Smad2 and 3 transcription factors control muscle mass in adulthood
Abstract
Loss of muscle mass occurs in a variety of diseases, including cancer, chronic heart failure, aquired immunodeficiency syndrome, diabetes, and renal failure, often aggravating pathological progression. Preventing muscle wasting by promoting muscle growth has been proposed as a possible therapeutic approach. Myostatin is an important negative modulator of muscle growth during myogenesis, and myostatin inhibitors are attractive drug targets. However, the role of the myostatin pathway in adulthood and the transcription factors involved in the signaling are unclear. Moreover, recent results confirm that other transforming growth factor-β (TGF-β) members control muscle mass. Using genetic tools, we perturbed this pathway in adult myofibers, in vivo, to characterize the downstream targets and their ability to control muscle mass. Smad2 and Smad3 are the transcription factors downstream of myostatin/TGF-β and induce an atrophy program that is muscle RING-finger protein 1 (MuRF1) independent. Furthermore, Smad2/3 inhibition promotes muscle hypertrophy independent of satellite cells but partially dependent of mammalian target of rapamycin (mTOR) signaling. Thus myostatin and Akt pathways cross-talk at different levels. These findings point to myostatin inhibitors as good drugs to promote muscle growth during rehabilitation, especially when they are combined with IGF-1-Akt activators.
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Rapamycin treatment or mTOR knockdown reverts the hypertrophic effect of myostatin blockade, indicating cross-talk between myostatin and the AKT/mTOR axis.
“Indeed, rapamycin treatment or mTOR knockdown revert the hypertrophic effect of myostatin blockade17,18.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [17]
Inhibition of Smad2/3 is sufficient to promote muscle growth, suggesting that genes involved in protein turnover are targets of these transcription factors.
“Importantly, just inhibition of Smad2/3 is sufficient to promote muscle growth17,18, suggesting that genes involved in protein turnover are the target of these transcription factors.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [17]
Inhibition of SMAD 2 and SMAD 3 is sufficient to induce muscle growth.
“Accordingly, inhibition of SMAD 2 and SMAD 3 is sufficient to induce muscle growth [4, 5].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [4]
Cites
Identification of ubiquitin ligases required for skeletal muscle atrophy.
Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521 · see citing works
Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012 · see citing works
Self-citationBodine, 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 · see citing works
Smad transcription factorsPreprint
Massagué, J., Seoane, J., & Wotton, D. (2005) · Genes & Development · doi:10.1101/gad.1350705 · Cited by 2,432 · see citing works
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 · see citing works
Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964 · see citing works
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works
Self-citationAtrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774 · see citing works
Regulation of myostatin activity and muscle growth
Lee, S.-J., & McPherron, A. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151270098 · Cited by 1,616 · see citing works
Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539 · see citing works
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 · see citing works
IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice
Cai, D., Frantz, J. D., Tawa, N. E., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.027 · Cited by 1,367 · see citing works
Clop, A., Marcq, F., Takeda, H., Pirottin, D., Tordoir, X., Bibé, B., Bouix, J., Caiment, F., Elsen, J.-M., Eychenne, F., et al. (2006) · Nature Genetics · doi:10.1038/ng1810 · Cited by 1,260 · see citing works
Musarò, A., McCullagh, K., Paul, A., Houghton, L., Dobrowolny, G., Molinaro, M., Barton, E. R., L Sweeney, H., & Rosenthal, N. (2001) · Nature Genetics · doi:10.1038/84839 · Cited by 1,137 · see citing works
Seoane, J., Le, H.-V., Shen, L., Anderson, S. A., & Massagué, J. (2004) · Cell · doi:10.1016/s0092-8674(04)00298-3 · Cited by 1,029 · see citing works
Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974 · see citing works
Self-citationMyostatin Inhibits Myoblast Differentiation by Down-regulating MyoD Expression
Langley, B. C., Thomas, M., Bishop, A., Sharma, M., Gilmour, S., & Kambadur, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204291200 · Cited by 910 · see citing works
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 · see citing works
Signaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 830 · see citing works
Self-citationMosher, D. S., Quignon, P., Bustamante, C. D., Sutter, N. B., Mellersh, C. S., Parker, H. G., & Ostrander, E. A. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030079 · Cited by 826 · see citing works
REGULATION OF MUSCLE MASS BY MYOSTATIN
Lee, S.-J. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.012103.135836 · Cited by 819 · see citing works
Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size
Trendelenburg, A. U., Meyer, A., Rohner, D., Boyle, J., Hatakeyama, S., & Glass, D. J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00105.2009 · Cited by 792 · see citing works
Musarò, A., McCullagh, K. J. A., Naya, F. J., Olson, E. N., & Rosenthal, N. A. (1999) · Nature · doi:10.1038/23060 · Cited by 652 · see citing works
Sacheck, J. M., Ohtsuka, A., McLary, S. C., & Goldberg, A. L. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00073.2004 · Cited by 606 · see citing works
Sacheck, J. M., Hyatt, J. K., Raffaello, A., Thomas Jagoe, R., Roy, R. R., Reggie Edgerton, V., Lecker, S. H., & Goldberg, A. L. (2007) · The FASEB Journal · doi:10.1096/fj.06-6604com · Cited by 585 · see citing works
Rebbapragada, A., Benchabane, H., Wrana, J. L., Celeste, A. J., & Attisano, L. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7230-7242.2003 · Cited by 566 · see citing works
Inhibition of myostatin in adult mice increases skeletal muscle mass and strength
Whittemore, L.-A., Song, K., Li, X., Aghajanian, J. D., Davies, M. V., Girgenrath, S., Hill, J. J., Jalenak, M., Kelley, P. E., Knight, A., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02953-4 · Cited by 503 · see citing works
Regulation of muscle growth by multiple ligands signaling through activin type II receptors
Lee, S.-J., Reed, L. A., Davies, M. V., Girgenrath, S., Goad, M. E. P., Tomkinson, K. N., Wright, J. F., Barker, C., Ehrmantraut, G., Holmstrom, J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505996102 · Cited by 501 · see citing works
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 · see citing works
McFarlane, C., Plummer, E., Thomas, M., Hennebry, A., Ashby, M. G., Ling, N., Smith, H., Sharma, M., & Kambadur, R. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20757 · Cited by 480 · see citing works
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1999) · Nature Genetics · doi:10.1038/10320 · Cited by 471 · see citing works
Activation of latent myostatin by the BMP-1/tolloid family of metalloproteinases
Wolfman, N. M., McPherron, A. C., Pappano, W. N., Davies, M. V., Song, K., Tomkinson, K. N., Wright, J. F., Zhao, L., Sebald, S. M., Greenspan, D. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2534946100 · Cited by 454 · see citing works
Conditional Activation of Akt in Adult Skeletal Muscle Induces Rapid Hypertrophy
Lai, K.-M. V., Gonzalez, M., Poueymirou, W. T., Kline, W. O., Na, E., Zlotchenko, E., Stitt, T. N., Economides, A. N., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9295-9304.2004 · Cited by 442 · see citing works
Pallafacchina, G., Calabria, E., Serrano, A. L., Kalhovde, J. M., & Schiaffino, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142166599 · Cited by 402 · see citing works
Fast/Glycolytic Muscle Fiber Growth Reduces Fat Mass and Improves Metabolic Parameters in Obese Mice
Izumiya, Y., Hopkins, T., Morris, C., Sato, K., Zeng, L., Viereck, J., Hamilton, J. A., Ouchi, N., LeBrasseur, N. K., & Walsh, K. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.003 · Cited by 395 · see citing works
Ohanna, M., Sobering, A. K., Lapointe, T., Lorenzo, L., Praud, C., Petroulakis, E., Sonenberg, N., Kelly, P. A., Sotiropoulos, A., & Pende, M. (2005) · Nature Cell Biology · doi:10.1038/ncb1231 · Cited by 392 · see citing works
