A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification
Open accessAbstract
Nerve activity controls fiber size and fiber type in skeletal muscle, but the underlying molecular mechanisms remain largely unknown. We have previously shown that Ras–mitogen-activated protein kinase and calcineurin control fiber type but not fiber size in regenerating rat skeletal muscle. Here we report that constitutively active protein kinase B (PKB), also known as Akt, increases fiber size and prevents denervation atrophy in regenerating and adult rat muscles but does not affect fiber type profile. The coexistence of hypertrophic muscle fibers overexpressing activated PKB with normal-size untransfected fibers within the same muscle points to a cell-autonomous control of muscle growth by PKB. The physiological role of this pathway is confirmed by the finding that PKB kinase activity and phosphorylation status are significantly increased in innervated compared with denervated regenerating muscles in parallel with muscle growth. Muscle fiber hypertrophy induced by activated PKB and by a Ras double mutant (RasV12C40) that activates selectively the phosphoinositide 3-kinase–PKB pathway is completely blocked by rapamycin, showing that the mammalian target of rapamycin kinase is the major downstream effector of this pathway in the control of muscle fiber size. On the other hand, nerve activity-dependent growth of regenerating muscle is only partially inhibited by dominant negative PKB and rapamycin, suggesting that other nerve-dependent signaling pathways are involved in muscle growth. The present results support the notion that fiber size and fiber type are regulated by nerve activity through different mechanisms.
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Constitutively active AKT results in striking hypertrophy of transfected muscle fibers, with a similar effect using inducible muscle-specific transgenic models.
“Accordingly, constitutively active AKT results in striking hypertrophy of transfected muscle fibers9, with a similar effect being seen using inducible muscle-specific transgenic models10.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [9]
Rapamycin, a specific inhibitor of mTORC1, prevents muscle growth during anabolic conditions.
“Consistently, rapamycin, a specific inhibitor of mTORC1, prevents muscle growth during anabolic conditions9.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [9]
Cites
Calcium's Role in Mechanotransduction during Muscle Development
Damm, T. B., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,548 · see citing works
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 · see citing works
Bodine, 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
PKA Phosphorylation Dissociates FKBP12.6 from the Calcium Release Channel (Ryanodine Receptor)
Marx, S. O., Reiken, S. R., Hisamatsu, Y., Jayaraman, T., Burkhoff, D., Rosemblit, N., & Marks, A. R. (2000) · Cell · doi:10.1016/s0092-8674(00)80847-8 · Cited by 1,981 · see citing works
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 · see citing works
Regulation of translation initiation by FRAP/mTOR
Gingras, A.-C., Raught, B., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.887201 · Cited by 1,545 · see citing works
Ten years of protein kinase B signalling: a hard Akt to follow
Brazil, D. P., & Hemmings, B. A. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01958-2 · Cited by 1,177 · see citing works
Enhanced sensitivity of PTEN-deficient tumors to inhibition of FRAP/mTOR
Neshat, M., Mellinghoff, I., Tran, C., Stiles, B. L., Thomas, G., Petersen, R., Frost, P., Gibbons, J., Wu, H., & Sawyers, C. (2001) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.171076798 · Cited by 1,033 · see citing works
A calcineurin-dependent transcriptional pathway controls skeletal muscle fiber typePreprint
Chin, E. R., Olson, E. N., Richardson, J. A., Yang, Q., Humphries, C. G., Shelton, J. M., Wu, H., Zhu, W., Bassel‐Duby, R., & Williams, R. S. (1998) · Genes & Development · doi:10.1101/gad.12.16.2499 · Cited by 1,015 · see citing works
Three myosin heavy chain isoforms in type 2 skeletal muscle fibres
Schiaffino, S., Gorza, L., Sartore, S., Saggin, L., Ausoni, S., Vianello, M., Gundersen, K., & Lømo, T. (1989) · Journal of Muscle Research and Cell Motility · doi:10.1007/bf01739810 · Cited by 960 · see citing works
Self-citationElectrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms
Talmadge, R. J., & Roy, R. R. (1993) · Journal of Applied Physiology · doi:10.1152/jappl.1993.75.5.2337 · Cited by 804 · see citing works
Differentiation Stage-Specific Inhibition of the Raf-MEK-ERK Pathway by Akt
Rommel, C., Clarke, B. A., Zimmermann, S., Nuñez, L., Rossman, R., Reid, K., Moelling, K., Yancopoulos, G. D., & Glass, D. J. (1999) · Science · doi:10.1126/science.286.5445.1738 · Cited by 759 · see citing works
Coolican, S. A., Samuel, D. S., Ewton, D. Z., McWade, F. J., & Florini, J. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6653 · Cited by 646 · see citing works
Regulation of cellular growth by the Drosophila target of rapamycin dTORPreprint
Zhang, H., Stallock, J. P., Ng, J., Reinhard, C., & Neufeld, T. P. (2000) · Genes & Development · doi:10.1101/gad.835000 · Cited by 624 · see citing works
Andjelkovic, M., Jakubowicz, T., Cron, P., Ming, X., Han, J. W., & Hemmings, B. (1996) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.93.12.5699 · Cited by 525 · see citing works
