Alzheimer's disease (AD), a neurodegenerative disorder that severely i
mpairs cognitive and memory function in elderly people, is partially c
haracterized neuropathologically by extracellular deposits of beta-amy
loid protein. We were interested in studying how beta-amyloid may be i
nvolved in aspects of AD pathogenesis. To do this, we expressed the la
st 100 amino acids of the amyloid precursor protein, which contains th
e entire beta-amyloid region, in PC12 cells and in brains of transgeni
c mice. We found that expression of this fragment of beta PP altered c
ytoskeletal changes in PC12 cells following nerve growth factor treatm
ent. Using both in vitro and in vivo systems of human beta PP expressi
on, we can study the biology of beta PP and test hypotheses of how it
may be involved in Alzheimer's disease.