Caspase-cleaved Tau Expression Induces Mitochondrial Dysfunction in Immortalized Cortical Neurons
Open accessAbstract
In Alzheimer disease (AD) mitochondrial abnormalities occur early in the pathogenic process and likely play a significant role in disease progression. Tau is a microtubule-associated protein that is abnormally processed in AD, and a connection between tau pathology and mitochondrial impairment has been proposed. However, few studies have examined the relationship between pathological forms of tau and mitochondrial dysfunction. We recently demonstrated that inducible expression of tau truncated at Asp-421 to mimic caspase cleavage (T4C3) was toxic to immortalized cortical neurons compared with a full-length tau isoform (T4). In this study we investigated the effects of T4C3 on mitochondrial function. Expression of T4C3 induced mitochondrial fragmentation and elevated oxidative stress levels in comparison with T4-expressing cells. Thapsigargin treatment of T4 or T4C3 cells, which causes an increase in intracellular calcium levels, resulted in a significant decrease in mitochondrial potential and loss of mitochondrial membrane integrity in T4C3 cells when compared with cells expressing T4. The mitochondrial fragmentation and mitochondrial membrane damage were ameliorated in T4C3 cells by pretreatment with cyclosporine A or FK506, implicating the calcium-dependent phosphatase calcineurin in these pathogenic events. Increased calcineurin activity has been reported in AD brain, and thus, inhibition of this phosphatase may provide a therapeutic target for the treatment of AD.
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Mitochondrial abnormalities, synaptic loss and dysfunction, altered axonal transport, and activation of cell death pathways have been implicated as consequences of tau mislocalization or oligomerization.
“Mitochondrial abnormalities, synaptic loss and dysfunction, altered axonal transport, and activation of cell death pathways (including caspase activation and inflammatory responses) have all been directly or indirectly implicated as consequences of tau mislocalization or oligomerization (20, 40, 43–52).”
From All the Tau We Cannot See (2023) · cites this paper as [50]
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- Authors
- Quintanilla, R. A., Matthews-Roberson, T. A., Dolan, P. J., & Johnson, G. V. W.
- Affiliations
- University of Rochester Medicine (US)
- Corresponding author
- Johnson, Gail V.W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-07
- Volume
- 284
- Issue
- 28
- Pages
- 18754-18766
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2707209
- OpenAlex
- W2032879521
- Cited by
- 170
- References
- 51
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 8 · 2023: 10 · 2022: 7 · 2021: 17 · 2020: 8 · 2019: 7 · 2018: 6 · 2017: 14 · 2016: 8 · 2015: 10 · 2014: 6 · 2013: 9 · 2012: 15
- FWCI
- 10.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (NS051279, R01NS051279)
- 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
- tauopathy, Alzheimer's disease, mitochondrial dysfunction, mitochondrial fragmentation, oxidative stress, mitochondrial membrane integrity, mitochondrial membrane potential, calcineurin, cyclosporine, FK506, thapsigargin, intracellular calcium, cortical neurons, tau truncation
- MeSH terms
- Alzheimer Disease, Animals, Brain, Cytosol, Membrane Potentials, Microscopy, Fluorescence, Mitochondria, Models, Biological, Neurons, Superoxides, tau Proteins, Reactive Oxygen Species, Thapsigargin, Caspases, Mice
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