Genetic deletion of muscle RANK or selective inhibition of RANKL is not as effective as full-length OPG-fc in mitigating muscular dystrophy
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Although there is a strong association between osteoporosis and skeletal muscle atrophy/dysfunction, the functional relevance of a particular biological pathway that regulates synchronously bone and skeletal muscle physiopathology is still elusive. Receptor-activator of nuclear factor κB (RANK), its ligand RANKL and the soluble decoy receptor osteoprotegerin (OPG) are the key regulators of osteoclast differentiation and bone remodelling. We thus hypothesized that RANK/RANKL/OPG, which is a key pathway for bone regulation, is involved in Duchenne muscular dystrophy (DMD) physiopathology. Our results show that muscle-specific RANK deletion (mdx-RANK mko ) in dystrophin deficient mdx mice improves significantly specific force [54% gain in force] of EDL muscles with no protective effect against eccentric contraction-induced muscle dysfunction. In contrast, full-length OPG-Fc injections restore the force of dystrophic EDL muscles [162% gain in force], protect against eccentric contraction-induced muscle dysfunction ex vivo and significantly improve functional performance on downhill treadmill and post-exercise physical activity. Since OPG serves a soluble receptor for RANKL and as a decoy receptor for TRAIL, mdx mice were injected with anti-RANKL and anti-TRAIL antibodies to decipher the dual function of OPG. Injections of anti-RANKL and/or anti-TRAIL increase significantly the force of dystrophic EDL muscle [45% and 17% gains in force, respectively]. In agreement, truncated OPG-Fc that contains only RANKL domains produces similar gains, in terms of force production, than anti-RANKL treatments. To corroborate that full-length OPG-Fc also acts independently of RANK/RANKL pathway, dystrophin/RANK double-deficient mice were treated with full-length OPG-Fc for 10 days. Dystrophic EDL muscles exhibited a significant gain in force relative to untreated dystrophin/RANK double-deficient mice, indicating that the effect of full-length OPG-Fc is in part independent of the RANKL/RANK interaction. The sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) activity is significantly depressed in dysfunctional and dystrophic muscles and full-length OPG-Fc treatment increased SERCA activity and SERCA-2a expression. These findings demonstrate the superiority of full-length OPG-Fc treatment relative to truncated OPG-Fc, anti-RANKL, anti-TRAIL or muscle RANK deletion in improving dystrophic muscle function, integrity and protection against eccentric contractions. In conclusion, full-length OPG-Fc represents an efficient alternative in the development of new treatments for muscular dystrophy in which a single therapeutic approach may be foreseeable to maintain both bone and skeletal muscle functions.
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OPG has been shown to be capable of increasing muscle force when given to mdx mice, a model for muscular dystrophy.
“In addition to the role that OPG plays in modulating RANK signaling in osteoclasts, OPG has been shown to be capable of increasing muscle force when given to mdx mice (39, 40), which is a model for muscular dystrophy, raising the possibility that OPG may play a role in muscle hypertrophy induced by loss of MSTN/activin A signaling.”
From Targeting myostatin/activin A protects against skeletal muscle and bone loss during spaceflight (2020) · cites this paper as [40]
The effect of OPG on mdx muscle was reported to be greater than that induced by coadministration of anti-RANKL and anti-TRAIL antibodies and was also seen in mice in which RANK had been targeted in muscle, suggesting that OPG acts at least partly in a RANK-independent manner to regulate muscle function.
“In this regard, the effect of OPG on mdx muscle was reported to be greater than that induced by coadministration of anti-RANKL and anti-TRAIL antibodies and was also seen in mice in which RANK had been targeted in muscle, suggesting that OPG acts at least partly in a RANK-independent manner to regulate muscle function (40).”
From Targeting myostatin/activin A protects against skeletal muscle and bone loss during spaceflight (2020) · cites this paper as [40]
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- Authors
- Dufresne, S. S., Boulanger-Piette, A., Bossé, S., Argaw, A., Hamoudi, D., Marcadet, L., Gamu, D., Fajardo, V. A., Yagita, H., Penninger, J. M., Russell Tupling, A., & Frenette, J.
- Affiliations
- Centre hospitalier universitaire de Québec (CA)
- University of Waterloo (CA)
- Institute of Molecular Biotechnology (AT)
- Corresponding author
- Frenette, Jérôme
- ORCID
- Venue
- Acta Neuropathologica Communications
- Published
- 2018-04-24
- Volume
- 6
- Issue
- 1
- Pages
- 31-31
- ISSN
- 2051-5960 (ISSN-L)
- PMC
- PMC5922009
- OpenAlex
- W2800829257
- Cited by
- 59
- References
- 40
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 11 · 2023: 11 · 2022: 4 · 2021: 8 · 2020: 9 · 2019: 5 · 2018: 2
- FWCI
- 2.13
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Acta Neuropathologica Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Constellation (Université du Québec à Chicoutimi) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Natural Sciences and Engineering Research Council of Canada (RGPIN 2016-05845)
- Institute of Musculoskeletal Health and Arthritis (JNM 123675)
- Jesse´s Journey
- Duchenne Alliance
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
- Health Sciences › Medicine › Genetics › Neurogenetic and Muscular Disorders Research
- Keywords
- Duchenne muscular dystrophy, RANK, RANKL, osteoprotegerin, mdx mice, muscle atrophy, muscle force, eccentric contraction, anti-RANKL antibody, SERCA, SERCA2a, dystrophin, skeletal muscle function, muscle-bone crosstalk, RANK/RANKL/OPG pathway
- MeSH terms
- Animals, Creatine Kinase, Disease Models, Animal, Mice, Inbred C57BL, Mice, Transgenic, Muscle Contraction, Muscular Dystrophies, RNA, Messenger, Signal Transduction, Mice, Inbred mdx, Muscle, Skeletal, Mice, Osteoprotegerin, Receptor Activator of Nuclear Factor-kappa B
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