2005 Fiscal Year Final Research Report Summary
The investigation of immunological mechanism of postinfectious acute cerebellar ataxia.
| Project/Area Number |
16590844
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Neurology
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| Research Institution | Kyorin University |
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Principal Investigator |
CHIBA Atsuro Kyorin University, Department of Neurology, Associate Professor, 医学部, 助教授 (30313133)
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| Co-Investigator(Kenkyū-buntansha) |
KUSUNOKI Susumu Kinki University, Department of Neurology, Professor, 医学部, 教授 (90195438)
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| Project Period (FY) |
2004 – 2005
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| Keywords | acute cerebellar ataxia / autoantibody / triose phosphate isomerase / Epstein-Barr virus / antigenic epitopes / glycolytic pathway |
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| Research Abstract |
We investigated serum autoantibodies in patients with acute cerebellar ataxia (ACA), identified an antigen molecule, and analyzed its epitopic region. In Western blot screening with SDS-extracted total protein fraction of the cerebellum, an IgM antibody reacting with about 26 kDa protein was detected. The protein was identified as triose phosphate isomerase (TPI), by N-terminal amino acid sequence analysis. IgM anti-TPI antibody was detected in 8 of 23 patients with ACA, and all of the antibody-positive patients developed ACA following Epstein-Barr virus (EBV) infection. In chronological studies of the antibody titer, it was already raised before neurological onset and seemed to reach a peak around the onset of ataxia. Immunization of rabbits with purified TPI induced IgG anti-TPI antibody promptly, but no animals manifested neurological abnormalities. In Western blot investigations with protein extracts from various tissues, anti-TPI antibodies in patients with ACA showed the tendency of the stronger reaction with TPI from the cerebellum than that from other tissues, compared with anti-TPI antibodies in the immunized animals. The patterns of reaction with protease-digested products of TPI were different between the patients with ACA and the immunized animals. These observations suggested that the epitopes recognized by anti-TPI antibodies were different between the two groups. N-terminal amino acid analyses of the recognized and non-recognized spots following two-dimensional electrophoretic separation of the protease-digested products revealed that a main immunogenic epitope to the anti-TPI antibodies in ACA patient following EBV infection was localized in C-terminal 80-100 amino acid region of TPI.
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