Aß-ganglioside interactions in the pathogenesis of Alzheimer's disease.

It is widely accepted that the abnormal self-association of amyloid ß-protein (Aß) is central to the pathogenesis of Alzheimer's disease, the most common form of dementia. Accumulating evidence, both in vivo and in vitro, suggests that the binding of Aß to gangliosides, especially monosialoganglioside GM1, plays an important role in the aggregation of Aß. This review summarizes the molecular details of the binding of Aß to ganglioside-containing membranes and subsequent structural changes, as revealed by liposomal and cellular studies. Furthermore, mechanisms of cytotoxicity by aggregated Aß are also discussed.