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J. Biol. Chem., Vol. 269, Issue 52, 32721-32724, Dec, 1994
A Tamaoka, A Odaka, Y Ishibashi, M Usami, N Sahara, N Suzuki, N Nukina, H Mizusawa, S Shoji and I Kanazawa
We have biochemically purified A beta from brains of two unrelated familial
Alzheimer's disease (FAD) pedigrees with the APP717 mutation (Val-->Ile)
and from two sporadic Alzheimer's disease (AD) brains and characterized
them by means of mass spectrometry and enzyme-linked immunosorbent assay.
We observed two types of amyloid beta protein (A beta), the short-tail form
(A beta 1-40) and the long-tail form (A beta 1-42/43), in sporadic AD and
FAD brains, and found that the ratio of the long-tail form of A beta (A
beta 1-42/43) to total A beta was increased in FAD brains. These in vivo
results were confirmed in vitro using cultured cells transfected with three
kinds of APP cDNAs bearing the APP717 mutations (Val-->Ile, Gly, or
Phe). Taken together with the hypothesis that A beta 1-42/43 functions as a
"seed" that increases the kinetics of amyloid fibril formation (Jarrett, J.
T., and Lansbury, P. T., Jr. (1993) Cell 73, 1055-1058), we conclude that
the APP717 missense mutation does not create new A beta species but
promotes the increased accumulation of A beta 1-42/43 in the brain, which
results in the enhancement of amyloid fibril formation from soluble A beta.
These findings provide a causal relationship between this FAD genotype and
the pathological phenotype of A beta deposition and senile plaque
formation.
APP717 missense mutation affects the ratio of amyloid beta protein species (A beta 1-42/43 and a beta 1-40) in familial Alzheimer's disease brain
Department of Neurology, University of Tsukuba, Ibaraki, Japan.
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