Lower skeletal muscle mass in male transgenic mice with muscle-specific overexpression of myostatin
Reisz‐Porszasz, S., Bhasin, S., Artaza, J. N., Shen, R., Sinha‐Hikim, I., Hogue, A., Fielder, T. J., & González-Cadavid, N. F. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00107.2003 · Cited by 333 · see citing works
Lagirand-Cantaloube, J., Offner, N., Csibi, A., Leibovitch, M.-P., Batonnet‐Pichon, S., Tintignac, L. A. J., Segura, C. T., & Leibovitch, S. A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.52 · Cited by 328 · see citing works
Regulation of Muscle Protein Degradation
Lee, S. W., Dai, G., Hu, Z., Wang, X., Du, J., & Mitch, W. E. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000127211.86206.e1 · Cited by 324 · see citing works
Quadrupling Muscle Mass in Mice by Targeting TGF-ß Signaling Pathways
Lee, S.-J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000789 · Cited by 316 · see citing works
The muscle-specific ubiquitin ligase atrogin-1/MAFbx mediates statin-induced muscle toxicity
Hanai, J., Cao, P., Tanksale, P., Imamura, S., Koshimizu, E., Zhao, J., Kishi, S., Yamashita, M., Phillips, P. S., Sukhatme, V. P., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32741 · Cited by 281 · see citing works
Allen, D. L., & Unterman, T. G. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00542.2005 · Cited by 264 · see citing works
A FoxO–Smad synexpression group in human keratinocytes
Gomis, R. R., Alarcón, C. R., He, W., Wang, Q., Seoane, J., Lash, A., & Massagué, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605333103 · Cited by 245 · see citing works
Durieux, A., Amirouche, A., Banzet, S., Koulmann, N., Bonnefoy, R., Pasdeloup, M., Mouret, C., Bigard, X. A., Peinnequin, A., & Freyssenet, D. G. (2007) · Endocrinology · doi:10.1210/en.2006-1500 · Cited by 162 · see citing works
Molecular and Cellular Determinants of Skeletal Muscle Atrophy and Hypertrophy
Sartorelli, V., & Fulco, M. (2004) · Science s STKE · doi:10.1126/stke.2442004re11 · Cited by 145 · see citing works
Welle, S. L., Burgess, K., & Mehta, S. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90862.2008 · Cited by 117 · see citing works
Muscle growth after postdevelopmental myostatin gene knockout
Welle, S. L., Bhatt, K. S., Pinkert, C. A., Tawil, R., & Thornton, C. A. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00531.2006 · Cited by 113 · see citing works
Functional in vivo gene transfer into the myofibers of adult skeletal muscle
Donà, M., Sandri, M., Rossini, K., Dell’Aica, I., Podhorska‐Okołów, M., & Carraro, U. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.11.032 · Cited by 95 · see citing works
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Sarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797 · see citing works
Self-citationMechanisms regulating skeletal muscle growth and atrophy
Schiaffino, S., Dyar, K. A., Ciciliot, S., Blaauw, B., & Sandri, M. (2013) · The FEBS Journal · doi:10.1111/febs.12253 · Cited by 1,492 · see citing works
Self-citationCellular and molecular mechanisms of muscle atrophy
Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284 · see citing works
Self-citationMuscle wasting in disease: molecular mechanisms and promising therapies
Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089 · see citing works
Mechanisms of muscle atrophy and hypertrophy: implications in health and disease
Sartori, R., Romanello, V., & Sandri, M. (2021) · Nature Communications · doi:10.1038/s41467-020-20123-1 · Cited by 940 · see citing works
Self-citationRegulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
Schiaffino, S., & Mammucari, C. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-4 · Cited by 816 · see citing works
“Myostatin, together with activin A, another member of the TGFb family, acts via its receptor activin receptor IIB (ActRIIB) on Smad2 and Smad3, inhibitors of Akt; conversely, mTOR inhibits Smads [17,18].”
BackgroundSelf-citationMyostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size
Trendelenburg, A. U., Meyer, A., Rohner, D., Boyle, J., Hatakeyama, S., & Glass, D. J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00105.2009 · Cited by 792 · see citing works
Exercise is the real polypill.
