Immune targeting of apolipoprotein E in amyloid deposits ; a fundamental study using murine model
| Project/Area Number |
15590496
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Laboratory medicine
|
|---|
| Research Institution | JICHI MEDICAL SCHOOL (2005)
Juntendo University (2003-2004) |
|---|
Principal Investigator |
YAMADA Toshiyuki JMS, School of Medicine, Associate Professor, 医学部, 助教授 (50211636)
|
|---|
| Project Period (FY) |
2003 – 2005
|
| Project Status |
Completed (Fiscal Year 2005)
|
| Budget Amount *help |
¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 2005: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2004: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2003: ¥1,000,000 (Direct Cost: ¥1,000,000)
|
|---|
| Keywords | amyloidosis / apolipoprotein E / monoclonal antibody / inflammation / tracer experiment / mouse model / knock-in-mouse / immune targeting / アポリポ蛋白E / 診断法 / イメージング |
|---|
| Research Abstract |
Amyloidosis is usually diagnosed histologically on biopsy specimens. However, this approach is not only invasive but also is unable to evaluate the amount and localization of amyloid deposits in the whole body. Apolipoprotein (apoE) is known to be present in the deposits. Aiming to develop the new diagnostic tool, in this study, apoE was focused as a target. Human apoE expressing mouse and a monoclonal antibody recognizing human apoE fragment were utilized.
Labeled antibody efficiently bound to the deposits in vivo and its localization in the deposits was confirmed immunohistochemically. However, high background of administered radioactivity could not follow the imaging study. The plasma half life of the antibody was not shortened in the amyloidotic mouse. Administration of antibody did not prevent the mouse from amyloidosis development or enhance the absorption of already present amyloid deposits.
These results indicate that the strategy itself is reasonable but the antibody may be improved to have the stronger affinity with the amyloid deposits.
|
Report
(4 results)
Research Products
(20 results)
