Cited by 442Muscle Physiology and DisordersMuscle metabolism and nutritionMetabolism, Diabetes, and Cancer

The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.

Conditional Activation of Akt in Adult Skeletal Muscle Induces Rapid Hypertrophy

Open access

Lai, Ka-Man V., Gonzalez, Michael, Poueymirou, William T., Kline, William O., Na, Erqian, Zlotchenko, Elizabeth, Stitt, Trevor N., Economides, Aris N., Yancopoulos, George D., Glass, David J.·2004·Molecular and Cellular Biology

DOI 10.1128/mcb.24.21.9295-9304.2004PMC PMC522257

Open this paper in CoChat — free account

Abstract

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.

Integrity signals

Registry

Crossref · 10.1128/mcb.24.21.9295-9304.2004

Cites

25 of 25 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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-citation
Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
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
Self-citation
A 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
Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways
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-citation
Growth 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
Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle
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).”
Background
Regulation 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

Show all 25 references

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

Sorted by citations

Items 101–200 of 439

Molecular Mechanisms and Treatment Options for Muscle Wasting Diseases
Rüegg, M. A., & Glass, D. J. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010510-100537 · Cited by 114
Self-citation
Expression of IGF-1 isoforms after exercise-induced muscle damage in humans: characterization of the MGF E peptide actions in vitro.
Philippou, Α., Papageorgiou, E., Bogdanis, G. C., Halapas, A., Sourla, A., Maridaki, M. D., Pissimissis, N., & Koutsilieris, M. (2009) · PubMed · Cited by 110
Autophagy as a Potential Target for Sarcopenia: AUTOPHAGY REGULATION IN SARCOPENIA
Fan, J., Kou, X., Jia, S., Yang, X., Yang, Y., & Chen, N. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25260 · Cited by 101
Role of microRNAs in skeletal muscle hypertrophy
Hitachi, K., & Tsuchida, K. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2013.00408 · Cited by 106
TAK-1/p38/nNFκB signaling inhibits myoblast differentiation by increasing levels of Activin A
Trendelenburg, A. U., Meyer, A. S., Jacobi, C., Feige, J. N., & Glass, D. J. (2012) · Skeletal Muscle · doi:10.1186/2044-5040-2-3 · Cited by 106
Self-citation
Of bears, frogs, meat, mice and men: complexity of factors affecting skeletal muscle mass and fat
Shavlakadze, T., & Grounds, M. D. (2006) · BioEssays · doi:10.1002/bies.20479 · Cited by 104
Isometric resistance exercise fails to counteract skeletal muscle atrophy processes during the initial stages of unloading
Haddad, F., Adams, G., Bodell, P. W., & Baldwin, K. M. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01203.2005 · Cited by 109
Resveratrol promotes myogenesis and hypertrophy in murine myoblasts
Montesano, A., Luzi, L., Senesi, P., Mazzocchi, N., & Terruzzi, I. (2013) · Journal of Translational Medicine · doi:10.1186/1479-5876-11-310 · Cited by 104
Molecular events and signalling pathways involved in skeletal muscle disuse‐induced atrophy and the impact of countermeasures
Chopard, A., Hillock, S., & Jasmin, B. J. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00864.x · Cited by 106
AMP‐activated protein kinase enhances the expression of muscle‐specific ubiquitin ligases despite its activation of IGF‐1/Akt signaling in C2C12 myotubes
Tong, J. F., Yan, X., Zhu, M. J., & Du, ‬. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22272 · Cited by 100
Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin‐deficient mice
Lipina, C., Kendall, H., McPherron, A. C., Taylor, P. M., & Hundal, H. S. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.039 · Cited by 98
PI3 kinase directly phosphorylates Akt1/2 at Ser473/474 in the insulin signal transduction pathway
Tsuchiya, A., Kanno, T., & Nishizaki, T. (2013) · Journal of Endocrinology · doi:10.1530/joe-13-0172 · Cited by 95
Skeletal muscle cytokines: regulation by pathogen-associated molecules and catabolic hormones
Frost, R. A., & Lang, C. H. (2005) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000165003.16578.2d · Cited by 94
Molecular signaling pathways regulating muscle proteolysis during atrophy
Franch, H. A., & Price, S. R. (2005) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000165005.01331.45 · Cited by 94
Poor maternal nutrition inhibits muscle development in ovine offspring
Reed, S. A., Raja, J., Hoffman, M. L., Zinn, S. A., & Govoni, K. E. (2014) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/2049-1891-5-43 · Cited by 99
β-Hydroxy-β-methylbutyrate (HMβ) supplementation stimulates skeletal muscle hypertrophy in rats via the mTOR pathway
Pimentel, G. D., Neto, J. C. R., Lira, F. S., Zanchi, N. E., Ropelle, E. R., Oyama, L. M., do Nascimento, C. M. O., de Mello, M. T., Tufik, S., & dos Santos, R. V. T. (2011) · Nutrition & Metabolism · doi:10.1186/1743-7075-8-11 · Cited by 91
TACE release of TNF-α mediates mechanotransduction-induced activation of p38 MAPK and myogenesis
Zhan, M., Jin, B., Chen, S., Reecy, J. M., & Li, Y.-P. (2007) · Journal of Cell Science · doi:10.1242/jcs.03372 · Cited by 90
The methyltransferase SMYD3 mediates the recruitment of transcriptional cofactors at the myostatin and c-Met genes and regulates skeletal muscle atrophyPreprint
Proserpio, V., Fittipaldi, R., Ryall, J. G., Sartorelli, V., & Caretti, G. (2013) · Genes & Development · doi:10.1101/gad.217240.113 · Cited by 99
Betaine supplement enhances skeletal muscle differentiation in murine myoblasts via IGF-1 signaling activation
Senesi, P., Luzi, L., Montesano, A., Mazzocchi, N., & Terruzzi, I. (2013) · Journal of Translational Medicine · doi:10.1186/1479-5876-11-174 · Cited by 90
Akt activation prevents the force drop induced by eccentric contractions in dystrophin-deficient skeletal muscle
Blaauw, B., Mammucari, C., Toniolo, L., Agatea, L., Abraham, R., Sandri, M., Reggiani, C., & Schiaffino, S. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn264 · Cited by 84
A Strategy for Discovery of Endocrine Interactions with Application to Whole-Body Metabolism
Seldin, M. M., Koplev, S., Rajbhandari, P., Vergnes, L., Rosenberg, G. M., Meng, Y., Pan, C., Phuong, T. M. N., Gharakhanian, R., Che, N., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.015 · Cited by 84
Signalling and the control of skeletal muscle size
Otto, A., & Patel, K. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.04.009 · Cited by 84
Saikosaponin A and D attenuate skeletal muscle atrophy in chronic kidney disease by reducing oxidative stress through activation of PI3K/AKT/Nrf2 pathway
Huang, M., Yan, Y., Deng, Z., Zhou, L., She, M., Yang, Y., Zhang, M., & Wang, D. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154766 · Cited by 83
Myofiber degeneration/regeneration is induced in the cachecticApcMin/+mouse
Mehl, K. A., Davis, J. M., Berger, F. G., & Carson, J. A. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00778.2005 · Cited by 84
Conditional Loss of Pten in Myogenic Progenitors Leads to Postnatal Skeletal Muscle Hypertrophy but Age-Dependent Exhaustion of Satellite Cells
Yue, F., Bi, P., Wang, C., Li, J., Liu, X., & Kuang, S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.11.002 · Cited by 81
Activity of the Akt-dependent anabolic and catabolic pathways in muscle and liver samples in cancer-related cachexia
