The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Bone and morphogenetic protein signalling and muscle mass
Abstract
PURPOSE OF REVIEW: The purpose of this study is to discuss the involvement of bone and morphogenetic proteins (BMPs) in the control of muscle mass. RECENT FINDINGS: The transforming growth factor-beta (TGFβ) superfamily comprises a large number of secreted proteins that regulate a variety of fundamental biological processes. Sequence similarities define two ligand subfamilies: the TGFβ/Activin subfamily and the BMP subfamily. Within the members of TGFβ subfamily, myostatin emerged as the most critical ligand that affects muscle size and function. Indeed, mutations that inactivate Myostatin lead to important muscle growth in animals and humans. However, recent findings have increased the complexity of the TGFβ superfamily. Indeed, two independent groups have shown that BMP pathway, acting through Smad1/5/8, is the fundamental hypertrophic signal and dominates Myostatin signalling. Moreover, BMP-Smad1/5/8 negatively regulates a novel ubiquitin ligase, named MUSA1 that is required for muscle loss. This article reviews the rapid progress made in the last year regarding the signalling downstream TGFβ superfamily and its involvement in the homeostasis of adult muscle fibres. SUMMARY: The recent insights gained into the interplay of TGFβ and BMP signalling in muscle have challenged our pre-existing ideas of how the adult skeletal muscle phenotype is regulated in health and disease.
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“BMP pathway is activated in myostatin knockout and is sufficient, when induced, to promote muscle growth and to counteract muscle loss after denervation and in the absence of nutrients [6–8].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [8]
In the citing paper
“Mechanistically, muscle loss is due to FoxO-mediated activation of the ubiquitin–proteasome system together with the impairment of general autophagy and mitophagy pathways [25,31,32].”
From Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles (2019) · cites this paper as [32]
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1 retracted
Lokireddy, S., Wijesoma, I. W., Teng, S., Bonala, S., Gluckman, P. D., McFarlane, C., Sharma, M., & Kambadur, R. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.005 · Cited by 154
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Schiaffino, S., Dyar, K. A., Ciciliot, S., Blaauw, B., & Sandri, M. (2013) · The FEBS Journal · doi:10.1111/febs.12253 · Cited by 1,492
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Zhou, X., Wang, J. L., Lu, J., Song, Y., Kwak, K. S., Jiao, Q., Rosenfeld, R., Chen, Q., Boone, T. C., Simonet, W. S., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.011 · Cited by 960
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Sandri, M. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.023 · Cited by 689
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Yu, P. B., Deng, D. Y., Lai, C. S. C., Hong, C. C., Cuny, G. D., Bouxsein, M., Hong, D. W., McManus, P. M., Katagiri, T., Sachidanandan, C., et al. (2008) · Nature Medicine · doi:10.1038/nm.1888 · Cited by 641
A phase I/IItrial of MYO‐029 in adult subjects with muscular dystrophy
Wagner, K. R., Fleckenstein, J. L., Amato, A. A., Barohn, R. J., Bushby, K., Escolar, D. M., Flanigan, K. M., Pestronk, A., Tawil, R., Wolfe, G. I., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21338 · Cited by 481
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Sartori, R., Schirwis, E., Blaauw, B., Bortolanza, S., Zhao, J., Enzo, E., Stantzou, A., Mouisel, E., Toniolo, L., Ferry, A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2772 · Cited by 467
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Identification of Progenitor Cells That Contribute to Heterotopic Skeletogenesis
Lounev, V. Y., Ramachandran, R., Wosczyna, M. N., Yamamoto, M., Maidment, A. D. A., Shore, E. M., Glaser, D. L., Goldhamer, D. J., & Kaplan, F. S. (2009) · Journal of Bone and Joint Surgery · doi:10.2106/jbjs.h.01177 · Cited by 303
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Ulbricht, A., Eppler, F. J., Tapia, V. E., van der Ven, P. F. M., Hampe, N., Hersch, N., Vakeel, P., Stadel, D., Haas, A., Saftig, P., et al. (2013) · Current Biology · doi:10.1016/j.cub.2013.01.064 · Cited by 288
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Paul, P. K., Gupta, S. K., Bhatnagar, S., Panguluri, S. K., Darnay, B. G., Choi, Y., & Kumar, A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201006098 · Cited by 234
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Winbanks, C. E., Chen, J. L., Qian, H., Liu, Y., Bernardo, B. C., Beyer, C., Watt, K. I., Thomson, R. E., Connor, T., Turner, B. J., et al. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201211134 · Cited by 225
Cohen, S., Zhai, B., Gygi, S. P., & Goldberg, A. L. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201110067 · Cited by 205
Ono, Y., Calhabeu, F., Morgan, J. E., Katagiri, T., Amthor, H., & Zammit, P. S. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.95 · Cited by 198
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Goff, C. L., Mahaut, C., Abhyankar, A., Goff, W. L., Serre, V., Afenjar, A., Destrèe, A., Rocco, M. D., Héron, D., Jacquemont, S., et al. (2011) · Nature Genetics · doi:10.1038/ng.1016 · Cited by 161
Paul, P. K., Bhatnagar, S., Mishra, V. K., Srivastava, S., Darnay, B. G., Choi, Y., & Kumar, A. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06351-11 · Cited by 157
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Shi, J., Luo, L., Eash, J. K., Ibebunjo, C., & Glass, D. J. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.09.011 · Cited by 153
Krause, C., Guzman, A., & Knaus, P. I. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.01.007 · Cited by 148
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Beharry, A. W., Sandesara, P. B., Roberts, B. M., Ferreira, L. F., Senf, S. M., & Judge, A. R. (2014) · Journal of Cell Science · doi:10.1242/jcs.136390 · Cited by 128
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Nagpal, P., Plant, P. J., Correa, J., Bain, A., Takeda, M., Kawabe, H., Rotin, D., Bain, J. R., & Batt, J. A. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046427 · Cited by 85
Clever, J. L., Sakai, Y., Wang, R. A., & Schneider, D. B. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00388.2009 · Cited by 61
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Ratti, F., Ramond, F., Moncollin, V., Simonet, T., Milan, G., Méjat, A., Thomas, J.-L., Streichenberger, N., Gilquin, B., Matthias, P., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.600916 · Cited by 47
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Huang, P., Schulz, T. J., Beauvais, A., Tseng, Y., & Gussoni, E. (2014) · Nature Communications · doi:10.1038/ncomms5063 · Cited by 44
Collins‐Hooper, H., Sartori, R., Macharia, R., Visanuvimol, K., Foster, K., Matsakas, A., Flasskamp, H., Ray, S., Dash, P. R., Sandri, M., et al. (2014) · The Journals of Gerontology Series A · doi:10.1093/gerona/glt170 · Cited by 31
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Metadata
- Authors
- Sartori, R., & Sandri, M.
- Affiliations
- University of Padua (IT)
- Corresponding author
- Sandri, Marco
- Venue
- Current Opinion in Clinical Nutrition and Metabolic Care
- Published
- 2015-05
- Volume
- 18
- Issue
- 3
- Pages
- 215-220
- ISSN
- 1363-1950 (ISSN-L)
- OpenAlex
- W2076444039
- Cited by
- 22
- References
- 33
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2023: 2 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 2
- FWCI
- 0.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Clinical Nutrition & Metabolic Care (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- myostatin, TGF-beta superfamily, skeletal muscle mass, muscle hypertrophy, muscle atrophy, muscle growth
- MeSH terms
- Animals, Humans, Muscular Diseases, Signal Transduction, Transforming Growth Factor beta, Muscle, Skeletal, Bone Morphogenetic Proteins, Activins, Myostatin
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