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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2013.1
- 수록면
- 21 - 33 (13page)
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Formation of amyloid-${\beta}$ ($A{\beta}$) aggregates is a core process in the pathogenesis of Alzheimer's disease. Importance of interaction of the length variants, $A{\beta}42$ and $A{\beta}40$ in the process and consequent cytotoxicity has been pointed out for wild-type $A{\beta}$ previously. In addition to confirming the findings, the current study demonstrates that the potential interaction is also important for cytotoxicity of the Flemish and Dutch sequence variants. The interaction could strengthen or inhibit cytotoxicity of $A{\beta}42/A{\beta}40$ mixture, depending on interaction time of the length variants as well as the ratio and amyloidogenic property. The inhibitory effect was prominent at the early stage of aggregate formation in less amyloidogenic Flemish $A{\beta}42/A{\beta}40$ mixture, while strengthened cytotoxicity was exhibited at the stage in potently amyloidogenic Dutch variant and at the later stage in wild-type and the Flemish variant. The samples showing relatively robust cytotoxicity were those enriched in $A{\beta}$ protofibril-like structures, implying strong correlation of the structure with cytotoxicity. The different consequence of the interaction on sequence variants is likely due to differential amyloidogenic property of each $A{\beta}40$ variant, rather than that of $A{\beta}42$, because aggregation rates and levels of $A{\beta}40$ variants are greatly variable depending on the sequence, compared to $A{\beta}42$ variants. These studies may highlight a potential role of $A{\beta}40$ in the cytotoxicity, providing a novel mechanistic insight into the pathogenesis of each FAD-associated variant.
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