| Project/Area Number |
13460092
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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 |
Fisheries chemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
YANO Tomoki Kyushu University, Faculty of Agriculture, Professor, 大学院・農学研究院, 教授 (90038266)
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| Co-Investigator(Kenkyū-buntansha) |
NAKAO Miki Kyushu University, Faculty of Agriculture, Assistant Professor, 大学院・農学研究院, 助手 (50212080)
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| Project Period (FY) |
2001 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥15,400,000 (Direct Cost: ¥15,400,000)
Fiscal Year 2003: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2002: ¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 2001: ¥10,000,000 (Direct Cost: ¥10,000,000)
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| Keywords | Fish / complement / innate immunity / C3d / adaptive immunity / CR2 / receptor / diversity / コイ / 硬骨魚類 / 分子クローニング |
|---|
| Research Abstract |
In mammals, an activation fragment(C3d) of the third complement component(C3) plays a crucial role in supporting nomal humoral immune responces, by stimulating B cells thrugh a specific receptor termed CR2. In the present study, we have examined if the adaptive immunity-regulatory effect is conserved in bony fish. First, we have analyzed physiolocial brakedown of carp C3 in serum activated by zymosan, and found that carp C3 generates a fragment equivalent to human C3d. It was also demonstrated that both C3-H1 and C3-S isoforms of carp C3 are fragmented into C3d. Next we have constructed expression vectors for fusion proteins of glutathione-S-transferase(GST) and C3d, and succeeded to prepare the recombinant proteins. Using the GST-C3d protein as a probe, we have attemted to detect receptors that recognize carp C3d fragment on carp peripheral lymphocytes. As a result, we observed significant and specific binding of GST-C3d to the lymphocytes. Anti-carp C3 rabbit IgG, but not EDTA, inhibited the binding, suggesting that carp lymphocytes carry receptors specific for C3d. The divalent-independent nature agrees well with that of mammalian CR2.
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