期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 496, 期 2, 页码 84-92出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2010.02.001
关键词
Beta amyloid; Oligomers; Fibrils; Neurons; Cell death; Atomic force microscopy; Dynamic light scattering; Fluorescence correlation spectroscopy
资金
- Lithuanian State Science and Studies Foundation [B38]
- NIH [AG032131]
- American Health Assistance Foundation [A2008-307]
The link between the size of soluble amyloid beta (A beta) oligomers and their toxicity to rat cerebellar granule cells (CGC) was investigated. Variation in conditions during in vitro oligomerization of A beta(1-42) resulted in peptide assemblies with different particle size as measured by atomic force microscopy and confirmed by dynamic light scattering and fluorescence correlation spectroscopy. Small oligomers of A beta(1-42) with a mean particle z-height of 1-2 nm exhibited propensity to bind to phospholipid vesicles and they were the most toxic species that induced rapid neuronal necrosis at submicromolar concentrations whereas the bigger aggregates (z-height above 4-5 nm) did not bind vesicles and did not cause detectable neuronal death. A similar neurotoxic pattern was also observed in primary cultures of cortex neurons whereas A beta(1-42) oligomers, monomers and fibrils were non-toxic to glial cells in CGC cultures or macrophage J774 cells. However, both oligomeric forms of A beta(1-42) induced reduction of neuronal cell densities in the CGC cultures. (C) 2010 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据