The DOI matches its Crossref record; 38 of the 39 references it cites were found in a registry or an index.
The effects of a soluble activin type IIB receptor on obesity and insulin sensitivity
Open accessAbstract
Background Myostatin, also known as Growth and Differentiation Factor 8, is a secreted protein that inhibits muscle growth. Disruption of myostatin signaling increases muscle mass and decreases glucose, but it is unclear whether these changes are related. We treated mice on chow and high-fat diets with a soluble activin receptor type IIB (ActRIIB, RAP-031), which is a putative endogenous signaling receptor for myostatin and other ligands of the TGF-beta superfamily.Results After 4 weeks, RAP-031 increased lean and muscle mass, grip strength and contractile force. RAP-031 enhanced the ability of insulin to suppress glucose production under clamp conditions in high-fat fed mice, but did not significantly change insulin-mediated glucose disposal. The hepatic insulin-sensitizing effect of RAP-031 treatment was associated with increased adiponectin levels. RAP-031 treatment for 10 weeks further increased muscle mass and drastically reduced fat content in mice on either chow or high-fat diet. RAP-031 suppressed hepatic glucose production and increased peripheral glucose uptake in chow-fed mice. In contrast, RAP-031 suppressed glucose production with no apparent change in glucose disposal in high-fat-diet mice.Conclusion Our findings show that disruption of ActRIIB signaling is a viable pharmacological approach for treating obesity and diabetes.
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“Inhibition of ActRII signaling through genetic deletion of muscle ActRIIA/B, antibody blockade of ActRIIA/B, or treatment with a soluble ActRIIB decoy receptor all lead to significant increases in muscle mass [[15], [16], [17]].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [15]
In the citing paper
“It is well appreciated that ActRII ligands such as myostatin and activin A negatively regulate muscle size”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [15]
In the citing paper
“ActRII blockade increases muscle size as well as reduces fat mass [15,18]”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [15]
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Cites
Inflammation and metabolic disorders
Hotamisligil, G. S. (2006) · Nature · doi:10.1038/nature05485 · Cited by 9,199
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
Obesity and insulin resistance
Kahn, B. B., & Flier, J. S. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10842 · Cited by 3,345
Adiponectin and Adiponectin Receptors
Kadowaki, T., & Yamauchi, T. (2005) · Endocrine Reviews · doi:10.1210/er.2005-0005 · Cited by 2,634
Muscle as an Endocrine Organ: Focus on Muscle-Derived Interleukin-6
Pedersen, B. K., & Febbraio, M. A. (2008) · Physiological Reviews · doi:10.1152/physrev.90100.2007 · Cited by 2,388
Double muscling in cattle due to mutations in the myostatin gene
McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039
Dystrophin protects the sarcolemma from stresses developed during muscle contraction
Petrof, B. J., Shrager, J. B., Stedman, H. H., Kelly, A. M., & Sweeney, H. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3710 · Cited by 1,526
Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child
Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040933 · Cited by 1,399
Induction of Cachexia in Mice by Systemically Administered Myostatin
Zimmers, T. A., Davies, M. V., Koniaris, L. G., Haynes, P. A., Esquela‐Kerscher, A., Tomkinson, K. N., McPherron, A. C., Wolfman, N. M., & Lee, S. (2002) · Science · doi:10.1126/science.1069525 · Cited by 908
Functional improvement of dystrophic muscle by myostatin blockade
Bogdanovich, S., Krag, T. O. B., Barton, E. R., Morris, L. D., Whittemore, L.-A., Ahima, R. S., & Khurana, T. S. (2002) · Nature · doi:10.1038/nature01154 · Cited by 831
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Items 101–140 of 140
Dichtel, L. E., Kimball, A., Bollinger, B., Scarff, G., Gerweck, A. V., Bredella, M. A., & Haines, M. S. (2024) · Physiological Reports · doi:10.14814/phy2.16169 · Cited by 9
Tavoian, D., Arnold, W. D., Mort, S. C., & Lacalle, S. D. (2019) · PLoS ONE · doi:10.1371/journal.pone.0225283 · Cited by 11
Li, M., Tang, X., You, W., Wang, Y., Chen, Y., Liu, Y., Yuan, H., Gao, C., Chen, X., Xiao, Z., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.06.011 · Cited by 9
Lee, S.-J. (2012) · Muscle · doi:10.1016/b978-0-12-381510-1.00079-x · Cited by 8
Puolakkainen, T., Rummukainen, P., Nieminen-Pihala, V., Ritvos, O., Savontaus, E., & Kiviranta, R. (2022) · Calcified Tissue International · doi:10.1007/s00223-021-00934-0 · Cited by 9
Saremi, A., & Parastesh, M. (2019) · International Journal of Diabetes and Metabolism · doi:10.1159/000497712 · Cited by 8
Cheng, J., Lee, J., Liu, Y., Wang, Y., Duan, M., & Zeng, Z. (2023) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/171300 · Cited by 7
Myostatin in Obesity: A Molecular Link Between Metabolic Dysfunction and Musculotendinous Remodeling
Cesanelli, L., Minderis, P., Fokin, A., Ratkevičius, A., Satkunskienė, D., & Degens, H. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020967 · Cited by 7
