1This work was supported by Wellcome Trust grant 067660 (DMW), NIH grant AG06173 (DJS and DMW) and by the Foundation for Neurologic Diseases.
Aβ Oligomers – a decade of discovery
Article first published online: 4 JAN 2007
Journal of Neurochemistry
Volume 101, Issue 5, pages 1172–1184, June 2007
How to Cite
Walsh, D. M. and Selkoe, D. J. (2007), Aβ Oligomers – a decade of discovery. Journal of Neurochemistry, 101: 1172–1184. doi: 10.1111/j.1471-4159.2006.04426.x
- Issue published online: 4 JAN 2007
- Article first published online: 4 JAN 2007
- Received November 8, 2006; revised manuscript received December 9, 2006; accepted December 9, 2006.
- Alzheimer’s disease;
- amyloid β-protein;
- synaptic dysfunction
Converging lines of evidence suggest that progressive accumulation of the amyloid β-protein (Aβ) plays a central role in the genesis of Alzheimer’s disease, but it was long assumed that Aβ 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 Aβ peptides, cell culture models, β-amyloid precursor protein transgenic mice and human brain to suggest that pre-fibrillar, diffusible assemblies of Aβ are also deleterious. Although the precise molecular identity of these soluble toxins remains unsettled, accumulating evidence suggests that soluble forms of Aβ 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.