It is known that beta-amyloid peptide (A beta) contributes to the neurodege
neration in Alzheimer's disease (AD) and operates through activation of an
apoptotic pathway. Apoptotic signal is driven by a family of cysteine prote
ases called caspases. The beta-amyloid precursor protein (APP) is directly
and efficiently cleaved by caspases during apoptosis, resulting in elevated
beta-amyloid peptide formation. Cerebellar neurons from rat pups were trea
ted with the aged A beta(25-35) at 1 and 5 mu M and fluorescence assays of
caspase activity performed over 4 days. We observed an increase in caspase
activity after 48 h treatment in both 1 and 5 mu M treated cells, then (72-
96 h) caspase activity decreased to control values. The data presented supp
ort the hypothesis that A beta(25-35)-induced apoptosis is mediated by the
activation of Caspase-3 and that this is a transient effect. (C) 2000 Publi
shed by Elsevier Science Ireland Ltd.