Molecular Mechanism of Apoptosis by Amyloid β-Protein Fibrils Formed on Neuronal Cells

被引:43
作者
Takada, Eri [1 ]
Okubo, Kaori [1 ]
Yano, Yoshiaki [1 ]
Iida, Keiko [1 ]
Someda, Masataka [1 ]
Hirasawa, Akira [1 ]
Yonehara, Shin [1 ]
Matsuzaki, Katsumi [1 ]
机构
[1] Kyoto Univ, Grad Sch Pharmaceut Sci, Kyoto 6068501, Japan
来源
ACS CHEMICAL NEUROSCIENCE | 2020年 / 11卷 / 05期
关键词
Alzheimer's disease; amyloid beta-protein; toxic fibrils; apoptosis; inflammation; ALZHEIMERS-DISEASE; DEATH; INFLAMMASOME; RECEPTOR; FAS; PATHOLOGY; OLIGOMERS; PATHWAYS; SOFTWARE; PEPTIDE;
D O I
10.1021/acschemneuro.0c00011
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Aggregational states of amyloid beta-protein (A beta) are critical for its neurotoxicity, although they are not well characterized, particularly after binding to the cell membranes. This is one reason why the mechanisms of A beta neurotoxicity are controversial and elusive. In this study, the effects of toxic A beta-(1-42) fibrils formed in the membrane on cellular processes were investigated using human neuroblastoma SH-SY5Y cells. Consistent with previous observations, fibrillar A beta s formed on the membranes induced activation of caspase-3, the effector caspase for apoptosis. Knockdown analyses of the initiator caspases, caspase-8 and caspase-9, indicated that the apoptosis was induced via activation of caspase-8, followed by activation of caspase-9 and caspase-3. We also found that inflammation signaling pathways including Toll-like receptors and inflammasomes NOD-, LRR-, and pyrin domain-containing protein 3 are involved in the initiation of apoptosis by the A beta fibrils. These inflammation-related molecules are promising targets for the prevention of apoptotic cell death induced by A beta.
引用
收藏
页码:796 / 805
页数:19
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