期刊
SCIENTIFIC REPORTS
卷 6, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/srep38187
关键词
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资金
- Bright Focus Foundation [A2014270S]
- Cure Alzheimer's Fund [128873]
- Jeane B. Kempner Fellowship
- Charles F. and Joanne Knight ADRC [NIH P50 AG05681, NIH P01 AG03991, NIH P01 AG026276]
- NIH [R01 NS065069]
Soluble amyloid-beta (A beta) aggregates likely contribute substantially to the dementia that characterizes Alzheimer's disease. However, despite intensive study of in vitro preparations and animal models, little is known about the characteristics of soluble A beta aggregates in the human Alzheimer's disease brain. Here we present a new method for extracting soluble A beta aggregates from human brains, separating them from insoluble aggregates and A beta monomers using differential ultracentrifugation, and purifying them >6000 fold by dual antibody immunoprecipitation. The method resulted in <40% loss of starting material, no detectible ex vivo aggregation of monomeric A beta, and no apparent ex vivo alterations in soluble aggregate sizes. By immunoelectron microscopy, soluble A beta aggregates typically appear as clusters of 10-20 nanometer diameter ovoid structures with 2-3 amino-terminal A beta antibody binding sites, distinct from previously characterized structures. This approach may facilitate investigation into the characteristics of native soluble A beta aggregates, and deepen our understanding of Alzheimer's dementia.
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