Cardiac defects and altered ryanodine receptor function in mice lacking FKBP12
Shou, W., Aghdasi, B., Armstrong, D. L., Guo, Q., Bao, S., Charng, M., Mathews, L. S., Schneider, M. D., Hamilton, S. L., & Matzuk, M. M. (1998) · Nature · doi:10.1038/35146 · Cited by 431 · see citing works
Stimulation of Slow Skeletal Muscle Fiber Gene Expression by Calcineurin in Vivo
Naya, F. J., Mercer, B. M., Shelton, J. M., Richardson, J. A., Williams, R. S., & Olson, E. N. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.7.4545 · Cited by 420 · see citing works
Essential Role for Protein Kinase B (PKB) in Insulin-induced Glycogen Synthase Kinase 3 Inactivation
van Weeren, P. C., de Bruyn, K. M. T., de Vries-Smits, A. M. M., Lint, J. V., & Burgering, B. M. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13150 · Cited by 365 · see citing works
Cuenda, A., & Cohen, P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.4341 · Cited by 330 · see citing works
Delling, U., Turečková, J., Lim, H. W., Windt, L. J. D., Rotwein, P. S., & Molkentin, J. D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.17.6600-6611.2000 · Cited by 321 · see citing works
A role of the kinase mTOR in cellular transformation induced by the oncoproteins P3k and Akt
Aoki, M., Blazek, E., & Vogt, P. K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.136 · Cited by 306 · see citing works
Morisco, C., Zebrowski, D. C., Condorelli, G., Tsichlis, P., Vatner, S., & Sadoshima, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14466 · Cited by 295 · see citing works
Calcineurin Is Required for Skeletal Muscle Hypertrophy
Dunn, S. E., Burns, J. L., & Michel, R. N. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21908 · Cited by 274 · see citing works
Serrano, A. L., Murgia, M., Pallafacchina, G., Calabria, E., Coniglio, P., Lømo, T., & Schiaffino, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.231148598 · Cited by 265 · see citing works
Self-citationJiang, B., Aoki, M., Zheng, J. Z., Li, J., & Vogt, P. K. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2077 · Cited by 258 · see citing works
Stocker, H., & Hafen, E. (2000) · Current Opinion in Genetics and Development · doi:10.1016/s0959-437x(00)00123-4 · Cited by 257 · see citing works
Expression of myosin heavy chain isoforms in stimulated fast and slow rat muscles
Ausoni, S., Gorza, L., Schiaffino, S., Gundersen, K., & Lømo, T. (1990) · Journal of Neuroscience · doi:10.1523/jneurosci.10-01-00153.1990 · Cited by 238 · see citing works
Self-citationRas is involved in nerve-activity-dependent regulation of muscle genes
Murgia, M., Serrano, A. L., Calabria, E., Pallafacchina, G., Lømo, T., & Schiaffino, S. (2000) · Nature Cell Biology · doi:10.1038/35004013 · Cited by 218 · see citing works
Self-citationTroponin I Switching in the Developing Heart
Saggin, L., Gorza, L., Ausoni, S., & Schiaffino, S. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71621-9 · Cited by 206 · see citing works
Self-citationGene Transfer in Regenerating Muscle
Vitadello, M., Schiaffino, M. V., Picard, A., et al. (1994) · Human Gene Therapy · doi:10.1089/hum.1994.5.1-11 · Cited by 173 · see citing works
The calcineurin-NFAT pathway and muscle fiber-type gene expression
Swoap, S. J., Hunter, R. B., Stevenson, E. J., et al. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.279.4.c915 · Cited by 144 · see citing works
An essential role of phosphatidylinositol 3-kinase in myogenic differentiation
Jiang, B., Zheng, J. Z., & Vogt, P. K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.24.14179 · Cited by 125 · see citing works
Matching of Calcineurin Activity to Upstream Effectors Is Critical for Skeletal Muscle Fiber Growth
Dunn, S. E., Chin, E. R., & Michel, R. N. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.3.663 · Cited by 113 · see citing works
Protein Kinase B β/Akt2 Plays a Specific Role in Muscle Differentiation
Vandromme, M., Rochat, A., Meier, R., Carnac, G., Besser, D., Hemmings, B. A., Fernandez, A., & Lamb, N. J. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005587200 · Cited by 110 · see citing works
Calcineurin differentially regulates maintenance and growth of phenotypically distinct muscles
Mitchell, P. O., Mills, S. T., & Pavlath, G. K. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00483.2001 · Cited by 101 · see citing works
Ramocki, M. B., Johnson, S., White, M. A., et al. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.7.3547 · Cited by 81 · see citing works
Maintenance of muscle mass is not dependent on the calcineurin-NFAT pathway
Dupont‐Versteegden, E. E., Knox, M., Gurley, C. M., Houlé, J. D., & Peterson, C. A. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00424.2001 · Cited by 65 · see citing works
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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-citationStitt, 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-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-citationSkeletal muscle hypertrophy and atrophy signaling pathways
Glass, D. J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.018 · Cited by 1,106 · 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
Regulation 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
“Note the striking hypertrophy of labeled myofibers compared with untransfected neighbouring fibers. Modified from [ 69 ].”
