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Conditional Activation of Akt in Adult Skeletal Muscle Induces Rapid Hypertrophy
Open accessAbstract
Skeletal muscle atrophy is a severe morbidity caused by a variety of conditions, including cachexia, cancer, AIDS, prolonged bedrest, and diabetes. One strategy in the treatment of atrophy is to induce the pathways normally leading to skeletal muscle hypertrophy. The pathways that are sufficient to induce hypertrophy in skeletal muscle have been the subject of some controversy. We describe here the use of a novel method to produce a transgenic mouse in which a constitutively active form of Akt can be inducibly expressed in adult skeletal muscle and thereby demonstrate that acute activation of Akt is sufficient to induce rapid and significant skeletal muscle hypertrophy in vivo, accompanied by activation of the downstream Akt/p70S6 kinase protein synthesis pathway. Upon induction of Akt in skeletal muscle, there was also a significant decrease in adipose tissue. These findings suggest that pharmacologic approaches directed toward activating Akt will be useful in inducing skeletal muscle hypertrophy and that an increase in lean muscle mass is sufficient to decrease fat storage.
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“In animal models, mTORC1 activation either by animal-specific resistance training, IGF-1 [36], or Akt1 expression [37] causes muscle hypertrophy.”
From Effects of Skeletal Muscle Hypertrophy on Fat Mass and Glucose Homeostasis in Humans and Animals: A Narrative Review with Systematic Literature Search (2025) · cites this paper as [37]
In the citing paper
“Activation of Akt in skeletal muscle leads to rapid muscle hypertrophy 37 accompanied by improved metabolism 38.”
From Akt-dependent anabolic activity of natural and synthetic brassinosteroids in rat skeletal muscle cells (2011) · cites this paper as [37]
Citations
Cites
The phosphatidylinositol 3-Kinase–AKT pathway in human cancer
Vivanco, I., & Sawyers, C. L. (2002) · Nature reviews. Cancer · doi:10.1038/nrc839 · Cited by 6,155
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
Cellular survival: a play in three Akts
Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216
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
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
Self-citationA Calcineurin-Dependent Transcriptional Pathway for Cardiac Hypertrophy
Molkentin, J. D., Lu, J., Antos, C. L., Markham, B. E., Richardson, J. A., Robbins, J. M., Grant, S. R., & Olson, E. N. (1998) · Cell · doi:10.1016/s0092-8674(00)81573-1 · Cited by 2,566
Rommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1009 · Cited by 1,583
Self-citationGrowth Hormone and the Insulin-Like Growth Factor System in Myogenesis*
Florini, J. R., Ewton, D. Z., & Coolican, S. A. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-5-481 · Cited by 1,148
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 · cited 1×
“When IGF-1 levels were enhanced by using a musclespecific promoter in transgenic mice, increased muscle size resulted (4, 13).”
BackgroundRegulation of Cre Recombinase Activity by Mutated Estrogen Receptor Ligand-Binding Domains
Feil, R., Wagner, J. D., METZGER, D., & Chambon, P. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7124 · Cited by 992
Research works printed but not linked: 4
- DeVol D. L., 1990, Am. J. Physiol., 259, E89
- Florini J. R., 1996, Endocrinol. Rev., 17, 481
- Pallafacchina G., 2002, Proc. Natl. Acad. Sci. USA, 25, 25
- Ralston E., 1996, Scanning Microsc. Suppl., 10, 249
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Rankinen, T., Zuberi, A., Chagnon, Y. C., Weisnagel, S. J., Argyropoulos, G., Walts, B., Pérusse, L., & Bouchard, C. (2006) · Obesity · doi:10.1038/oby.2006.71 · Cited by 1,119
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Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 866
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Schiaffino, S., & Mammucari, C. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-4 · Cited by 816
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Signaling Pathways in Skeletal Muscle Remodeling
Bassel‐Duby, R., & Olson, E. N. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142622 · Cited by 823
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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
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Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756
Seynnes, O. R., de Boer, M., & Narici, M. V. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00789.2006 · Cited by 660
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Self-citationLatres, E., Amini, A. R., Amini, A. A., Griffiths, J., Martin, F. J., Wei, Y., Lin, H. C., Yancopoulos, G. D., & Glass, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407517200 · Cited by 538
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Izumiya, Y., Bina, H. A., Ouchi, N., Akasaki, Y., Kharitonenkov, A., & Walsh, K. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.10.021 · Cited by 415
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Small, E. M., O'Rourke, J. R., Moresi, V., Sutherland, L. B., McAnally, J., Gerard, R. D., Richardson, J. A., & Olson, E. N. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000300107 · Cited by 417
Guo, T., Jou, W., Chanturiya, T., Portas, J., Gavrilova, O., & McPherron, A. C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004937 · Cited by 402
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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
Lloyd, A. C. (2013) · Cell · doi:10.1016/j.cell.2013.08.053 · Cited by 393
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Hood, D. A., Irrcher, I., Ljubicic, V., & Joseph, A.-M. (2006) · Journal of Experimental Biology · doi:10.1242/jeb.02182 · Cited by 370
Chakraborty, A., Koldobskiy, M. A., Bello, N. T., Maxwell, M. J., Potter, J. J., Juluri, K. R., Maag, D., Kim, S., Huang, A. S., Dailey, M. J., et al. (2010) · Cell · doi:10.1016/j.cell.2010.11.032 · Cited by 364
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
Self-citationKunkel, S. D., Suneja, M., Ebert, S. M., Bongers, K. S., Fox, D. K., Malmberg, S. E., Alipour, F., Shields, R. K., & Adams, C. M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.020 · Cited by 345
“Because ursolic acid increasedAkt activity (Figure 5), and because muscle-specific increases in Akt activity reduce adiposity as a secondary consequence of muscle hypertrophy (Izumiya et al., 2008; Lai et al., 2004), we hypothesized that ursolic acid-treated mice might contain less fat.”