Schmitt, T. L., Martignoni, M. E., Bachmann, J., Fechtner, K., Friess, H., Kinscherf, R., & Hildebrandt, W. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0177-2 · Cited by 85
A New Role for Sterol Regulatory Element Binding Protein 1 Transcription Factors in the Regulation of Muscle Mass and Muscle Cell Differentiation
Lecomte, V., Meugnier, E., Euthine, V., Durand, C., Freyssenet, D. G., Némoz, G., Rome, S., Vidal, H., & Lefai, É. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00690-09 · Cited by 84
AKT controls protein synthesis and oxidative metabolism via combined mTORC1 and FOXO1 signalling to govern muscle physiology
Jaiswal, N., Gavin, M., Loro, E., Sostre‐Colón, J., Roberson, P. A., Uehara, K., Rivera‐Fuentes, N., Neinast, M., Arany, Z., Kimball, S. R., et al. (2022) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12846 · Cited by 79
Non-Coding RNA Regulates the Myogenesis of Skeletal Muscle Satellite Cells, Injury Repair and Diseases
Zhao, Y., Chen, M., Lian, D., Li, Y., Li, Y., Wang, J., Deng, S., Yu, K., & Lian, Z. (2019) · Cells · doi:10.3390/cells8090988 · Cited by 78
Role of Akt/GSK-3β/β-Catenin Transduction Pathway in the Muscle Anti-Atrophy Action of Insulin-Like Growth Factor-I in Glucocorticoid-Treated Rats
Schakman, O., Kalista, S., Bertrand, L., Lause, P., Verniers, J., Ketelslegers, J. M., & Thissen, J. (2008) · Endocrinology · doi:10.1210/en.2008-0439 · Cited by 83
Steroidal Androgens and Nonsteroidal, Tissue-Selective Androgen Receptor Modulator, S-22, Regulate Androgen Receptor Function through Distinct Genomic and Nongenomic Signaling Pathways
Narayanan, R., Coss, C. C., Yepuru, M., Kearbey, J. D., Miller, D. D., & Dalton, J. T. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0160 · Cited by 78
17β-Estradiol regulates the first steps of skeletal muscle cell differentiation via ER-α-mediated signals
Galluzzo, P., Rastelli, C., Bulzomi, P., Acconcia, F., Pallottini, V., & Marino, M. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00188.2009 · Cited by 79
Notch and Wnt Signaling, Physiological Stimuli and Postnatal Myogenesis
Tsivitse, S. K. (2010) · International Journal of Biological Sciences · doi:10.7150/ijbs.6.268 · Cited by 72
A Limited Role for PI(3,4,5)P3 Regulation in Controlling Skeletal Muscle Mass in Response to Resistance Exercise
Hamilton, D. L., Philp, A., MacKenzie, M. G., & Baar, K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011624 · Cited by 71
Phenotypic Improvement of Dystrophic Muscles by rAAV/Microdystrophin Vectors Is Augmented by Igf1 Codelivery
Abmayr, S., Gregorevic, P., Allen, J. M., & Chamberlain, J. S. (2005) · Molecular Therapy · doi:10.1016/j.ymthe.2005.04.001 · Cited by 73
Gene therapy for follistatin mitigates systemic metabolic inflammation and post-traumatic arthritis in high-fat diet–induced obesity
Tang, R., Harasymowicz, N. S., Wu, C., Collins, K. H., Choi, Y., Oswald, S. J., & Guilak, F. (2020) · Science Advances · doi:10.1126/sciadv.aaz7492 · Cited by 71
Distinct actions of Akt1 and Akt2 in skeletal muscle differentiation
Rotwein, P. S., & Wilson, E. M. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21692 · Cited by 74
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
The Intriguing Regulators of Muscle Mass in Sarcopenia and Muscular Dystrophy
Sakuma, K., Aoi, W., & Yamaguchi, A. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00230 · Cited by 70
Effects of a Novel Selective Androgen Receptor Modulator on Dexamethasone-Induced and Hypogonadism-Induced Muscle Atrophy
Jones, A. J., Hwang, D., Narayanan, R., Miller, D. D., & Dalton, J. T. (2010) · Endocrinology · doi:10.1210/en.2010-0150 · Cited by 67
Blockade of Metallothioneins 1 and 2 Increases Skeletal Muscle Mass and Strength