BackgroundInfluentialSelf-citationSignalling pathways that mediate skeletal muscle hypertrophy and atrophy
Glass, D. J. (2003) · Nature Cell Biology · doi:10.1038/ncb0203-87 · Cited by 694 · see citing works
Bentzinger, C. F., Romanino, K., Cloëtta, D., Lin, S., Mascarenhas, J. B., Oliveri, F., Xia, J., Casanova, E., Costa, C. F., Brink, M., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.10.002 · Cited by 640 · see citing works
Smad2 and 3 transcription factors control muscle mass in adulthood
Sartori, R., Milan, G., Patron, M., Mammucari, C., Blaauw, B., Abraham, R., & Sandri, M. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00104.2009 · Cited by 517 · 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
Atherton, P. J., Babraj, J. A., Smith, K., Singh, J., Rennie, M. J., & Wackerhage, H. (2005) · The FASEB Journal · doi:10.1096/fj.04-2179fje · Cited by 475 · see citing works
Sandri, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.056 · Cited by 451 · see citing works
Dreyer, H. C., Drummond, M. J., Pennings, B., Fujita, S., Glynn, E. L., Chinkes, D. L., Dhanani, S., Volpi, E., & Rasmussen, B. B. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00582.2007 · Cited by 447 · 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
New fundamental resistance exercise determinants of molecular and cellular muscle adaptations
Toigo, M., & Boutellier, U. (2006) · European Journal of Applied Physiology · doi:10.1007/s00421-006-0238-1 · Cited by 437 · see citing works
Role of β-Adrenoceptor Signaling in Skeletal Muscle: Implications for Muscle Wasting and Disease
Lynch, G. S., & Ryall, J. G. (2008) · Physiological Reviews · doi:10.1152/physrev.00028.2007 · Cited by 410 · 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
Control of the size of the human muscle mass
Rennie, M. J., Wackerhage, H., Spangenburg, E. E., & Booth, F. W. (2004) · Annual Review of Physiology · doi:10.1146/annurev.physiol.66.052102.134444 · Cited by 399 · see citing works
Myostatin 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
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
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-citationAutophagy 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
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 · see citing works
Self-citationThe Role of Water Homeostasis in Muscle Function and Frailty: A Review
Lorenzo, I., Serra-Prat, M., & Yébenes, J. C. (2019) · Nutrients · doi:10.3390/nu11081857 · Cited by 239 · 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
Abadi, A., Glover, E. I., Isfort, R. J., Raha, S., Safdar, A., Yasuda, N., Kaczor, J. J., Melov, S., Hubbard, A., Qu, X., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006518 · Cited by 189 · see citing works
mTOR pathway as a target in tissue hypertrophy
Lee, C.-H., Inoki, K., & Guan, K.-L. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105359 · Cited by 179 · see citing works
Inflammation and age-associated skeletal muscle deterioration (sarcopaenia)
Wang, J., Leung, K.-S., Chow, S. K.-H., & Cheung, W.-H. (2017) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2017.05.006 · Cited by 173 · see citing works
mTOR Signaling and the Molecular Adaptation to Resistance Exercise
BODINE, S. C. (2006) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000233797.24035.35 · Cited by 171 · see citing works
Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle
Hornberger, T. A. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.05.007 · Cited by 170 · see citing works
Cuthbertson, D. J., Babraj, J., Smith, K., Wilkes, E., Fedele, M. J., Esser, K., & Rennie, M. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00415.2005 · Cited by 166 · see citing works
Differential response of skeletal muscles to mTORC1 signaling during atrophy and hypertrophy
Bentzinger, C. F., Lin, S., Romanino, K., Castets, P., Guridi, M., Summermatter, S., Handschin, C., Tintignac, L. A., Hall, M. N., & Rüegg, M. A. (2013) · Skeletal Muscle · doi:10.1186/2044-5040-3-6 · Cited by 153 · see citing works