Fiuza-Luces, C., Garatachea, N., Berger, N. A., & Lucia, A. (2013) · Physiology · doi:10.1152/physiol.00019.2013 · Cited by 791 · see citing works
Transcriptional mechanisms regulating skeletal muscle differentiation, growth and homeostasis
Braun, T., & Gautel, M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3118 · Cited by 713 · see citing works
Mitochondrial fission and remodelling contributes to muscle atrophy
Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596 · see citing works
Self-citationA review on the mechanisms of blood-flow restriction resistance training-induced muscle hypertrophy
Pearson, S. J., & Hussain, S. R. (2015) · Sports Medicine · doi:10.1007/s40279-014-0264-9 · Cited by 592 · see citing works
Signaling pathways controlling skeletal muscle mass
Egerman, M. A., & Glass, D. J. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.857291 · Cited by 555 · see citing works
GDF11 increases with age and inhibits skeletal muscle regeneration
Egerman, M. A., Cadena, S. M., Gilbert, J. A., Meyer, A., Nelson, H. N., Swalley, S. E., Mallozzi, C., Jacobi, C., Jennings, L. L., Clay, I., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.010 · Cited by 527 · see citing works
Role of Skeletal Muscle in Insulin Resistance and Glucose Uptake
Merz, K. E., & Thurmond, D. C. (2020) · Comprehensive Physiology · doi:10.1002/cphy.c190029 · Cited by 494 · see citing works
mTOR as a key regulator in maintaining skeletal muscle mass
Yoon, M.-S. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00788 · Cited by 495 · see citing works
BMP signaling controls muscle mass
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 · see citing works
Self-citationSandri, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.056 · Cited by 451 · see citing works
Self-citationMyostatin and the skeletal muscle atrophy and hypertrophy signaling pathways
Rodriguez, J., Vernus, B., Chelh, I., Cassar-Malek, I., Gabillard, J. C., Hadj Sassi, A., Seiliez, I., Picard, B., & Bonnieu, A. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1689-x · Cited by 397 · see citing works
Signaling pathways perturbing muscle mass.
Glass, D. J. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833862df · Cited by 359 · see citing works
Sandri, M., Barberi, L., Bijlsma, A. Y., Blaauw, B., Dyar, K. A., Milan, G., Mammucari, C., Meskers, C. G. M., Pallafacchina, G., Paoli, A., et al. (2013) · Biogerontology · doi:10.1007/s10522-013-9432-9 · Cited by 340 · see citing works
Self-citationMyostatin/activin pathway antagonism: molecular basis and therapeutic potential
Han, H. Q., Zhou, X., Mitch, W. E., & Goldberg, A. L. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.019 · Cited by 314 · see citing works
Lach-Trifilieff, E., Minetti, G. C., Sheppard, K., Ibebunjo, C., Feige, J. N., Hartmann, S., Brachat, S., Rivet, H., Koelbing, C., Morvan, F., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01307-13 · Cited by 306 · see citing works
Autophagy as a new therapeutic target in Duchenne muscular dystrophy
De Palma, C., Morisi, F., Cheli, S., Pambianco, S., Cappello, V, Vezzoli, M., Rovere-Querini, P., Moggio, M., Ripolone, M., Francolini, M., et al. (2012) · Cell Death & Disease · doi:10.1038/cddis.2012.159 · Cited by 269 · see citing works
Self-citationThe influence of skeletal muscle on systemic aging and lifespan
Demontis, F., Piccirillo, R., Goldberg, A. L., & Perrimon, N. (2013) · Aging Cell · doi:10.1111/acel.12126 · Cited by 238 · see citing works
Stress-induced Skeletal Muscle Gadd45a Expression Reprograms Myonuclei and Causes Muscle Atrophy
Ebert, S. M., Dyle, M. C., Kunkel, S. D., Bullard, S. A., Bongers, K. S., Fox, D. K., Dierdorff, J. M., Foster, E. D., & Adams, C. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374777 · Cited by 221 · see citing works
The bone morphogenetic protein axis is a positive regulator of skeletal muscle mass
