Aβ Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors.


Journal

ACS chemical neuroscience
ISSN: 1948-7193
Titre abrégé: ACS Chem Neurosci
Pays: United States
ID NLM: 101525337

Informations de publication

Date de publication:
17 02 2021
Historique:
pubmed: 5 2 2021
medline: 22 6 2021
entrez: 4 2 2021
Statut: ppublish

Résumé

Alzheimer's disease, which is the most common form of dementia, is characterized by the aggregation of the amyloid β peptide (Aβ) and by an impairment of calcium homeostasis caused by excessive activation of glutamatergic receptors (excitotoxicity). Here, we studied the effects on calcium homeostasis caused by the formation of Aβ oligomeric assemblies. We found that Aβ oligomers cause a rapid influx of calcium ions (Ca

Identifiants

pubmed: 33538575
doi: 10.1021/acschemneuro.0c00811
pmc: PMC7898266
doi:

Substances chimiques

Amyloid beta-Peptides 0
Peptide Fragments 0
Receptors, N-Methyl-D-Aspartate 0
alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid 77521-29-0
Calcium SY7Q814VUP

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

766-781

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Auteurs

Giulia Fani (G)

Department of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, 50134 Florence, Italy.
Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Benedetta Mannini (B)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Giulia Vecchi (G)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Roberta Cascella (R)

Department of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, 50134 Florence, Italy.

Cristina Cecchi (C)

Department of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, 50134 Florence, Italy.

Christopher M Dobson (CM)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Michele Vendruscolo (M)

Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K.

Fabrizio Chiti (F)

Department of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, Viale Morgagni 50, 50134 Florence, Italy.

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Classifications MeSH