Project/Area Number |
60440085
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Research Category |
Grant-in-Aid for General Scientific Research (A)
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Allocation Type | Single-year Grants |
Research Field |
Functional basic dentistry
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Research Institution | TOKYO MEDICAL AND DENTAL UNIVERSITY |
Principal Investigator |
SASAKI Satoshi Professor, Dept. of Biochemistry, Faculty of Dentistry, Tokyo Med. and Dent. University, 歯学部生化学, 教授 (80013803)
|
Co-Investigator(Kenkyū-buntansha) |
SUZUKI Michiko Technical Assistant, Dept. of Biochemistry, Faculty of Dentistry, Tokyo Med. and, 歯学部生化学, 技官(教務) (80171255)
SHIMOKAWA Hitoyata Associate Professor, Dept. of Biochemistry, Faculty of Dentistry, Tokyo Med. and, 歯学部生化学, 助教授 (80014257)
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Project Period (FY) |
1985 – 1988
|
Project Status |
Completed (Fiscal Year 1988)
|
Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 1988: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1987: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1986: ¥2,300,000 (Direct Cost: ¥2,300,000)
|
Keywords | Dentin / Calcification / Phosphoprotein / プロテオグリカン / オステオネクチン / ホスホホリン / セリンリン酸 / β-脱離反応 |
Research Abstract |
Various non-collagenous components such as phosphophoryn, proteoglycans, osteonectin and serum alpha-2-HS-glycoprotein are known to be present in dentin matrix. These components are supposed to be related to the calcification mechanisms in dentin. In the present study we intended to isolate, purify and characterize non-collagenous proteins in dentin for the purpose of elucidation of their physiological roles. And, the following results were obtained. 1) The amount of the precipitates of calcium phosphate in agar gel system decreased when dentin phosphophoryn was added but an effect to produce a sharp band was observed. Dephosphorylated phosphophoryn had no effect. Distribution of this protein was different between deciduous and permanent teeth and between crown and root dentin. Dentinogenesis imperfecta dentin did not contain phosphophoryn. Biosynthesis of bovine phosphophoryn was identified by odontoblast incubation and immunoblotting. 2) Proteoglycans in dentin were analyzed in comparison to those in bone and the soft tissues. Immunological properties and structure of the core protein of low molecular weight proteoglycan in dentin and related tissues were clarified. This type of proteoglycan was also found in the soft tissues. 3) Amino acid sequence of dentin osteonectin was elucidated from base sequence of cDNA prepared by mRNA from odontoblasts and cloned by using monoclonal anti-osteonectin antibody. The sequence was identical to that of SPARC. The presence of this protein in various soft tissues was detected by immunohistochemical technics. These results suggest a possibility that non-collagenous components in dentin may play regulatory roles in development, differentiation and calcification process of the dentin formation.
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