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 · see citing works
Winbanks, C. E., Weeks, K. L., Thomson, R. E., Sepulveda, P. V., Beyer, C., Qian, H., Chen, J. L., Allen, J. M., Lancaster, G. I., Febbraio, M. A., et al. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201109091 · Cited by 218 · see citing works
Roberts, M. D., McCarthy, J. J., Hornberger, T. A., Phillips, S. M., Mackey, A. L., Nader, G. A., Boppart, M. D., Kavazis, A. N., Reidy, P. T., Ogasawara, R., et al. (2023) · Physiological Reviews · doi:10.1152/physrev.00039.2022 · Cited by 214 · see citing works
Treatment of sporadic inclusion body myositis with bimagrumab
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., et al. (2014) · Neurology · doi:10.1212/wnl.0000000000001070 · Cited by 210 · see citing works
Dong, J., Dong, Y., Dong, Y., Chen, F., Mitch, W. E., & Zhang, L. (2016) · International Journal of Obesity · doi:10.1038/ijo.2015.200 · Cited by 212 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Self-citationMyostatin and Sarcopenia: Opportunities and Challenges - A Mini-Review
White, T. A., & LeBrasseur, N. K. (2014) · Gerontology · doi:10.1159/000356740 · Cited by 191 · see citing works
Enoki, Y., Watanabe, H., Arake, R., Sugimoto, R., Imafuku, T., Tominaga, Y., Ishima, Y., Kotani, S., Nakajima, M., Tanaka, M., et al. (2016) · Scientific Reports · doi:10.1038/srep32084 · Cited by 188 · see citing works
TGFβ and BMP signaling in skeletal muscle: potential significance for muscle-related disease
Sartori, R., Gregorevic, P., & Sandri, M. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2014.06.002 · Cited by 177 · see citing works
Self-citationJunB transcription factor maintains skeletal muscle mass and promotes hypertrophy
Raffaello, A., Milan, G., Masiero, E., Carnio, S., Lee, D., Lanfranchi, G., Goldberg, A. L., & Sandri, M. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201001136 · Cited by 156 · see citing works
Self-citationAnabolic and catabolic pathways regulating skeletal muscle mass
McCarthy, J. J., & Esser, K. A. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833781b5 · Cited by 148 · see citing works
Sarcopenia and cachexia: the adaptations of negative regulators of skeletal muscle mass
Sakuma, K., & Yamaguchi, A. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0052-4 · Cited by 137 · see citing works
The effects of a soluble activin type IIB receptor on obesity and insulin sensitivity
Akpan, I., Goncalves, M. D., Dhir, R., Yin, X., Pistilli, E. E., Bogdanovich, S., Khurana, T. S., Ucran, J., Lachey, J., & Ahima, R. S. (2009) · International Journal of Obesity · doi:10.1038/ijo.2009.162 · Cited by 140 · see citing works
Bergen, H. R., Farr, J. N., Vanderboom, P. M., Atkinson, E. J., White, T. A., Singh, R. J., Khosla, S., & LeBrasseur, N. K. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0047-5 · Cited by 137 · see citing works
Protein breakdown in cancer cachexia
Sandri, M. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.11.002 · Cited by 134 · see citing works
Self-citationSkeletal muscle gene expression in response to resistance exercise: sex specific regulation
Liu, D., Sartor, M. A., Nader, G. A., Gutmann, L., Treutelaar, M. K., Pistilli, E. E., IglayReger, H. B., Burant, C. F., Hoffman, E. P., & Gordon, P. M. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-659 · Cited by 122 · see citing works
Myokines in skeletal muscle physiology and metabolism: Recent advances and future perspectives
Das, D. K., Graham, Z. A., & Cardozo, C. P. (2020) · Acta Physiologica · doi:10.1111/apha.13367 · Cited by 129 · see citing works
Goodman, C. A., Dietz, J. M., Jacobs, B. L., McNally, R. M., You, J.-S., & Hornberger, T. A. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.04.047 · Cited by 121 · see citing works
JNK regulates muscle remodeling via myostatin/SMAD inhibition