Summermatter, S., Bouzan, A., Pierrel, E., Melly, S., Stauffer, D., Gutzwiller, S., Nolin, E., Dornelas, C., Fryer, C., Leighton-Davies, J., et al. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00305-16 · Cited by 66
Self-citation
Eukaryotic initiation factor 2B epsilon induces cap‐dependent translation and skeletal muscle hypertrophy
Mayhew, D. L., Hornberger, T. A., Lincoln, H. C., & Bamman, M. M. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2010.202432 · Cited by 64
More than a bystander: the contributions of intrinsic skeletal muscle defects in motor neuron diseases
Boyer, J. G., Ferrier, A., & Kothary, R. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00356 · Cited by 69
Resistance to body fat gain in ‘double-muscled’ mice fed a high-fat diet
Hamrick, M. W., Pennington, C., Webb, C. N., & Isales, C. M. (2006) · International Journal of Obesity · doi:10.1038/sj.ijo.0803200 · Cited by 66
Musclin, A Myokine Induced by Aerobic Exercise, Retards Muscle Atrophy During Cancer Cachexia in Mice
Re Cecconi, A. D., Forti, M., Chiappa, M., Zhu, Z., Zingman, L. V., Cervo, L., Beltrame, L., Marchini, S., & Piccirillo, R. (2019) · Cancers · doi:10.3390/cancers11101541 · Cited by 66
Des-acyl ghrelin exhibits pro-anabolic and anti-catabolic effects on C2C12 myotubes exposed to cytokines and reduces burn-induced muscle proteolysis in rats
Sheriff, S., Kadeer, N., Joshi, R., Friend, L. A., James, J. H., & Balasubramaniam, A. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.12.021 · Cited by 64
Cellular and molecular features of neurogenic skeletal muscle atrophy
Ehmsen, J. T., & Höke, A. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113379 · Cited by 63
Effect of DLK1 and RTL1 but Not MEG3 or MEG8 on Muscle Gene Expression in Callipyge Lambs
Waddell, J. N., Olbricht, G. R., Taxis, T. M., White, J. D., Vuocolo, T., Craig, B. Α., Tellam, R. L., Neary, M. K., Cockett, N., & Bidwell, C. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007399 · Cited by 64
Constant heat stress reduces skeletal muscle protein deposition in broilers
Zuo, J., Xu, M., Abdullahi, A. Y., Ma, L., Zhang, Z., & Feng, D. (2014) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.6749 · Cited by 61
Akt/protein kinase B in skeletal muscle physiology and pathology
Wu, M., Falasca, M., & Blough, E. R. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22353 · Cited by 60
The Type 1 Insulin-Like Growth Factor Receptor (IGF-IR) Pathway Is Mandatory for the Follistatin-Induced Skeletal Muscle Hypertrophy
Kalista, S., Schakman, O., Gilson, H., Lause, P., Demeulder, B., Bertrand, L., Pende, M., & Thissen, J. (2011) · Endocrinology · doi:10.1210/en.2011-1687 · Cited by 60
Akt-mediated Liver Growth Promotes Induction of Cyclin E through a Novel Translational Mechanism and a p21-mediated Cell Cycle Arrest
Mullany, L. K., Nelsen, C. J., Hanse, E. A., Goggin, M. M., Anttila, C. K., Peterson, M., Bitterman, P. B., Raghavan, A., Crary, G. S., & Albrecht, J. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702110200 · Cited by 59
Molecular mechanism of sphingosine-1-phosphate action in Duchenne muscular dystrophy
Nguyen-Tran, D.-H., Hait, N. C., Sperber, H., Qi, J., Fischer, K., Ieronimakis, N., Pantoja, M., Hays, A., Allegood, J., Reyes, M., et al. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.013631 · Cited by 58
“Because many signaling molecules are anchored to the sarcolemma via dystrophin (Lai et al., 2004; Li et al., 2010), the lack of dystrophin gene expression in individuals with DMD significantly alters the DGC and results in mislocalization of key signaling components (Brenman et al.”
Background
Defining Akt actions in muscle differentiation
Gardner, S., Anguiano, M., & Rotwein, P. S. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00259.2012 · Cited by 58
Increased sphingosine-1-phosphate improves muscle regeneration in acutely injured mdx mice
