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OPA1 deficiency promotes secretion of FGF21 from muscle that prevents obesity and insulin resistance
Open accessAbstract
Mitochondrial dynamics is a conserved process by which mitochondria undergo repeated cycles of fusion and fission, leading to exchange of mitochondrial genetic content, ions, metabolites, and proteins. Here, we examine the role of the mitochondrial fusion protein optic atrophy 1 (OPA1) in differentiated skeletal muscle by reducing OPA1 gene expression in an inducible manner. OPA1 deficiency in young mice results in non-lethal progressive mitochondrial dysfunction and loss of muscle mass. Mutant mice are resistant to age- and diet-induced weight gain and insulin resistance, by mechanisms that involve activation of ER stress and secretion of fibroblast growth factor 21 (FGF21) from skeletal muscle, resulting in increased metabolic rates and improved whole-body insulin sensitivity. OPA1-elicited mitochondrial dysfunction activates an integrated stress response that locally induces muscle atrophy, but via secretion of FGF21 acts distally to modulate whole-body metabolism.
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In the citing paper
“Inhibition of the IMM profusion factor, OPA1, in muscle resulted in a similar but more severe phenotype than skeletal muscle MFN1 and MFN2 ablation [187, 192, 193].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [193]
In the citing paper
“Consistent with the other OPA1 knockout mice, also in this model, the metabolic changes are mediated by the muscle secretion of FGF21, whose level was mildly increased when compared to the ones present in mice in which OPA1 is completely deleted in adulthood.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [193]
In the citing paper
“When OPA1 was deleted during fetal development, animals died a few days after birth.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [193]
In the citing paper
“Interestingly, a mild inhibition of OPA1, which does not alter mitochondrial complex and supercomplex formation as well as mitochondrial DNA content and citrate synthase activity, in muscle during neonatal growth results in several beneficial metabolic changes in terms of resistance to obesity when the animals were challenged with a high-fat diet [193].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [193]
In the citing paper
“Deletion of OPA1 in adult mice (3–5 months of age) resulted in a decrease of mtDNA, reduced respiratory complexes and supercomplexes content, and complex activity, respiration, and mitochondrial membrane potential.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [193]
In the citing paper
“Moreover, we and others recently demonstrated that in a muscle‐specific OPA1 knockout animal model, characterized by mitochondrial dysfunction and by extensive muscle loss, the contribution of skeletal muscle to circulating FGF21 was predominant.15, 16, 18”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [15]
In the citing paper
“In contrast, muscle‐dependent systemic release of FGF21 increases with starvation, endoplasmic reticulum stress, mitochondrial dysfunction, obesity, mitochondrial myopathies, and aging.6, 13, 14, 15, 16, 17, 18, 19”
From Fibroblast growth factor 21 controls mitophagy and muscle mass (2019) · cites this paper as [15]
In the citing paper
“Specific deletion of Opa1 in skeletal muscle leads to mitochondrial dysfunction, oxidative stress, endoplasmic reticulum (ER) stress, and inflammation [36,37,38].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [37]
In the citing paper
“Taken altogether, the available literature clearly indicates that mitochondrial fusion proteins are essential for the maintenance of mitochondrial and skeletal muscle health.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [37]
In the citing paper
“Recently, the quality of mitochondria has emerged as important control process that regulates skeletal muscle function20–23.”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [21]
In the citing paper
“multiple alterations in mitochondrial function such as mitophagy and mitochondrial dynamics can lead to a surprising phenotype characterized by reduced muscle mitochondrial energetics, but remarkably, with resistance to high-fat-diet-induced obesity21,46.”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [21]
In the citing paper
“proper maintenance of mitochondria dynamics, i.e. the balance between fission and fusion, is necessary for optimal muscle mitochondrial function and fitness20–23,43.”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [21]
In the citing paper
“For example, FGF21 production from skeletal muscle (56, 61, 103, 128), BAT (59), and cardiac tissue (143) is increased in genetic mouse models of cellular or mitochondrial stress.”
From Fibroblast Growth Factor 21: A Versatile Regulator of Metabolic Homeostasis (2018) · cites this paper as [103]
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Self-citationMitochondrial quality control in exercise-mitigated muscular atrophy
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Creating Optimal Western Blot Conditions for OPA1 Isoforms in Skeletal Muscle Cells and Tissue
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A Polymorphism in the FGF21 Gene is a Novel Risk Variant for Metabolic-Associated Steatohepatitis
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OGG1 increases exercise endurance via elevated skeletal muscle FGF21
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Self-citationProof of principle of therapies for dominant optic atrophy type1
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Metadata
- Authors
- Pereira, R. O., Tadinada, S. M., Zasadny, F. M., Oliveira, K. J., Pires, K. M. P., Olvera, A., Jeffers, J., Souvenir, R., Mcglauflin, R., Seei, A., Funari, T., Sesaki, H., Potthoff, M. J., Adams, C. M., Anderson, E. J., & Abel, E. D.
- Affiliations
- University of Iowa (US)
- University of Utah (US)
- Johns Hopkins University (US)
- Corresponding author
- Abel, E Dale
- ORCID
- Venue
- The EMBO Journal
- Published
- 2017-06-12
- Volume
- 36
- Issue
- 14
- Pages
- 2126-2145
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC5510002
- OpenAlex
- W2625633983
- Cited by
- 211
- References
- 63
- Citations by year
- 2026: 25 · 2025: 17 · 2024: 23 · 2023: 28 · 2022: 23 · 2021: 30 · 2020: 23 · 2019: 17 · 2018: 22 · 2017: 3
- FWCI
- 7.26
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association (15SDG25710438)
- HHS | National Institutes of Health (R01HL108379, R01DK092065)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
- 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
- Keywords
- OPA1, optic atrophy 1, mitochondrial fusion, mitochondrial dysfunction, skeletal muscle, endoplasmic reticulum stress, integrated stress response, muscle atrophy, obesity, insulin resistance, aging, metabolic rate, whole-body metabolism
- MeSH terms
- Animals, Fibroblast Growth Factors, Insulin Resistance, Muscles, Muscular Atrophy, Obesity, GTP Phosphohydrolases, Mice, Gene Knockdown Techniques
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