Lessard, S. J., MacDonald, T. L., Pathak, P., Han, M. S., Coffey, V. G., Edge, J., Rivas, D. A., Hirshman, M. F., Davis, R. J., & Goodyear, L. J. (2018) · Nature Communications · doi:10.1038/s41467-018-05439-3 · Cited by 119 · see citing works
Posttranslational modifications control FoxO3 activity during denervation
Bertaggia, E., Coletto, L., & Sandri, M. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00142.2011 · Cited by 114 · see citing works
Self-citationMueller, T. C., Bachmann, J., Prokopchuk, O., Friess, H., & Martignoni, M. E. (2016) · BMC Cancer · doi:10.1186/s12885-016-2121-8 · Cited by 95 · see citing works
Androgen-mediated regulation of skeletal muscle protein balance
Rossetti, M. L., Steiner, J. L., & Gordon, B. S. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.02.031 · Cited by 95 · see citing works
Akt deficiency attenuates muscle size and function but not the response to ActRIIB inhibition
Goncalves, M. D., Pistilli, E. E., Balduzzi, A., Birnbaum, M. J., Lachey, J., Khurana, T. S., & Ahima, R. S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012707 · Cited by 69 · see citing works
An embryonic CaVβ1 isoform promotes muscle mass maintenance via GDF5 signaling in adult mouse
Traoré, M., Gentil, C., Benedetto, C., Hogrel, J.-Y., De la Grange, P., Cadot, B., Benkhelifa-Ziyyat, S., Julien, L., Lemaitre, M., Ferry, A., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aaw1131 · Cited by 36 · see citing works
Lu, L., Wang, D.-T., Shi, Y., Yin, Y., Wei, L.-B., Zou, Y.-C., Huang, B., Zhao, Y., Wang, M., Wan, H., et al. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2013.06.027 · Cited by 33 · see citing works
New roles for Smad signaling and phosphatidic acid in the regulation of skeletal muscle mass
Goodman, C. A., & Hornberger, T. A. (2014) · F1000Prime Reports · doi:10.12703/p6-20 · Cited by 30 · see citing works
Wang, X., Wei, Z., Gu, M., Zhu, L., Hai, C., Di, A., Wu, D., Bai, C., Su, G., Liu, X., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415707 · Cited by 29 · see citing works
- Authors
- Sartori, R., Milan, G., Patron, M., Mammucari, C., Blaauw, B., Abraham, R., & Sandri, M.
- Affiliations
- Veneto Institute of Molecular Medicine (IT)
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2009-06
- Volume
- 296
- Issue
- 6
- Pages
- C1248-C1257
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2035555824
- Cited by
- 517
- References
- 48
- Citations by year
- 2026: 32 · 2025: 24 · 2024: 25 · 2023: 24 · 2022: 28 · 2021: 34 · 2020: 32 · 2019: 24 · 2018: 37 · 2017: 23 · 2016: 24 · 2015: 28 · 2014: 38 · 2013: 41 · 2012: 38
- FWCI
- 13.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Cell Physiology (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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Keywords
- Smad2, Smad3, myostatin, muscle mass, muscle atrophy, muscle hypertrophy, TGF-beta signaling, mTOR signaling, AKT pathway, insulin-like growth factor I, myostatin inhibitors, satellite cells
- MeSH terms
- Tripartite Motif Proteins, Receptor, Transforming Growth Factor-beta Type I, Receptor, Transforming Growth Factor-beta Type II, Age Factors, Animals, Carrier Proteins, Cell Differentiation, Cells, Cultured, Disease Models, Animal, Hypertrophy, Male, Mice, Transgenic, Muscle Denervation, Muscle Proteins, Muscular Atrophy, Mutation, Phosphorylation, Sciatic Nerve, Transfection, Signal Transduction, Transforming Growth Factor beta, Protein Serine-Threonine Kinases, Phosphotransferases (Alcohol Group Acceptor), Receptors, Transforming Growth Factor beta, Muscle, Skeletal, Muscle Development, RNA Interference, RNA, Small Interfering, Ubiquitin-Protein Ligases, Proto-Oncogene Proteins c-akt, Mice, Smad2 Protein, Smad3 Protein, Myostatin, TOR Serine-Threonine Kinases
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