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Cited by 975Alzheimer's disease research and treatmentsMitochondrial Function and PathologyDementia and Cognitive Impairment Research

Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer’s disease

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Reddy, P. Hemachandra, Beal, M. Flint·2008·Trends in Molecular Medicine
DOI 10.1016/j.molmed.2007.12.002PMC PMC3107703
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Abstract

Recent studies of postmortem brains from Alzheimer's disease (AD) patients and transgenic mouse models of AD suggest that oxidative damage, induced by amyloid beta (Abeta), is associated with mitochondria early in AD progression. Abeta and amyloid-precursor protein are known to localize to mitochondrial membranes, block the transport of nuclear-encoded mitochondrial proteins to mitochondria, interact with mitochondrial proteins, disrupt the electron-transport chain, increase reactive oxygen species production, cause mitochondrial damage and prevent neurons from functioning normally. Furthermore, accumulation of Abeta at synaptic terminals might contribute to synaptic damage and cognitive decline in patients with AD. Here, we describe recent studies regarding the roles of Abeta and mitochondrial function in AD progression and particularly in synaptic damage and cognitive decline.

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  • Mitochondrial ROS can trigger production of amyloid β, which can in turn further damage mitochondria.

    “There is also evidence that mitochondrial ROS can trigger the production of amyloid β, which can in turn further damage mitochondria [66,67], providing an additional layer to positive feedback models.”

    From Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease? (2022) · cites this paper as [67]

    The Introduction’s “Aβ and mitochondrial dysfunction” section reports that amyloid β can cause mitochondrial dysfunction and increase ROS production. Its “Biochemical changes” section says mitochondrial oxidative stress occurs before Aβ pathology, but does not say that mitochondrial ROS triggers Aβ production. The proposed feedback loop is therefore only partly supported. Page numbers are unavailable in our copy. (LLM, conf=0.86)

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Cited by

Sorted by citations

Authors
Reddy, P. H., & Beal, M. F.
Affiliations
  • Oregon Health & Science University (US)
  • Cornell University (US)
Corresponding author
Reddy, P. Hemachandra
ORCID
Venue
Trends in Molecular Medicine
Publisher
Elsevier BV
Published
2008-02
Volume
14
Issue
2
Pages
45-53
ISSN
1471-4914 (ISSN-L)
DOI
10.1016/j.molmed.2007.12.002
PMC
PMC3107703
OpenAlex
W2007047564
Cited by
975
References
24
Citations by year
2026: 46 · 2025: 60 · 2024: 63 · 2023: 61 · 2022: 65 · 2021: 66 · 2020: 69 · 2019: 63 · 2018: 74 · 2017: 43 · 2016: 42 · 2015: 30 · 2014: 47 · 2013: 45 · 2012: 51
FWCI
5.49
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Trends in Molecular Medicine (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Institute on Aging (AG026051, R03AG026051, R01AG028072, AG028072)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords
amyloid-beta, mitochondrial dysfunction, synaptic damage, Alzheimer's disease, cognitive decline, aging, oxidative stress, reactive oxygen species, electron transport chain, mitochondrial membrane, amyloid precursor protein, mitochondrial protein transport, synaptic terminals
MeSH terms
Aging, Alzheimer Disease, Animals, Cognition Disorders, Humans, Mitochondria, Models, Biological, Amyloid beta-Peptides, Presynaptic Terminals, Oxidative Stress, Disease Progression, Mice

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