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Treatment of sporadic inclusion body myositis with bimagrumab
Open accessAbstract
OBJECTIVE: To study activin signaling and its blockade in sporadic inclusion body myositis (sIBM) through translational studies and a randomized controlled trial. METHODS: We measured transforming growth factor β signaling by SMAD2/3 phosphorylation in muscle biopsies of 50 patients with neuromuscular disease (17 with sIBM). We tested inhibition of activin receptors IIA and IIB (ActRII) in 14 patients with sIBM using one dose of bimagrumab (n = 11) or placebo (n = 3). The primary outcome was the change in right thigh muscle volume by MRI at 8 weeks. Lean body mass, strength, and function were secondary outcomes. Twelve of the patients (10 bimagrumab, 2 placebo) participated in a subsequent 16-week observation phase. RESULTS: Muscle SMAD2/3 phosphorylation was higher in sIBM than in other muscle diseases studied (p = 0.003). Eight weeks after dosing, the bimagrumab-treated patients increased thigh muscle volume (right leg +6.5% compared with placebo, p = 0.024; left leg +7.6%, p = 0.009) and lean body mass (+5.7% compared with placebo, p = 0.014). Subsequently, bimagrumab-treated patients had improved 6-minute walking distance, which peaked at 16 weeks (+14.6%, p = 0.008) compared with placebo. There were no serious adverse events; the main adverse events with bimagrumab were mild acne and transient involuntary muscle contractions. CONCLUSIONS: Transforming growth factor β superfamily signaling, at least through ActRII, is implicated in the pathophysiology of sIBM. Inhibition of ActRII increased muscle mass and function in this pilot trial, offering a potential novel treatment of sIBM. CLASSIFICATION OF EVIDENCE: This study provides Class I evidence that for patients with inclusion body myositis, bimagrumab increases thigh muscle volume at 8 weeks.
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“blocking these receptors can result in profound muscle growth in animals and humans18–22”
From GDF8 and activin A blockade protects against GLP-1–induced muscle loss while enhancing fat loss in obese male mice and non-human primates (2025) · cites this paper as [18]
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Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
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Rommel, C., Clarke, B. A., Zimmermann, S., Nuñez, L., Rossman, R., Reid, K., Moelling, K., Yancopoulos, G. D., & Glass, D. J. (1999) · Science · doi:10.1126/science.286.5445.1738 · Cited by 760
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Metadata
- Authors
- Amato, A. A., Sivakumar, K., Goyal, N., David, W. S., Salajegheh, M., Praestgaard, J., Lach-Trifilieff, E., Trendelenburg, A.-U., Laurent, D., Glass, D. J., Roubenoff, R., Tseng, B. S., & Greenberg, S. A.
- Affiliations
- Brigham and Women's Hospital (US)
- From Brigham and Women's Hospital and Harvard Medical School (A.A.A., M.S., S.A.G.), Boston; Boston Children's Hospital (S.A.G.); Harvard–Massachusetts Institute of Technology (S.A.G.), Division of Health Sciences and Technology, Cambridge, MA; Barrow Neurological Institute (K.S.), Phoenix AZ; Massachusetts General Hospital (N.G., W.S.D.), Boston; Novartis Institutes for Biomedical Research (E.L.-T., A.-U.T., D.L., D.J.G., R.R., B.S.T.), Cambridge, MA and Basel, Switzerland; and Novartis...
- ORCID
- Venue
- Neurology
- Published
- 2014-12-09
- Volume
- 83
- Issue
- 24
- Pages
- 2239-2246
- ISSN
- 0028-3878 (ISSN-L)
- 1526-632X
- PMC
- PMC4277670
- OpenAlex
- W2163067250
- Semantic Scholar
- 6c0c2ff1bf6a3ea2dd7c0ab956dec951fc496e44
- Cited by
- 210
- References
- 24
- Citations by year
- 2026: 13 · 2025: 13 · 2024: 11 · 2023: 10 · 2022: 16 · 2021: 25 · 2020: 20 · 2019: 13 · 2018: 21 · 2017: 22 · 2016: 28 · 2015: 18
- FWCI
- 17.17
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Neurology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Rheumatology › Inflammatory Myopathies and Dermatomyositis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Genetics (clinical) › Neurogenetic and Muscular Disorders Research
- Keywords
- sporadic inclusion body myositis, bimagrumab, TGF-beta signaling, Smad2/3 phosphorylation, thigh muscle volume, lean body mass, 6-minute walk distance, neuromuscular disorders, muscle mass and function
- MeSH terms
- Adult, Aged, Aged, 80 and over, Antibodies, Monoclonal, Double-Blind Method, Exercise Test, Female, Humans, Immunologic Factors, Magnetic Resonance Imaging, Male, Middle Aged, Neuromuscular Diseases, Organ Size, Phosphorylation, Thigh, Treatment Outcome, Muscle, Skeletal, Myositis, Inclusion Body, Antibodies, Blocking, Activin Receptors, Type II, Smad2 Protein, Smad3 Protein, Antibodies, Monoclonal, Humanized
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