期刊
JOURNAL OF NEUROCHEMISTRY
卷 101, 期 5, 页码 1172-1184出版社
WILEY
DOI: 10.1111/j.1471-4159.2006.04426.x
关键词
aggregation; Alzheimer's disease; amyloid beta-protein; oligomerization; synaptic dysfunction
资金
- NATIONAL INSTITUTE ON AGING [R01AG006173, R37AG006173] Funding Source: NIH RePORTER
- NIA NIH HHS [AG06173] Funding Source: Medline
- Wellcome Trust [067660] Funding Source: Medline
Converging lines of evidence suggest that progressive accumulation of the amyloid beta-protein (A beta) plays a central role in the genesis of Alzheimer's disease, but it was long assumed that A beta had to be assembled into extracellular amyloid fibrils to exert its cytotoxic effects. Over the past decade, data have emerged from the use of synthetic A beta peptides, cell culture models, beta-amyloid precursor protein transgenic mice and human brain to suggest that pre-fibrillar, diffusible assemblies of A beta are also deleterious. Although the precise molecular identity of these soluble toxins remains unsettled, accumulating evidence suggests that soluble forms of A beta are indeed the proximate effectors of synapse loss and neuronal injury. Here we review recent progress in understanding the role of soluble oligomers in Alzheimer's disease.
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