Ieronimakis, N. M., Pantoja, M., Hays, A. L., Dosey, T. L., Qi, J., Fischer, K. A., Hoofnagle, A. N., Sadı́lek, M., Chamberlain, J. S., Ruohola‐Baker, H., et al. (2013) · Skeletal Muscle · doi:10.1186/2044-5040-3-20 · Cited by 57
The SH2 domain containing inositol polyphosphate 5-phosphatase-2: SHIP2
Dyson, J. M., Kong, A. M., Wiradjaja, F., Astle, M. V., Gurung, R., & Mitchell, C. A. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.05.003 · Cited by 56
Differential effects of Hsp90 inhibition on protein kinases regulating signal transduction pathways required for myoblast differentiation
Yun, B.-G., & Matts, R. L. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.03.003 · Cited by 56
Genes Whose Gain or Loss-Of-Function Increases Skeletal Muscle Mass in Mice: A Systematic Literature Review
Verbrugge, S. A. J., Schönfelder, M., Becker, L., Yaghoob Nezhad, F., Hrabě de Angelis, M., & Wackerhage, H. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00553 · Cited by 56
A novel PKB/Akt inhibitor, MK-2206, effectively inhibits insulin-stimulated glucose metabolism and protein synthesis in isolated rat skeletal muscle
Lai, Y., Liu, Y., Jacobs, R., & Rider, M. H. (2012) · Biochemical Journal · doi:10.1042/bj20120772 · Cited by 57
lncRNA Chronos is an aging-induced inhibitor of muscle hypertrophy
Neppl, R. L., Wu, C., & Walsh, K. X. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201612100 · Cited by 54
AKT as a therapeutic target in multiple myeloma
Keane, N. A., Glavey, S. V., Krawczyk, J., & O'Dwyer, M. E. (2014) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2014.924507 · Cited by 55
Akt1–Mediated Skeletal Muscle Growth Attenuates Cardiac Dysfunction and Remodeling After Experimental Myocardial Infarction
Araki, S., Izumiya, Y., Hanatani, S., Rokutanda, T., Usuku, H., Akasaki, Y., Takeo, T., Nakagata, N., Walsh, K. X., & Ogawa, H. (2011) · Circulation Heart Failure · doi:10.1161/circheartfailure.111.964783 · Cited by 53
Brown fat organogenesis and maintenance requires AKT1 and AKT2
Sánchez-Gurmaches, J., Calejman, C. M., Jung, S. M., Li, H., & Guertin, D. A. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.02.004 · Cited by 55
Effect of nandrolone decanoate administration on recovery from bupivacaine-induced muscle injury.
White, J., Baltgalvis, K. A., Sato, S., Wilson, L., & Carson, J. A. (2009) · Journal of applied physiology · doi:10.1152/japplphysiol.00668.2009 · Cited by 62
Insulin-Like Growth Factor (IGF) Binding Protein-5 Blocks Skeletal Muscle Differentiation by Inhibiting IGF Actions
Mukherjee, A., Wilson, E. M., & Rotwein, P. S. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0336 · Cited by 53
Hsp90 functions to balance the phosphorylation state of Akt during C2C12 myoblast differentiation
Yun, B.-G., & Matts, R. L. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.006 · Cited by 52
PTEN Contributes to Profound PI3K/Akt Signaling Pathway Deregulation in Dystrophin-Deficient Dog Muscle
Feron, M., Guével, L., Rouger, K., Dubreil, L., Arnaud, M., Ledevin, M., Megeney, L. A., Chérel, Y., & Sakanyan, V. A. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080460 · Cited by 52
How nutrition and exercise maintain the human musculoskeletal mass
Wackerhage, H., & Rennie, M. J. (2006) · Journal of Anatomy · doi:10.1111/j.1469-7580.2006.00544.x · Cited by 52
Cancer cachexia: lessons from Drosophila
Liu, Y., Saavedra, P. H. V., & Perrimon, N. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049298 · Cited by 44
Grb10 regulates the development of fiber number in skeletal muscle
Holt, L. J., Turner, N. A., Mokbel, N., Trefely, S., Kanzleiter, T., Kaplan, W. H., Ormandy, C. J., Daly, R. J., & Cooney, G. J. (2012) · The FASEB Journal · doi:10.1096/fj.11-199349 · Cited by 49
Dystrophin glycoprotein complex‐associated Gβγ subunits activate phosphatidylinositol‐3‐kinase/Akt signaling in skeletal muscle in a laminin‐dependent manner
