IMR Press / FBL / Volume 20 / Issue 1 / DOI: 10.2741/4304

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.


Critical analysis of Alzheimer’s amyloid-beta toxicity to mitochondria

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1 Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Russia
2 Pushchino State Institute of Natural Sciences, Pushchino, Russia
Academic Editor:Gjumrakch Aliev
Front. Biosci. (Landmark Ed) 2015, 20(1), 173–197;
Published: 1 January 2015

Amyloid-beta peptide (Abeta) is believed to be a central player in the Alzheimer disease (AD) pathogenesis. However, its mechanisms of toxicity to the central nervous system are unknown. To explore this area, investigators have recently focused on Abeta-induced cellular dysfunction. Extensive research has been conducted to investigate Abeta monomers and oligomers, and these multiple facets have provided a wealth of data from specific models. Abeta appears to be accumulated in neuronal mitochondria and mediates mitochondrial toxicity. Mitochondrial dysfunction became a hallmark of Abeta-induced neuronal toxicity. Mitochondria are currently considered as primary targets in the pathobiology of neurodegeneration. This review provides an overview of the Abeta toxicity to isolated mitochondria, mitochondria in different tissues and cells in vitro and in vivo. Full texts and abstracts from all 530 biomedical articles listed in PubMed and published before January 2014 were analysed. The mechanisms underlying the interaction between Abeta and mitochondrial membranes and resulting mitochondrial dysfunction are most disputed issues. Understanding and discussing this interaction is essential to evaluating Abeta effects on various intracellular metabolic processes.

Alzheimer’s disease
Brain regions
Non-neuronal cells
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