Hsp60 Protects against Amyloid β Oligomer Synaptic Toxicity via Modification of Toxic Oligomer Conformation

Claudia Marino, Balaji Krishnan, Francesco Cappello, Giulio Taglialatela

    Research output: Contribution to journalArticlepeer-review

    13 Scopus citations

    Abstract

    Alzheimer's disease (AD) is the leading cause of dementia worldwide. While the etiology of AD remains uncertain, neurotoxic effects of amyloid beta oligomers (Aβo) on synaptic function, a well-established early event in AD, is an attractive area for the development of novel strategies to modify or cease the disease's progression. In this work, we tested the protective action of the mitochondrial chaperone Hsp60 against Aβo neurotoxicity, by determining the direct effect of Hsp60 in changing Aβo toxic conformations and thus reducing their dysfunctional synaptic binding and consequent suppression of long-term potentiation. Our data suggest that Hsp60 has a direct impact on Aβo, resulting in a reduction of cytotoxicity and rescue of Aβo-driven synaptic damage, thus proposing Hsp60 as an attractive therapeutic target candidate.

    Original languageEnglish (US)
    Pages (from-to)2858-2867
    Number of pages10
    JournalACS chemical neuroscience
    Volume10
    Issue number6
    DOIs
    StatePublished - Jun 19 2019

    Keywords

    • Alzheimer's disease
    • Amyloid-β oligomers
    • Hsp60
    • chaperonin
    • synaptic plasticity
    • synaptic toxicity

    ASJC Scopus subject areas

    • Biochemistry
    • Physiology
    • Cognitive Neuroscience
    • Cell Biology

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