Abstract
The 4-kilodalton amyloid β protein (Aβ), which forms fibrillar deposits in Alzheimer's disease (AD), is derived from a large protein referred to as the amyloid β protein precursor (βAPP). Human neuroblastoma (M17) cells transfected with constructs expressing wild-type βAPP or a mutant, βAPPσNL, recently linked to familial AD were compared. After continuous metabolic labeling for 8 hours, cells expressing βAPPΔNL had five times more of an Aβ-bearing, carboxyl terminal, βAPP derivative than cells expressing wild-type βAPP and they released six times more Aβ into the medium. Thus this mutant βAPP may cause AD because its processing is altered in a way that releases increased amounts of Aβ.
Original language | English (US) |
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Pages (from-to) | 514-516 |
Number of pages | 3 |
Journal | Science |
Volume | 259 |
Issue number | 5094 |
State | Published - Jan 22 1993 |
ASJC Scopus subject areas
- General