The inhibition mechanism of protein aggregation by extracellular chaperone
| Project/Area Number |
24770150
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
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| Research Institution | University of Fukui |
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Principal Investigator |
OZAWA Daisaku 福井大学, テニュアトラック推進本部, 助教 (60554524)
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| Research Collaborator |
NAIKI Hironobu 福井大学, 医学部, 教授 (10227704)
HASEGAWA Kazuhiro 福井大学, 医学部, 助教 (60324159)
OOKOSHI Tadakazu 福井大学, 医学部, 助教 (90362037)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2013: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2012: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | シャペロン / 蛋白質品質管理 / アミロイド / アミロイドーシス |
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| Research Abstract |
To reveal the inhibition mechanism of protein aggregation by extracellular chaperone, we searched for new extracellular chaperone and examined its function. Serum amyloid P component and C-reactive protein are members of the pentraxin family of cyclic pentameric protein. These proteins inhibited various amyloid fibril formations in the presence and absence of calcium. Moreover, serum amyloid P component bound to amyloid fibrils and suppressed the cytotoxicity induced by amyloid fibrils. These results suggest that serum amyloid P component and C reactive protein play an important role as new extracellular chaperones that inhibit protein aggregation in vivo.
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Report
(3 results)
Research Products
(10 results)
