| Project/Area Number |
16390573
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
補綴理工系歯学
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| Research Institution | Fukuoka Dental College |
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Principal Investigator |
SATO Hironobu Fukuoka Dental College, Dentistry, Professor (00145955)
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| Co-Investigator(Kenkyū-buntansha) |
MATSUURA Takashi Fukuoka Dental College, Dentistry, Associate Professor (60330966)
TSUZUKI Takashi Fukuoka Dental College, Dentistry, Assistant Professor (70330967)
MATSUNAGA Tatsuaki Fukuoka Dental College, Dentistry, Assistant Professor (50389409)
KATAFUCHI Michitsuna Fukuoka Dental College, Dentistry, Research associate (90454933)
生山 隆 福岡歯科大学, 歯学部, 講師 (00389412)
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| Project Period (FY) |
2004 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥12,720,000 (Direct Cost: ¥12,000,000、Indirect Cost: ¥720,000)
Fiscal Year 2007: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
Fiscal Year 2006: ¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 2005: ¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 2004: ¥4,800,000 (Direct Cost: ¥4,800,000)
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| Keywords | osteoporosis / senescence-accelerated mouse / collagen / lysine / hydroxylation / mandible / bone morphometry / コラーゲン線維 / 骨基質 / リシン基の水酸化 / 骨質 / 大腿骨 / 皮質骨 / 海綿骨 / 骨芽細胞 / 破骨細胞 / リジルハイドロキシラーゼ / 骨髄 / アルカリフォスファターゼ / 老年性骨粗鬆症 / 変形性顎関節症 / 遺伝子発現 |
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| Research Abstract |
We investigated the mandibular bones of senile osteoporotic mice (SAMP6) by histological and biochemical analyses. With Comparison of their control mice (SAMR1), the, mandibular bones of SAMP6 exhibited lower bone quantity by histomorphometric analysis and thinner collagen fibrils in the bone matrix by transmission electron microscope analysis. The bone biochemical analysis showed the major extracellular matrix was type I collagen both in the two mice. Compared with SAMR1, the mandibular bones of SAMP6 showed lower content of collagen in the bone matrix but higher extent of hydroxylysine which was produced through a collagen posttransiation modification. Since it has been reported that higher lysine hydroxylation leads to thinner collagen fibril formation, the high level of lysine hydroxylation likely induces collagen fibrils thinner. As well, higher extent of lysine hydroxylation has been reported in the femoral bones of SAMP6 and osteoporotic patients. It is suggested that a collagen posttranslational modification, lysine hydroxylation, affects the quality of collagen, leading to low bone quality in osteoporosis.
This study indicates an osteoporotic bone nature in quantity and quality of the mandibular bones in senile osteoporotic mice. Accordingly, the jaw bones of osteoporotic patients may be speculated to exhibit lower quality as well as lower quantity. The further study may reveal and confirm bone nature of the jaw of osteoporotic patients and then the future genome study may enable confirmation of diagnostic technique of jaw bone quality and development of the according dental treatment technique.
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