Advancements in the management of obesity: a review of current evidence and emerging therapies
Abdalla, M. A., Ssemmondo, E., Mark‐Wagstaff, C., & Sathyapalan, T. (2024) · Expert Review of Endocrinology & Metabolism · doi:10.1080/17446651.2024.2347258 · Cited by 7
Wang, J., Zhang, K., Hou, X., Yue, W., Yang, H., Chen, X., Wang, J., & Wang, C. (2020) · PeerJ · doi:10.7717/peerj.9673 · Cited by 6
Speed and endurance: you can have it all
Lee, S. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00618.2010 · Cited by 4
Possibility of small-molecule-based pharmacotherapy for sarcopenia
Watanabe, Y., & Miyagoe‐Suzuki, Y. (2015) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.4.73 · Cited by 3
Barbé, C., Loumaye, A., Lause, P., Ritvos, O., & Thissen, J. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.677746 · Cited by 4
Assessment of goat activin receptor type IIB knockdown by short hairpin RNAsin vitro
Patel, A. K., Tripathi, A. K., Shah, R. K., Patel, U. A., & Joshi, C. G. (2014) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2014.922574 · Cited by 3
Cadena, S. M., Bogdanovich, S., Khurana, T. S., Pullen, A. E., Pearsall, R. S., Curran, E., Faucette, R., Lane, J., Seehra, J. S., Lachey, J. L., et al. (2026) · PLoS ONE · doi:10.1371/journal.pone.0342666 · Cited by 2
Self-citationInnovative approaches to the treatment of obesity: from pharmacotherapy to nanomedicine
Romantsova, T. I. (2024) · Obesity and metabolism · doi:10.14341/omet13184 · Cited by 4
Equine obesity: concepts and mechanisms
Morrison, P. K. (2015) · University of Liverpool · doi:10.17638/02035680 · Cited by 2
Beige fat is dispensable for the metabolic benefits associated with myostatin deletion
Marchildon, F., Chi, J., O'Connor, S., Bediako, H., & Cohen, P. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101120 · Cited by 2
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Béchir, N., Pecchi, É., Vilmen, C., Bernard, M., Bendahan, D., & Giannesini, B. (2018) · Muscle & Nerve · doi:10.1002/mus.26306 · Cited by 1
Miedany, Y. M. E. (2022) · Springer eBooks · doi:10.1007/978-3-030-87950-1_3 · Cited by 1
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Foss, S. (2013) · Cited by 1
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Aydogdu, T. (2010)
Myostatin as a Potential Therapeutic Target for Obesity and Insulin Resistance
Jeong, K., & Choi, C. S. (2011) · The Korean Journal of Obesity · doi:10.7570/kjo.2011.20.3.91 · Cited by 1
The Effect of Myostatin on Glucose Metabolism and Insulin Sensitivity
Ghozlan, M. (2013) · Libraries and Cultural Resources (University of Calgary) · doi:10.11575/prism/28087
Khurana, T. S., Pistilli, E. E., Bogdanovich, S., Mosqueira, M., Lachey, J. L., Kunkel, L. M., Wagner, K. R., Rahimov, F., King, O. D., Warsing, L. C., et al. (2011)
Self-citationPoikonen, A. R. (2016) · Jyväskylä University Digital Archive (University of Jyväskylä)
Myostatin’s Role in Genetic Control of Muscle Size and Strength
Hittel, D. S. (2019) · Routledge eBooks · doi:10.4324/9781315146287-27
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Moyer, A. L. (2015)
Obesity, Myokines, and Metabolic Health
Malandrino, N., & Ahima, R. S. (2023) · Springer eBooks · doi:10.1007/978-3-319-12125-3_56-1
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Relizani, K. (2014) · theses.fr (ABES) · doi:10.70675/20978d43z02f0z4a1ezb428zf5dab86d9abf
Shao, C., Lin, H., Yu, J., Chen, H., Ren, Y., Ren, J., Zeng, Y., Wu, Y., Zhang, Q., & Xiao, X. (2026) · Diabetes Obesity and Metabolism · doi:10.1111/dom.71156
Bogdanovich, S., Pistilli, E. E., & Khurana, T. S. (2026) · Muscles · doi:10.3390/muscles5030058
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Metadata
- Authors
- Akpan, I., Goncalves, M. D., Dhir, R., Yin, X., Pistilli, E. E., Bogdanovich, S., Khurana, T. S., Ucran, J., Lachey, J., & Ahima, R. S.
- Affiliations
- University of Pennsylvania Health System (US)
- University of Pennsylvania (US)
- Acceleron Pharma (United States) (US)
- Corresponding author
- Ahima, R S
- Venue
- International Journal of Obesity
- Published
- 2009-08-11
- Volume
- 33
- Issue
- 11
- Pages
- 1265-1273
- ISSN
- 0307-0565 (ISSN-L)
- 1476-5497
- PMC
- PMC2783781
- OpenAlex
- W2050592095
- Cited by
- 140
- References
- 39
- Citations by year
- 2026: 4 · 2025: 1 · 2024: 8 · 2023: 7 · 2022: 4 · 2021: 8 · 2020: 9 · 2019: 6 · 2018: 4 · 2017: 4 · 2016: 7 · 2015: 12 · 2014: 17 · 2013: 12 · 2012: 10
- FWCI
- 8.28
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- International Journal of Obesity (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (P01DK049210, R01DK062348, P30 DK 19525, P30DK019525)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- myostatin, obesity, insulin sensitivity, high-fat diet, hepatic glucose production, glucose uptake, muscle mass, adiponectin, TGF-beta superfamily, diabetes mellitus
- MeSH terms
- Animals, Insulin Resistance, Male, Mice, Inbred C57BL, Obesity, Solubility, Glucose Clamp Technique, Signal Transduction, Case-Control Studies, Muscle, Skeletal, Activin Receptors, Type II, Mice, Myostatin
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