| Project/Area Number |
62480246
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Psychiatric science
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| Research Institution | KITASATO UNIVERSITY |
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Principal Investigator |
TAMAI Yoichi KITASATO UNIVERSITY SCHOOL OF MEDICINE, Professor, 医学部, 教授 (80050441)
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| Co-Investigator(Kenkyū-buntansha) |
NAKAMURA Kazuo KITASATO UNIVERSITY SCHOOL OF MEDICINE, Research Associate, 医学部, 助手 (40189030)
MIURA Sadanori KITASATO UNIVERSITY SCHOOL OF MEDICINE, Professor, 医学部, 教授 (70050383)
OHTANI Yoshio KITASATO UNIVERSITY SCHOOL OF MEDICINE, Lecturer, 医学部, 講師 (40095500)
TAGUCHI Fumiaki KITASATO UNIVERSITY SCHOOL OF HYGIENIC SCIENCE, Professor, 衛生学部, 教授 (40050455)
KIJOMA Hisako KITASATO UNIVERSITY SCHOOL OF MEDICINE, Lecturer, 医学部, 講師 (90118810)
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 1988: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1987: ¥2,000,000 (Direct Cost: ¥2,000,000)
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| Keywords | CREUTZFELDT-JAKOB DISEASE / TRANSMISSIBLE AGENT / PRION / GANGLIOSIDE / DEACTIVATION OF CREUTZFELDT-JAKOB DISEASE AGENT / ELISA / ELISA法 / 亜急性硬化性全脳炎 / クロイツフェルト・ヤコブ病 |
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| Research Abstract |
1. To elucidate the possible relationship between the CJD infectivity and prion proceins, the CJD mouse brain was fractionated into ten fractions, and the infectivity was examined. The CJD infectivity was found not only in the prion fraction but also to comparable extent in the fractions that were free of prion protein. Thus, we concluded that prion proteins are not necessarily requisits for the CJD infectivity.
2. Microsomal fractions which had been found to contain the high CJD titer were solubilized with a detergent to obtain the more CJD agent-enriched fraction. The titration study is in progress.
3. The affinity of prion proteins with lipids were examined by the ELISA method. The total ganglioside extracts from rat brain and phosphatidyl ethanolamine were found to react with the synthetic prion peptides in the range of about 80% of the control. These findings may indicate that prion peptides require some lipid species to form their characteristic fibrillar structures.
4. To make the simple and convenient conditions for the deactivation of the CJD agent, a variety of procedures were tested. The complete inactivation was obtained by autoclaving at 121 C for 60 min after In NaOH treatment for 60 min and also by autoclaving at 131 C for 60 min.
5. Ganglisoside composition from the brain of a human case of subacute sclerosing panencephlitis and from the brain of zitter rat with genetic spongiform encephalopathy were investigated. The findings obtained indicate that the ganglioside composition in these two diseases were different from each other and also from that of CJD brain which had been reported. It was suggested, thus, that ganglioside alterations are specific to the respective diseases and closely related to their pathogenesis.
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