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. 1993 May 1;90(9):4146–4150. doi: 10.1073/pnas.90.9.4146

Altered processing of Alzheimer amyloid precursor protein in response to neuronal degeneration.

K Iverfeldt 1, S I Walaas 1, P Greengard 1
PMCID: PMC46463  PMID: 8483927

Abstract

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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Selected References

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