지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2013.1
- 수록면
- 220 - 233 (14page)
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초록· 키워드
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Amyloid-${\beta}$ peptide ($A{\beta}$), implicated in Alzheimer's disease, associates into the fibrils that deposit in senile plaque. The 39~43 amino acid long peptide assemble into various species which could be regulated by chaperone molecules. Despite extensive progress, the results are conflicting; for example, both reduction and enhancement of $A{\beta}$ cytotoxicity by chaperone have been reported. And the relationship of $A{\beta}$ structural species with chaperone, and further its implication in cytotoxicity remain to be elucidated. To address this question and to understand the underlying mechanism(s), in this study, the effect of a chaperone molecule, DnaK, on $A{\beta}$ structure and its effect on cytotoxicity were investigated under several different conditions. A significant amount of oligomeric species of $A{\beta}$ that is believed to be more toxic among $A{\beta}$ structures was accumulated at 0.01~0.1 ratio of DnaK/abeta42, while such accumulation was not observed with higher ratio, where the oligomers appeared in the form of complexes with the chaperone molecules. Importantly, accumulation of these $A{\beta}$ oligomers exerted enhanced toxicity concomitantly and, in contrast, cytoprotection was observed at excess molar of DnaK. In all conditions, fibrillar forms were markedly inhibited. Further, fibrillization kinetics indicated that DnaK might affect on nucleation step, while circular dichroism spectroscopy demonstrated that DnaK delayed overall ${\beta}$-sheet formation. Taken together, results indicate that the chaperone influences $A{\beta}$ structural transition from oligomer to fibrillar structures as well as from monomer to oligomer with variable rates, and as results, it decreased or increased the amount of $A{\beta}$ oligomer as well as the cytotoxicity.
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