ERK2 is required for efficient terminal differentiation of skeletal myoblasts
Li, J., & Johnson, S. E. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.051 · 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
Important role for AMPKαl in limiting skeletal muscle cell hypertrophy
Mounier, R., Lantier, L., Leclerc, J., Sotiropoulos, A., Pende, M., Daegelen, D., Sakamoto, K., Foretz, M., & Viollet, B. (2009) · The FASEB Journal · doi:10.1096/fj.08-119057 · Cited by 133 · see citing works
The Transcription Factor ATF4 Promotes Skeletal Myofiber Atrophy during Fasting
Ebert, S. M., Monteys, A. M., Fox, D. K., Bongers, K. S., Shields, B. E., Malmberg, S. E., Davidson, B. L., Suneja, M., & Adams, C. M. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0345 · Cited by 130 · see citing works
Selective control of skeletal muscle differentiation by Akt1
Wilson, E. M., & Rotwein, P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c600315200 · Cited by 118 · see citing works
Mieulet, V., Roceri, M., Espeillac, C., Sotiropoulos, A., Ohanna, M., Oorschot, V., Klumperman, J., Sandri, M., & Pende, M. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00499.2006 · Cited by 99 · see citing works
Hamilton, D. L., Philp, A., MacKenzie, M. G., & Baar, K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011624 · Cited by 71 · see citing works
Lambertucci, A. C., Lambertucci, R. H., Hirabara, S. M., Curi, R., Moriscot, A. S., Alba-Loureiro, T. C., Guimarães-Ferreira, L., Levada-Pires, A. C., Vasconcelos, D. A. A., Sellitti, D. F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050390 · Cited by 67 · see citing works
Proteasome inhibition improves the muscle of laminin α2 chain-deficient mice.
Carmignac, V., Quéré, R., & Durbeej, M. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddq499 · Cited by 58 · see citing works
Hand, B. D., Kostek, M. C., Ferrell, R. E., Delmonico, M. J., Douglass, L. W., Roth, S. M., Hagberg, J. M., & Hurley, B. F. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00420.2007 · Cited by 53 · see citing works
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 · see citing works
Borg, M. L., Massart, J., De Castro Barbosa, T., Archilla‐Ortega, A., Smith, J. A. B., Lanner, J. T., Alsina‐Fernandez, J., Yaden, B., Culver, A. E., Karlsson, H. K. R., et al. (2021) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12746 · Cited by 23 · see citing works
- Authors
- Pallafacchina, G., Calabria, E., Serrano, A. L., Kalhovde, J. M., & Schiaffino, S.
- Affiliations
- University of Padua (IT)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2002-06-25
- Volume
- 99
- Issue
- 14
- Pages
- 9213-9218
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC123120
- OpenAlex
- W2168107233
- Cited by
- 402
- References
- 38
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 11 · 2023: 8 · 2022: 10 · 2021: 14 · 2020: 12 · 2019: 16 · 2018: 17 · 2017: 12 · 2016: 13 · 2015: 17 · 2014: 16 · 2013: 22 · 2012: 23
- FWCI
- 6.68
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (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 › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- Akt, skeletal muscle growth, muscle fiber size, nerve activity, muscle regeneration, denervation atrophy, rapamycin, mTOR kinase, phosphatidylinositol 3-kinase, calcineurin, cell-autonomous signaling
- MeSH terms
- Animals, Electric Stimulation, Hypertrophy, Male, Muscle Denervation, Muscular Atrophy, Mutation, Phosphorylation, Protein Kinases, Proto-Oncogene Proteins, Regeneration, Signal Transduction, Rats, Wistar, Protein Serine-Threonine Kinases, Muscle, Skeletal, Muscle Fibers, Skeletal, Phosphatidylinositol 3-Kinases, Sirolimus, Proto-Oncogene Proteins c-akt, Rats, TOR Serine-Threonine Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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