Attack on amyloid.

Introduction At this meeting, recent breakthrough findings on the molecular mechanisms, animal models and, in particular, the therapy of Alzheimer’s disease (AD), and the second most common chronic neurodegenerative disorder Parkinson’s disease (PD), were discussed. Both illnesses are paradigmatic for an expanding class of late-onset diseases that are characterized by brain deposits of misfolded proteins. The cross-β-sheet conformation of these pathologically misfolded proteins is a common biophysical feature of aggregation diseases. Specific dyes (such as thioflavin S) selectively bind to such so-called amyloid structures, irrespective of the individual protein that aggregates in each ‘amyloidosis’. In the case of AD, the hallmark lesions are extracellular plaques composed of amyloid-β peptides (Aβ) that are derived from a larger Aβ precursor protein (APP; Fig. 1) and neurofibrillary tangles (NFTs) formed by the microtubule-associated protein tau. Furthermore, the presynaptic protein α-synuclein (α-SYN) fibrillizes into Lewy bodies (LBs), which are diagnostic for PD but also occur in some dementias including certain variants of AD. Although the underlying pathogenic cascades and the areas of the brain most affected are different for each disease, it is becoming increasingly apparent that the amyloidoses in the brain mutually influence each other, and experimental approaches used in one field have stimulated research in the other. Obviously, the amount of information and the broad area of research that is touched on at meetings such as this cannot all be incorporated into a brief meeting report. Here, we summarize some of the highlights.