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[beta-amyloid cascade: current status and future directions].

The deposition of amyloid beta peptides (A beta) is one of the pathological hallmarks of Alzheimer's disease (AD) brains. A beta are composed of 40-42 amino acid peptides that are proteolytically cleaved from beta APP. The deposition as diffuse plaques of a species of A beta ending at the 42nd residue (A beta 42) is one of the earliest pathological changes of AD. Importantly, mutations in beta APP genes located in positions flanking the A beta sequences have been shown to cosegregate with the clinical manifestations of AD in a subset of familial AD (FAD) pedigrees. Moreover, mutations in presenilin (PS) 1 and 2, novel polytopic membrane proteins identified as causative molecules for the majority of FAD, also increase the production of A beta 42. These results support the notion that A beta (42) plays a key role in the cascadic development of AD. Recently, PS 1 and PS 2 are shown to be the catalytic subunits of gamma-secretase that cleave the intramembrane segments of beta APP and Notch. Future therapeutic approaches to reduce amyloid deposition, including inhibitors for beta- and gamma-secretases, as well as beta-amyloid vaccine therapy, raise high hopes towards the cure and prevention of AD, although the outcome thereof would be key to the consistency of amyloid cascade hypothesis.

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