A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
(2021) In Communications Biology 4(1).- 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... (More)
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.
(Less)
- author
- organization
- publishing date
- 2021
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Communications Biology
- volume
- 4
- issue
- 1
- article number
- 19
- publisher
- Nature Publishing Group
- external identifiers
-
- scopus:85098622368
- pmid:33398040
- ISSN
- 2399-3642
- DOI
- 10.1038/s42003-020-01490-3
- language
- English
- LU publication?
- yes
- id
- 3ef8a5b9-b63c-4fce-b39a-8b3335645b5c
- date added to LUP
- 2021-01-12 12:15:58
- date last changed
- 2024-04-17 23:24:49
@article{3ef8a5b9-b63c-4fce-b39a-8b3335645b5c,
abstract = {{<p>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.</p>}},
author = {{Cataldi, Rodrigo and Chia, Sean and Pisani, Katarina and Ruggeri, Francesco S. and Xu, Catherine K. and Šneideris, Tomas and Perni, Michele and Sarwat, Sunehera and Joshi, Priyanka and Kumita, Janet R. and Linse, Sara and Habchi, Johnny and Knowles, Tuomas P.J. and Mannini, Benedetta and Dobson, Christopher M. and Vendruscolo, Michele}},
issn = {{2399-3642}},
language = {{eng}},
number = {{1}},
publisher = {{Nature Publishing Group}},
series = {{Communications Biology}},
title = {{A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers}},
url = {{http://dx.doi.org/10.1038/s42003-020-01490-3}},
doi = {{10.1038/s42003-020-01490-3}},
volume = {{4}},
year = {{2021}},
}