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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
Ouchi, N., Oshima, Y., Ohashi, K., Higuchi, A., Ikegami, C., Izumiya, Y., & Walsh, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803440200 · Cited by 338
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Perrini, S., Laviola, L., Carreira, M. C., Cignarelli, A., Natalicchio, A., & Giorgino, F. (2010) · Journal of Endocrinology · doi:10.1677/joe-09-0431 · Cited by 317
Castets, P., Lin, S., Rion, N., Di Fulvio, S., Romanino, K., Guridi, M., Frank, S., Tintignac, L. A., Sinnreich, M., & Rüegg, M. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.015 · Cited by 302
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Self-citationHealth, A. A. B. C. S., Visser, M., Kritchevsky, S. B., Newman, A. B., Goodpaster, B. H., Tylavsky, F. A., Nevitt, M. C., & Harris, T. B. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn.82.3.531 · Cited by 249
Blaauw, B., Canato, M., Agatea, L., Toniolo, L., Mammucari, C., Masiero, E., Abraham, R., Sandri, M., Schiaffino, S., & Reggiani, C. (2009) · The FASEB Journal · doi:10.1096/fj.09-131870 · Cited by 244
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Self-citationKubica, N., Bolster, D. R., Farrell, P. A., Kimball, S. R., & Jefferson, L. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413732200 · Cited by 209
Hu, Z., Wang, H., Lee, I. H., Du, J., & Mitch, W. E. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38770 · Cited by 205
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Zamani, N., & Brown, C. (2010) · Endocrine Reviews · doi:10.1210/er.2010-0018 · Cited by 214
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Dubois, V., Laurent, M., Boonen, S., Vanderschueren, D., & Claessens, F. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0883-3 · Cited by 197
Kovacheva, E. L., Hikim, A. P. S., Shen, R., Sinha, I., & Sinha‐Hikim, I. (2009) · Endocrinology · doi:10.1210/en.2009-1177 · Cited by 201
Barreto, R., Waning, D. L., Gao, H., Liu, Y., Zimmers, T. A., & Bonetto, A. (2016) · Oncotarget · doi:10.18632/oncotarget.9779 · Cited by 205
Miyazaki, M., McCarthy, J. J., Fedele, M. J., & Esser, K. A. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.205658 · Cited by 204
Johns, N., Stephens, N. A., & Fearon, K. C. H. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.032 · Cited by 196
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
Philippou, Α., Halapas, A., Maridaki, M. D., & Koutsilieris, M. (2007) · PubMed · Cited by 189
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Uezumi, A., Ikemoto‐Uezumi, M., Zhou, H., Kurosawa, T., Yoshimoto, Y., Nakatani, M., Hitachi, K., Yamaguchi, H., Wakatsuki, S., Araki, T., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci139617 · Cited by 166
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Self-citationZhu, M. J., Han, B., Tong, J., Ma, C., Kimzey, J. M., Underwood, K. R., Xiao, Y., Hess, B. W., Ford, S. P., Nathanielsz, P. W., et al. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2007.149633 · Cited by 158
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Hodges, P. W., James, G., Blomster, L. V., Hall, L., Schmid, A. B., Shu, C. C., Little, C. B., & Melrose, J. (2015) · Spine · doi:10.1097/brs.0000000000000972 · Cited by 153
Léger, B., Vergani, L., Sorarú, G., Hespel, P., Derave, W., Gobelet, C., D'Ascenzio, C., Angelini, C. I., & Russell, A. P. (2006) · The FASEB Journal · doi:10.1096/fj.05-5249fje · Cited by 147
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Zanchi, N. E., & Lancha, A. H. (2007) · European Journal of Applied Physiology · doi:10.1007/s00421-007-0588-3 · Cited by 131
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Metadata
- Authors
- 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.
- Affiliations
- Regeneron (United States) (US)
- Corresponding author
- Glass, David J.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2004-11-01
- Volume
- 24
- Issue
- 21
- Pages
- 9295-9304
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC522257
- OpenAlex
- W2148625376
- Cited by
- 442
- References
- 25
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 16 · 2023: 17 · 2022: 21 · 2021: 17 · 2020: 17 · 2019: 21 · 2018: 18 · 2017: 10 · 2016: 21 · 2015: 23 · 2014: 25 · 2013: 34 · 2012: 22
- FWCI
- 7.34
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Procter and Gamble
- Regeneron Pharmaceuticals
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- Akt, skeletal muscle hypertrophy, skeletal muscle atrophy, p70 S6 kinase, protein synthesis, transgenic mice, adipose tissue, lean muscle mass, cachexia, Akt activation
- MeSH terms
- Adipose Tissue, Aging, Animals, Enzyme Activation, Female, Hypertrophy, Male, Mice, Inbred C57BL, Mice, Transgenic, Microscopy, Fluorescence, Proto-Oncogene Proteins, Tamoxifen, Protein Serine-Threonine Kinases, Muscle, Skeletal, Microscopy, Confocal, Proto-Oncogene Proteins c-akt, Mice
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