proteoglycans in embryonic chick bone" Journal of Nihon University School of Dentsitry. 39・3. 156-163 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] 小野世範,重政香代子,高城 稔: "鶏胚大腿骨のグリコサミノグリカンについて" 解剖学雑誌. (1997)

    • Related Report
      1996 Annual Research Report

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Published: 1996-04-01   Modified: 2016-04-21  

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