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A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers.

Published version
Peer-reviewed

Type

Article

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Authors

Chia, Sean 
Pisani, Katarina 
Ruggeri, Francesco S  ORCID logo  https://orcid.org/0000-0002-1232-1907

Abstract

Aberrant soluble oligomers formed by the amyloid-β peptide (Aβ) are major pathogenic agents in the onset and progression of Alzheimer's disease. A variety of biomolecules can influence the formation of these oligomers in the brain, although their mechanisms of action are still largely unknown. Here, we studied the effects on Aβ aggregation of DOPAL, a reactive catecholaldehyde intermediate of dopamine metabolism. We found that DOPAL is able to stabilize Aβ oligomeric species, including dimers and trimers, that exert toxic effects on human neuroblastoma cells, in particular increasing cytosolic calcium levels and promoting the generation of reactive oxygen species. These results reveal an interplay between Aβ aggregation and key biochemical processes regulating cellular homeostasis in the brain.

Description

Keywords

Alzheimer Disease, Amyloid beta-Peptides, Cell Line, Tumor, Dopamine, Escherichia coli, Humans

Journal Title

Commun Biol

Conference Name

Journal ISSN

2399-3642
2399-3642

Volume Title

4

Publisher

Springer Science and Business Media LLC