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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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Salamone, I. M., Quattrocelli, M., Barefield, D. Y., Page, P., Tahtah, I., Hadhazy, M., Tomar, G., & McNally, E. M. (2022) · Journal of Clinical Investigation · doi:10.1172/jci149828 · Cited by 35
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Cantuti‐Castelvetri, L., Maravilla, E. J., Marshall, M., Tamayo, T., D’Auria, L., Monge, J., Jeffries, J., Sural‐Fehr, T., Lopez‐Rosas, A., Li, G., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2431-14.2015 · Cited by 34
Allopurinol partially prevents disuse muscle atrophy in mice and humans
Ferrando, B., Gómez‐Cabrera, M. C., Salvador‐Pascual, A., Puchades, C., Derbré, F., Gratas‐Delamarche, A., Laparre, L., González, G. O., Cerda, M., Viosca, E., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-21552-1 · Cited by 33
Webster, J. M., Fenton, C. G., LANGEN, R. C. J., & Hardy, R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225768 · Cited by 36
Bawa, S., Piccirillo, R., & Geisbrecht, E. R. (2021) · Biomolecules · doi:10.3390/biom11030408 · Cited by 35
Tsai, C.-J., Wang, P.-C., Hsiung, T., Fan, Y.-H., Wu, J.-T., Kan, W., & Shiao, C. (2025) · Biomedicines · doi:10.3390/biomedicines13020352 · Cited by 39
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Fukatsu, Y., Noguchi, T., Hosooka, T., Ogura, T., Kotani, K., Abe, T., Shibakusa, T., Inoue, K., Sakai, M., Tobimatsu, K., et al. (2009) · Endocrinology · doi:10.1210/en.2008-1647 · Cited by 33
Recent advances in mitochondrial turnover during chronic muscle disuse
Tryon, L. D., Vainshtein, A., Memme, J. M., Crilly, M. J., & Hood, D. A. (2014) · Integrative Medicine Research · doi:10.1016/j.imr.2014.09.001 · Cited by 33
Gardan, D., Gondret, F., den Maagdenberg, K. V., Buys, N., SMET, S. D., & Louveau, I. (2006) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2006.10.001 · Cited by 33
Montano, M. A., Flanagan, J. N., Jiang, L., Sebastiani, P., Rarick, M., LeBrasseur, N. K., Morris, C. A., Jasuja, R., & Bhasin, S. (2007) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2006-2722 · Cited by 33
Zhang, Q., Duplany, A., Moncollin, V., Mouradian, S., Goillot, E., Mazelin, L., Gauthier, K., Streichenberger, N., Angleraux, C., Chen, J., et al. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12336 · Cited by 31
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Fukada, S., & Ito, N. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112907 · Cited by 32
Johns, N., Tan, B. H. L., Macmillan, M. T., Solheim, T. S., Ross, J. A. F., Baracos, V. E., Damaraju, S., & Fearon, K. C. H. (2014) · Journal of Genetics · doi:10.1007/s12041-014-0405-9 · Cited by 30
Akt activation induces hypertrophy without contractile phenotypic maturation in airway smooth muscle
Ma, L., Brown, M. L., Kogut, P., Serban, K. A., Li, X., McConville, J. F., Chen, B., Bentley, J. K., Hershenson, M. B., Dulin, N. O., et al. (2011) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00119.2009 · Cited by 31
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Köentgen, F., Süss, G., & Näf, D. (2009) · Methods in molecular biology · doi:10.1007/978-1-60761-058-8_4 · Cited by 31
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Glass, D. J. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.016 · Cited by 31
Self-citationKaragounis, L. G., Yaspelkis, B. B., Reeder, D. W., Lancaster, G. I., Hawley, J. A., & Coffey, V. G. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1427-5 · Cited by 31
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Lund-Ricard, Y., Cormier, P., Morales, J., & Boutet, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082718 · Cited by 30
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Mao, S., Luo, X., Yu, L., Chao-rong, H., Huang, F., & Su, C. (2019) · Current Neurovascular Research · doi:10.2174/1567202617666191223144715 · Cited by 29
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Fanzani, A., Colombo, F., Giuliani, R., Preti, A., & Marchesini, S. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05380.x · Cited by 29
Lauber, B. S., Hardegger, L. A., Alam, K. A., Lund, B. A., Dumele∞, O., Harder, M., Kuhn, B., Engh, R. A., & Diederich, F. (2015) · Chemistry - A European Journal · doi:10.1002/chem.201503552 · Cited by 28
Penniman, C. M., Beltran, P. A. S., Bhardwaj, G., Junck, T. L., Jena, J., Poro, K., Hirshman, M. F., Goodyear, L. J., & O'Neill, B. T. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.10.001 · Cited by 27
