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Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path.

Authors
Buxbaum-JD; Thinakaran-G; Koliatsos-V; O'Callahan-J; Slunt-HH; Price-DL; Sisodia-SS
Source
J Neurosci 1998 Dec; 18(23):9629-9637
NIOSHTIC No.
20000650
Abstract
Amyloid deposition is a neuropathological hallmark of Alzheimer's disease. The principal component of amyloid deposits is beta amyloid peptide (Abeta), a peptide derived by proteolytic processing of the amyloid precursor protein (APP). APP is axonally transported by the fast anterograde component. Several studies have indicated that Abeta deposits occur in proximity to neuritic and synaptic profiles. Taken together, these latter observations have suggested that APP, axonally transported to nerve terminals, may be processed to Abeta at those sites. To examine the fate of APP in the CNS, we injected [35S]methionine into the rat entorhinal cortex and examined the trafficking and processing of de novo synthesized APP in the perforant pathway and at presynaptic sites in the hippocampal formation. We report that both full-length and processed APP accumulate at presynaptic terminals of entorhinal neurons. Finally, we demonstrate that at these synaptic sites, C-terminal fragments of APP containing the entire Abeta domain accumulate, suggesting that these species may represent the penultimate precursors of synaptic Abeta.
Keywords
Neurons; Metabolism; Amyloid-beta-protein; Analysis; Genetics; Epidemiology;
CODEN
JNRSDS
CAS No.
7005-18-7;
Publication Date
19981201
Document Type
Journal Article;
Fiscal Year
1999
NTIS Accession No.
NTIS Price
Issue of Publication
23
ISSN
0270-6474
NIOSH Division
HELD;
Priority Area
Disease and Injury;
Source Name
The Journal of Neuroscience
State
WV;
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