Mechanisms involved in inhibition of osteoclast formation by beta-glucan
| Project/Area Number |
15K11263
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Surgical dentistry
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| Research Institution | Kyushu Dental College |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | 破骨細胞 / curdlan / dectin-1 / オートファジー / spleen tyrosine kinase / エンドサイトーシス / PI3-kinase / cudrlan |
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| Outline of Final Research Achievements |
In the previous study, we have demonstrated that the dectin-1 agonsist curdlan inhibits osteoclast formation through autophagy-induced Syk protein degradation.
To clarify the detailed molecular mechanisms of curdlan on osteoclast formation, we examined the Syk expression in dectin-1 over expressing RAW264.7 cells (d-RAWs) and observed the time-dependent Syk protein degradation in the presence of curdlan. Pretreatment with the autophagy/lysosome inhibitor, bafilomycin A1 markedly blocked the Syk degradation induced by curdlan. We also found that curdlan stimulation increased and autolysosome formation and the expression of autophagy marker, LC3-II. These results indicate that autophagy plays an important role in inhibition of osteoclast formation by curdlan via degradation of Syk protein. Furthermore, present study revealed that activation of phosphoinositide 3-kinase and internalization of curdlan-dencti-1 complex are required for the curdlan-induced syk degradation in d-RAWs.
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Report
(4 results)
Research Products
(24 results)
