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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Inhibition of OPA1 in muscle results in a similar but more severe phenotype than skeletal muscle MFN1 and MFN2 ablation.
“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]
The metabolic changes in the mild OPA1 inhibition model are mediated by muscle secretion of FGF21, whose level was mildly increased compared to complete OPA1 deletion in adulthood.
“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]
When OPA1 was deleted during fetal development, animals died a few days after birth.
“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]
Mild inhibition of OPA1 during neonatal growth, which does not alter mitochondrial complex and supercomplex formation, mitochondrial DNA content, or citrate synthase activity, results in beneficial metabolic changes in resistance to obesity when animals are challenged with a high-fat diet.
“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]
Deletion of OPA1 in adult mice (3-5 months of age) results in a decrease of mtDNA, reduced respiratory complexes and supercomplexes content, and reduced complex activity, respiration, and mitochondrial membrane potential.
“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 a muscle-specific OPA1 knockout animal model, the contribution of skeletal muscle to circulating FGF21 is predominant.
“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]
Muscle-dependent systemic release of FGF21 increases with starvation, endoplasmic reticulum stress, mitochondrial dysfunction, obesity, mitochondrial myopathies, and aging.
“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]
Specific deletion of Opa1 in skeletal muscle leads to mitochondrial dysfunction, oxidative stress, endoplasmic reticulum stress, and inflammation.
“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]
Mitochondrial fusion proteins are essential for the maintenance of mitochondrial and skeletal muscle health.
“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]
The quality of mitochondria has emerged as an important control process that regulates skeletal muscle function.
“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]
Multiple alterations in mitochondrial function such as mitophagy and mitochondrial dynamics can lead to reduced muscle mitochondrial energetics but resistance to high-fat-diet-induced obesity.
“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]
Proper maintenance of mitochondria dynamics, i.e. the balance between fission and fusion, is necessary for optimal muscle mitochondrial function and fitness.
“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 genetic mouse models of cellular or mitochondrial stress, FGF21 production is increased from skeletal muscle, BAT, and cardiac tissue.
“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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- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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