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Ruiz, A., Dror, E., Handschin, C., Furrer, R., Pérez‐Schindler, J., Bachmann, C., Treves, S., & Zorzato, F. (2018) · Scientific Reports · doi:10.1038/s41598-017-18844-3 · Cited by 26
Sakuma, K., Akiho, M., Nakashima, H., Nakao, R., Hirata, M., Inashima, S., Yamaguchi, A., & Yasuhara, M. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0371-5 · Cited by 31
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Scotton, C., Bovolenta, M., Schwartz, E., Falzarano, M. S., Martoni, E., Passarelli, C., Armaroli, A., Osman, H., Rodolico, C., Messina, S., et al. (2016) · Journal of Cell Science · doi:10.1242/jcs.175927 · Cited by 25
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Wackerhage, H., Miah, A., Harris, R. C., Montgomery, H., & Williams, A. G. (2009) · Journal of Sports Sciences · doi:10.1080/02640410903114364 · Cited by 24
Du, J., & Mitch, W. E. (2005) · Current Opinion in Nephrology & Hypertension · doi:10.1097/01.mnh.0000172726.75369.b2 · Cited by 25
Romeo-Guitart, D., Forés, J., Navarro, X., & Casas, C. (2017) · Scientific Reports · doi:10.1038/s41598-017-11086-3 · Cited by 27
Hénin, G., Lanthier, N., & Dahlqvist, G. (2022) · Acta gastro-enterologica belgica · doi:10.51821/85.4.10899 · Cited by 26
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Esposito, D., Rathinasabapathy, T., Poulev, A., Komarnytsky, S., & Raskin, I. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200028h · Cited by 22
Okuma, H., & Tsuchiya, K. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108699 · Cited by 23
Automated Methods for the Analysis of Skeletal Muscle Fiber Size and Metabolic Type
Kostrominova, T. Y., Reiner, D. S., Haas, R., Ingermanson, R. S., & McDonough, P. M. (2013) · International review of cytology · doi:10.1016/b978-0-12-407694-5.00007-9 · Cited by 22
Ucci, S., Renzini, A., Russi, V., Mangialardo, C., Cammarata, I., Cavioli, G., Santaguida, M. G., Virili, C., Centanni, M., Adamo, S., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225754 · Cited by 21
Ginsenoside Rg5 promotes muscle regeneration via p38MAPK and Akt/mTOR signaling
Kim, R., Kim, J. W., Choi, H., Oh, J., Kim, T. H., Go, G.-Y., Lee, S.-J., & Bae, G. (2023) · Journal of Ginseng Research · doi:10.1016/j.jgr.2023.06.004 · Cited by 21
Mukai, R., Horikawa, H., Lin, P.-Y., Tsukumo, N., Nikawa, T., Kawamura, T., Nemoto, H., & Terao, J. (2016) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00521.2015 · Cited by 21
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Choi, D. H., Yang, J., & Kim, Y. (2019) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2018.12.009 · Cited by 21
Stadhouders, L. E. M., Smith, J. A. B., Gabriel, B. M., Verbrugge, S. A. J., Hammersen, T. D., Kolijn, D., Vogel, I. S. P., Mohamed, A. D., de Wit, G. M. J., Offringa, C., et al. (2023) · Experimental Cell Research · doi:10.1016/j.yexcr.2023.113820 · Cited by 19
Gardner, S., Gross, S. M., David, L. L., Klimek, J. E., & Rotwein, P. S. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00184.2015 · Cited by 19
Kim, S.-Y., Lee, J., Kang, N., Kim, K., & Jeon, Y. (2021) · Marine Drugs · doi:10.3390/md19050266 · Cited by 19
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Harrison, B. C., & Leinwand, L. A. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.01.003 · Cited by 19
Nagendra, A. H., Najar, M. A., Bose, B., & Sudheer Shenoy, P. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.128654 · Cited by 18
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Rao, V. K., Das, D., & Taneja, R. (2022) · Cancers · doi:10.3390/cancers14174258 · Cited by 21
Cheng, K., Akasaki, Y., Lecommandeur, E., Lindsay, R. T., Murfitt, S. A., Walsh, K., & Griffin, J. L. (2014) · Journal of Proteome Research · doi:10.1021/pr500756u · Cited by 18
Natural constituents from food sources: potential therapeutic agents against muscle wasting
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Verhees, K. J. P., Pansters, N. A. M., Schols, A. M. W. J., & LANGEN, R. C. J. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319180011 · Cited by 19
Angelica Sinensis promotes myotube hypertrophy through the PI3K/Akt/mTOR pathway
Yeh, T., Hsu, C.-C., Yang, S., Hsu, M., & Liu, J. (2014) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-14-144 · Cited by 19
Havers, T., Held, S., Schönfelder, M., Geisler, S., & Wackerhage, H. (2025) · Sports Medicine · doi:10.1007/s40279-025-02263-w · Cited by 19
“In animal models, mTORC1 activation either by animal-specific resistance training, IGF-1 [36], or Akt1 expression [37] causes muscle hypertrophy.”
