Structure and function of chemotactic factor, C5a, and its receptor
| Project/Area Number |
03670211
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
細菌学
|
|---|
| Research Institution | Osaka University |
|---|
Principal Investigator |
TAKEDA Junji Osaka University Research Institute for Microbial Diseases, 微生物病研究所, 助教授 (50163407)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
KINOSHITA Taroh Osaka University Research Institute for Microbial Diseases, 微生物病研究所, 教授 (10153165)
|
|---|
| Project Period (FY) |
1991 – 1992
|
| Project Status |
Completed (Fiscal Year 1992)
|
| Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1992: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1991: ¥1,100,000 (Direct Cost: ¥1,100,000)
|
|---|
| Keywords | Complement / C5a / Chemotactic activity / Monoclonal antibody / Epitope / 補体活性化フラグメントC5a / モノクロ-ナル抗体 / エピト-プマッピッグ |
|---|
| Research Abstract |
C5a is a potent chemotactic peptide derived from complement C5. C5a is immediately inactivated to C5a des Arg by carboxypeptidase N after activation of complement. Physiological C5a action occur through C5a receptor on phagocytic cells. In this study, we determined epitopes on C5a to understand the role of C5a using series of anti C5a monoclonal antibodies and N-terminal or C-terminal oligopeptides from C5a. Bindings between C5a des Arg and anti C5a monoclonal antibody were not inhibited by either N-terminal or C-terminal oligopeptides. However C-terminal oligopeptides without Arg could inhibit binding between C5a des Arg and some anti C5a monoclonal antibodies. These results demonstrate that some anti C5a monoclonal antibodies can recognize C-terminal peptide only without Arg.
|
Report
(3 results)
Research Products
(10 results)
