GM1 ganglioside-mediated accumulation of amyloid β-protein on cell membranes

被引：108
作者：
Wakabayashi, M
Okada, T
Kozutsumi, Y
Matsuzaki, K [1 ]
机构：
[1] Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan
[2] Kyoto Univ, Grad Sch Biostudies, Sakyo Ku, Kyoto 6068501, Japan
[3] RIKEN Frontier Res Syst, Glycochain Express Lab, Wako, Saitama 3510198, Japan
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 328卷 / 04期
关键词：
amyloid beta-protein; ganglioside; cholesterol; Alzheimer's disease; lipid raft;
D O I：
10.1016/j.bbrc.2005.01.060
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：
The conversion of soluble, nontoxic amyloid beta-protein (Abeta) to aggregated, toxic Abeta is the key step in the development of Alzheimer's disease. Liposomal studies proposed that Abeta specifically recognizes a cholesterol-dependent cluster of monosialoganglioside GM1 and a conformationally altered form of Abeta promotes the aggregation of the protein. In this study, the accumulation of Abeta on living cells was investigated for the first time. The interaction of fluorescein-labeled Abeta (FL-Abeta) with rat pheochromocytoma PC12 cells was visualized using confocal laser microscopy. FL-Abeta was found to colocalize with GM1-rich domains oil cell membranes and to accumulate in a concentration- and time-dependent manner, leading to cytotoxicity. Cholesterol depletion significantly reduced Abeta accumulation. These observations corroborate the GM1-mediated Abeta accumulation model. (C) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码：1019 / 1023
页数：5
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