Zhang, R., Pan, Y., Zou, C.-X., An, Q., Cheng, J., Li, P.-J., Zheng, Z., Pan, Y., Feng, W., Yang, S., et al. (2022) · BMC Genomics · doi:10.1186/s12864-022-08518-4 · Cited by 17
Stretch-activated signaling is modulated by stretch magnitude and contraction
Dyke, J. M. V., Bain, J. L. W., & Riley, D. A. (2013) · Muscle & Nerve · doi:10.1002/mus.23880 · Cited by 17
Targeting cancer via ribosome biogenesis: the cachexia perspective
Figueiredo, V. C., & McCarthy, J. J. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03888-6 · Cited by 19
Sun, L., An, S., Zhang, Z., Zhou, Y., Yu, Y., Ma, Z., Fan, X., Tang, L., & Guo, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212112 · Cited by 17
Martins, K. J. B., Gehrig, S. M., Naim, T., Saenger, S., Baum, D. M., Metzger, F., & Lynch, G. S. (2013) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2013.03.002 · Cited by 17
Fanzani, A., Stoppani, E., Gualandi, L., Giuliani, R., Galbiati, F., Rossi, S., Fra, A., Preti, A., & Marchesini, S. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.09.055 · Cited by 17
Zhao, M., Danneskiold‐Samsøe, N. B., Uličná, L., Nguyen, Q., Coassolo, L., Lee, D. E., White, J. P., Jiang, Z., Cuthbert, N., Paramasivam, S., et al. (2022) · eLife · doi:10.7554/elife.80014 · Cited by 17
Wang, H., Wang, X., Li, M., Sun, H., Chen, Q., Yan, D., Dong, X., Pan, Y., & Lu, S. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1001352 · Cited by 16
Yang, J., Cao, R. Y., Li, Q. X., & Zhu, F. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1435-3_15 · Cited by 16
Freitas, P. S., Santana, T. S., Manoel, L. S., Serenza, F. D. S., & Riberto, M. (2019) · Journal of Spinal Cord Medicine · doi:10.1080/10790268.2019.1603489 · Cited by 16
Ciemiński, K., Flis, D. J., Dzik, K. P., Kaczor, J. J., Bialobrodzka, E. G., Hałoń, M., Wieckowski, M. R., Antosiewicz, J., & Ziółkowski, W. (2021) · Scientific Reports · doi:10.1038/s41598-021-00319-1 · Cited by 16
Akt-mediated phosphorylation controls the activity of the Y-box protein MSY3 in skeletal muscle
Angelis, L. D., Balasubramanian, S., & Berghella, L. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0043-9 · Cited by 14
Fanzani, A., Giuliani, R., Colombo, F., Rossi, S., Stoppani, E., Martinet, W., Preti, A., & Marchesini, S. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.111 · Cited by 18
Hoffmann, S. W., Schierbauer, J., Zimmermann, P., Voit, T., Grothoff, A., Wachsmuth, N. B., Rössler, A., Niedrist, T., Lackner, H. K., & Moser, O. (2024) · Biomolecules · doi:10.3390/biom14081029 · Cited by 19
Ancum, J. M. V., Tuttle, C. S. L., Koopman, R., Pijnappels, M. A. G. M., Meskers, C. G. M., Paul, S. K., Lim, W. K., Reijnierse, E. M., Lynch, G. S., & Maier, A. B. (2022) · European Geriatric Medicine · doi:10.1007/s41999-022-00625-5 · Cited by 15
Kubica, N., Jefferson, L. S., & Kimball, S. R. (2006) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(06)81007-x · Cited by 15
Chang, H.-C. (2010) · The Chinese Journal of Physiology · doi:10.4077/cjp.2010.amk080 · Cited by 15
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Nedergaard, A., Jespersen, J. G., Pingel, J., Christensen, B., Sroczynski, N., Langberg, H., Kjær, M., & Schjerling, P. (2012) · BMC Research Notes · doi:10.1186/1756-0500-5-166 · Cited by 17
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Mann, G., Riddell, M. C., & Adegoke, O. A. J. (2022) · Diabetology · doi:10.3390/diabetology3030032 · Cited by 16
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Norrby, M., Evertsson, K., Fjällström, A.-K., Svensson, A. C., & Tågerud, S. (2012) · Journal of Molecular Signaling · doi:10.1186/1750-2187-7-7 · Cited by 13
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Russell, S. T., Eley, H. L., Wyke, S. M., & Tisdale, M. J. (2008) · Biochemical Journal · doi:10.1042/bj20070688 · Cited by 13
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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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