Sj. Frucht et Eh. Koo, BETA-AMYLOID PROTEIN IS HIGHER IN ALZHEIMERS-DISEASE BRAINS - DESCRIPTION OF A QUANTITATIVE BIOCHEMICAL ASSAY, Journal of neuropathology and experimental neurology, 52(6), 1993, pp. 640-647
Deposition of beta-amyloid protein (Abeta) in senile plaques and in th
e walls of cerebral vessels is a pathologic hallmark of Alzheimer's di
sease (AD). The current diagnostic criteria for AD requires the presen
ce of neurofibrillary tangles and a minimum number of senile plaques i
n cortex. Senile plaques are readily visualized by silver staining or
immunocytochemistry using antibodies raised to Abeta. Available histoc
hemical and immunocytochemical methods are sensitive but the results m
ay occasionally be variable and sampling from many brain regions is di
fficult and impractical. This study describes a simple biochemical met
hod for quantifying the Abeta load in unfixed brain homogenates. The i
mmunoassay recognizes all forms of Abeta deposits (neuritic and diffus
e plaques, and cerebrovascular amyloid) and has a sensitivity and spec
ificity comparable to immunocytochemistry. In direct comparisons, resu
lts from the dot blot method correspond well with both Western blot an
alysis of partially purified Abeta and plaque counting by immunocytoch
emistry. In a retrospective series of 39 postmortem AD and control cas
es, the amount of Abeta in brain by dot blot immunoreactivity effectiv
ely separated the two groups. Therefore, this method provides a rapid,
sensitive, and accurate quantitation of Abeta in postmortem brain tis
sue and represents an alternative approach for studying Abeta depositi
on in aging and AD.