Altered processing of Alzheimer amyloid precursor protein in response to neuronal degeneration.
Author(s) -
Kerstin Iverfeldt,
S. Ivar Walaas,
Paul Greengard
Publication year - 1993
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.90.9.4146
Subject(s) - senile plaques , amyloid precursor protein , p3 peptide , gene isoform , bace1 as , biochemistry of alzheimer's disease , degeneration (medical) , amyloid (mycology) , alzheimer's disease , neuronal degeneration , peptide , neuron , neuroscience , chemistry , microbiology and biotechnology , biology , pathology , biochemistry , medicine , disease , gene
In the brains of individuals with Alzheimer disease, senile plaques containing aggregates of beta-amyloid peptide, derived from the beta-amyloid precursor protein (APP), are seen in association with degenerating nerve terminals. It is not known whether the degenerating nerve terminals cause the formation of these aggregates or whether beta-amyloid peptide in the aggregates causes nerve-terminal degeneration. In the present study of rat brain, degeneration either of local neurons or of nerve terminals caused decreased levels of a neuron-enriched isoform of APP, increased levels of a glia-enriched isoform of APP, and increased levels of potentially amyloidogenic, as well as nonamyloidogenic, COOH-terminal fragments of APP. Our results demonstrate that neuronal degeneration affects APP processing and suggest that it may contribute to amyloid formation in mammalian brain.
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