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Cited by 30Alzheimer's disease research and treatmentsMitochondrial Function and PathologyCalcium signaling and nucleotide metabolism

The contribution of mitochondria-associated endoplasmic reticulum membranes (MAMs) dysfunction in Alzheimer’s disease and the potential countermeasure

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Li, Zehui, Cao, Yu, Pei, Hui, Ma, Lina, Yang, Yang, Li, Hao·2023·Frontiers in Neuroscience
DOI 10.3389/fnins.2023.1158204PMC PMC10027904
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Abstract

Alzheimer’s disease (AD) is the most common neurodegenerative disease. There are many studies targeting extracellular deposits of amyloid β-peptide (Aβ) and intracellular neurofibrillary tangles (NFTs), however, there are no effective treatments to halt the progression. Mitochondria-associated endoplasmic reticulum membranes (MAMs) have long been found to be associated with various pathogenesis hypotheses of AD, such as Aβ deposition, mitochondrial dysfunction, and calcium homeostasis. However, there is a lack of literature summarizing recent advances in the mechanism and treatment studies. Accordingly, this article reviews the latest research involving the roles of MAM structure and tethering proteins in the pathogenesis of AD and summarizes potential strategies targeting MAMs to dissect treatment perspectives for AD.

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  • Abnormal localization of APP to MAM alters γ-secretase function and enhances Aβ generation.

    “Mechanistically, abnormal localization of APP to mitochondria-associated membranes alters γ-secretase function and enhances Aβ generation [61], while mitochondrial oxidative stress activates kinases such as GSK3β and CDK5, promoting tau hyperphosphorylation [62].”

    From Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses (2026) · cites this paper as [61]

    The section “The role of MAMs in Aβ generation of AD” (page unavailable) says APP and γ-secretase are found in MAMs, where APP-derived C99 is cleaved to produce Aβ. It also reports that reducing ER–mitochondria contact lowers γ-secretase activity and Aβ levels. It does not establish that abnormal localization of APP itself alters γ-secretase function or enhances Aβ generation. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Cites

  • Endoplasmic reticulum-mitochondria contacts: Function of the junction

    Rowland, A. A., & Voeltz, G. K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3440 · Cited by 1,018 · cited 1× · see citing works

    “They are not the collection of membranes but the employment of the proteinaceous tethers (Rowland and Voeltz, 2012), which play a key role in many important metabolic processes including the transfer of calcium, mitochondrial dynamics, lipid synthesis, autophagy, apoptosis, and inflammation.”
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Cited by

Sorted by citations

Authors
Li, Z., Cao, Y., Pei, H., Ma, L., Yang, Y., & Li, H.
Affiliations
  • Xiyuan Hospital (CN)
  • Wangjing Hospital of China Academy of Chinese Medical Sciences (CN)
Corresponding author
  • Yang, Yang
  • Li, Hao
ORCID
Venue
Frontiers in Neuroscience
Publisher
Frontiers Media SA
Published
2023-03-07
Volume
17
Pages
1158204-1158204
ISSN
1662-453X (ISSN-L)
DOI
10.3389/fnins.2023.1158204
PMC
PMC10027904
OpenAlex
W4323363922
Cited by
30
References
1
Citations by year
2026: 12 · 2025: 6 · 2024: 8 · 2023: 4
FWCI
1.01
Type
journal article
Language
en
Open access
Licence
Locations
  • Frontiers in Neuroscience (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • National Natural Science Foundation of China (82205233)
  • China Academy of Chinese Medical Sciences (CI2021A01401)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords
Alzheimer's disease, mitochondria-associated endoplasmic reticulum membranes, amyloid-beta, neurofibrillary tangles, mitochondrial dysfunction, calcium homeostasis, neurodegeneration pathogenesis, treatment options

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