The mechanism of extracellular protein quality control by extracellular chaperone
| Project/Area Number |
26840047
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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) |
2014-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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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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| Outline of Final Research Achievements |
C-reactive protein (CRP) and serum amyloid P component (SAP), two major classical pentraxins in humans, are soluble pattern recognition molecules that regulate the innate immune system, but their chaperone activities remain poorly understood. CRP and SAP dose-dependently and substoichiometrically inhibited both amyloid β (1-40) and D76N β2-microglobulin fibril formation in a Ca2+-independent manner. Interestingly, in the presence of Ca2+, SAP first inhibited, then significantly accelerated D76N β2-m fibril formation. In conclusion, we obtained new insight into the chaperone activity of pentraxins, proposing that classical pentraxins (CRP, SAP) may be a member of extracellular chaperones.
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Report
(3 results)
Research Products
(8 results)
