MCU-independent Ca2+ uptake mediates mitochondrial Ca2+ overload and necrotic cell death in a mouse model of Duchenne muscular dystrophy
Open accessAbstract
Mitochondrial Ca 2+ overload can mediate mitochondria-dependent cell death, a major contributor to several human diseases. Indeed, Duchenne muscular dystrophy (MD) is driven by dysfunctional Ca 2+ influx across the sarcolemma that causes mitochondrial Ca 2+ overload, organelle rupture, and muscle necrosis. The mitochondrial Ca 2+ uniporter (MCU) complex is the primary characterized mechanism for acute mitochondrial Ca 2+ uptake. One strategy for preventing mitochondrial Ca 2+ overload is deletion of the Mcu gene, the pore forming subunit of the MCU-complex. Conversely, enhanced MCU-complex Ca 2+ uptake is achieved by deleting the inhibitory Mcub gene. Here we show that myofiber-specific Mcu deletion was not protective in a mouse model of Duchenne MD. Specifically, Mcu gene deletion did not reduce muscle histopathology, did not improve muscle function, and did not prevent mitochondrial Ca 2+ overload. Moreover, myofiber specific Mcub gene deletion did not augment Duchenne MD muscle pathology. Interestingly, we observed MCU-independent Ca 2+ uptake in dystrophic mitochondria that was sufficient to drive mitochondrial permeability transition pore (MPTP) activation and skeletal muscle necrosis, and this same type of activity was observed in heart, liver, and brain mitochondria. These results demonstrate that mitochondria possess an uncharacterized MCU-independent Ca 2+ uptake mechanism that is sufficient to drive MPTP-dependent necrosis in MD in vivo.
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Elevated intracellular Ca2+ levels can lead to mitochondrial overload, disrupting mitochondrial membrane potential and impairing ATP synthesis.
“Elevated intracellular Ca²⁺ levels can lead to mitochondrial overload, disrupting the mitochondrial membrane potential and impairing ATP synthesis.”
From Impairing the interaction between Erg11 and cytochrome P450 reductase Ncp1 enhances azoles’ antifungal activities (2025) · cites this paper as [37]
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- Authors
- Bround, M. J., Abay, E., Huo, J., Havens, J. R., York, A. J., Bers, D. M., & Molkentin, J. D.
- Affiliations
- Cincinnati Children's Hospital Medical Center (US)
- University of California, Davis (US)
- Corresponding author
- Molkentin, Jeffery D.
- ORCID
- Venue
- Scientific Reports
- Published
- 2024-03-21
- Volume
- 14
- Issue
- 1
- Pages
- 6751-6751
- ISSN
- 2045-2322 (ISSN-L)
- OpenAlex
- W4393054563
- Cited by
- 20
- References
- 89
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 3
- FWCI
- 2.72
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Digital Commons-TMC (Texas Medical Center) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR078253)
- National Heart, Lung, and Blood Institute (HL132831; HL156852)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Keywords
- Duchenne muscular dystrophy, mitochondrial calcium overload, mitochondrial calcium uniporter, MCU, MCUB, mitochondrial permeability transition pore, necrosis, skeletal muscle necrosis, dystrophic muscle
- MeSH terms
- Animals, Calcium, Humans, Mitochondria, Necrosis, Calcium Channels, Cell Death, Muscular Dystrophy, Duchenne, Mitochondrial Proteins, Mitochondrial Membrane Transport Proteins, Mice
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