The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Amyloid peptides are toxic via a common oxidative mechanism.
Open accessAbstract
beta-Amyloid protein (A beta) is a member of a small group of proteins that accumulate as amyloid deposits in various tissues. It has recently been demonstrated that the toxicity of A beta toward some neural cells is caused by oxidative damage. Since all of the amyloid diseases are characterized by protein deposited in the antiparallel beta-sheet conformation, it was asked whether there is a common toxic mechanism. It is shown here that the protein components of other human amyloidoses, including amylin, calcitonin, and atrial natriuretic peptide, are all toxic to clonal and primary cells. The toxicity is mediated via a free radical pathway indistinguishable from that of A beta. Experiments with synthetic peptides suggest that it is the amphiphilic nature of the peptides generated by their beta structure rather than their beta structure per se that causes toxicity. These results tend to rule out the alternative that amyloid toxicity is exclusively mediated via specific cell surface receptors.
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Hydrogen peroxide mediates amyloid β protein toxicity
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Self-citationNeurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
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Christen, Y. (2000) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/71.2.621s · Cited by 1,158
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Metadata
- Authors
- Schubert, D., Behl, C., Lesley, R., Brack, A., Dargusch, R., Sagara, Y., & Kimura, H.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1995-03-14
- Volume
- 92
- Issue
- 6
- Pages
- 1989-1993
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2057714820
- Cited by
- 379
- References
- 7
- FWCI
- 14.15
- Type
- journal article
- Language
- en
- Open access
- green
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- Schubert, D., Behl, C., Lesley, R., Brack, A., Dargusch, R., Sagara, Y., & Kimura, H. (1995). Amyloid peptides are toxic via a common oxidative mechanism. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.92.6.1989
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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