Abstract
The amyloid β protein is deposited in the brains of patients with Alzheimer's disease but its pathogenic role is unknown. In culture, the amyloid β protein was neurotrophic to undifferentiated hippocampal neurons at low concentrations and neurotoxic to mature neurons at higher concentrations. In differentiated neurons, amyloid β protein caused dendritic and axonal retraction followed by neuronal death. A portion of the amyloid β protein (amino acids 25 to 35) mediated both the trophic and toxic effects and was homologous to the tachykinin neuropeptide family. The effects of the amyloid β protein were mimicked by tachykinin antagonists and completely reversed by specific tachykinin agonists. Thus, the amyloid β protein could function as a neurotrophic factor for differentiating neurons, but at high concentrations in mature neurons, as in Alzheimer's disease, could cause neuronal degeneration.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 2:10 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, midnight) |
Indexed | 3 days, 15 hours ago (Aug. 29, 2025, 6:35 a.m.) |
Issued | 34 years, 10 months ago (Oct. 12, 1990) |
Published | 34 years, 10 months ago (Oct. 12, 1990) |
Published Print | 34 years, 10 months ago (Oct. 12, 1990) |
@article{Yankner_1990, title={Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides}, volume={250}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.2218531}, DOI={10.1126/science.2218531}, number={4978}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Yankner, Bruce A. and Duffy, Lawrence K. and Kirschner, Daniel A.}, year={1990}, month=oct, pages={279–282} }