Xiong, Y., Zhou, Y., & Jarrett, H. W. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21684 · Cited by 47
Molecular and biochemical regulation of skeletal muscle metabolism
Zumbaugh, M. D., Johnson, S., Shi, T. H., & Gerrard, D. E. (2022) · Journal of Animal Science · doi:10.1093/jas/skac035 · Cited by 56
Does a Hypertrophying Muscle Fibre Reprogramme its Metabolism Similar to a Cancer Cell?
Wackerhage, H., Vechetti, I. J., Baumert, P., Gehlert, S., Becker, L., Jaspers, R. T., & de Angelis, M. H. (2022) · Sports Medicine · doi:10.1007/s40279-022-01676-1 · Cited by 46
Dual roles of mTORC1-dependent activation of the ubiquitin-proteasome system in muscle proteostasis
Kaiser, M. S., Milan, G., Ham, D. J., Lin, S., Oliveri, F., Chojnowska, K., Tintignac, L. A. J., Mittal, N., Zimmerli, C. E., Glass, D. J., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-04097-y · Cited by 51
Self-citation
Cellular and molecular pathways controlling muscle size in response to exercise
Attwaters, M., & Hughes, S. M. (2021) · FEBS Journal · doi:10.1111/febs.15820 · Cited by 47
The TWEAK-Fn14 System: Breaking the Silence of Cytokine-Induced Skeletal Muscle Wasting
Bhatnagar, S., & Kumar, A. (2011) · Current Molecular Medicine · doi:10.2174/156652412798376107 · Cited by 43
TGF-β Inhibits Muscle Differentiation by Blocking Autocrine Signaling Pathways Initiated by IGF-II
Gardner, S., Alzhanov, D., Knollman, P. E., Kuninger, D., & Rotwein, P. S. (2010) · Molecular Endocrinology · doi:10.1210/me.2010-0292 · Cited by 47
Autophagy is Impaired in the Tibialis Anterior of Dystrophin Null Mice
Spitali, P., Grumati, P., Hiller, M., Chrisam, M., Aartsma-Rus, A. M., & Bonaldo, P. (2013) · PLoS Currents · doi:10.1371/currents.md.e1226cefa851a2f079bbc406c0a21e80 · Cited by 47
Safety, tolerability, and preliminary efficacy of an IGF-1 mimetic in patients with spinal and bulbar muscular atrophy: a randomised, placebo-controlled trial
Grunseich, C., Miller, R. R., Swan, T., Glass, D. J., Mouelhi, M. E., Fornaro, M., Pétricoul, O., Voštiar, I., Roubenoff, R., Meriggioli, M. N., et al. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30320-x · Cited by 45
Self-citation
Insulin‐Like Growth Factor I Regulation and Its Actions in Skeletal Muscle
Vassilakos, G., & Barton, E. R. (2018) · Comprehensive physiology · doi:10.1002/cphy.c180010 · Cited by 48
GLUT4 On the move
Fazakerley, D. J., Koumanov, F., & Holman, G. D. (2022) · Biochemical Journal · doi:10.1042/bcj20210073 · Cited by 44
Edward F. Adolph Distinguished Lecture. Skeletal muscle atrophy: Multiple pathways leading to a common outcome
Bodine, S. C. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00381.2020 · Cited by 47
Chronic heart failure reduces Akt phosphorylation in human skeletal muscle: relationship to muscle size and function
Toth, M. J., Ward, K., van der Velden, J. L. J., Miller, M. S., VanBuren, P., LeWinter, M. M., & Ades, P. A. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00545.2010 · Cited by 42
Immunobiological factors aggravating the fatty infiltration on tendons and muscles in rotator cuff lesions
Thankam, F., Dilisio, M. F., & Agrawal, D. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2710-5 · Cited by 44
The clinical relevance and mechanism of skeletal muscle wasting
Duan, K., Gao, X., & Zhu, D. (2020) · Clinical Nutrition · doi:10.1016/j.clnu.2020.07.029 · Cited by 44
Ghrelin relieves cancer cachexia associated with the development of lung adenocarcinoma in mice
Tsubouchi, H., Yanagi, S., Miura, A., Matsumoto, N., Kangawa, K., & Nakazato, M. (2014) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2014.09.025 · Cited by 41
Impaired overload-induced hypertrophy in obese Zucker rat slow-twitch skeletal muscle
Paturi, S., Gutta, A. K., Kakarla, S. K., Katta, A., Arnold, E. C., Wu, M., Rice, K. M., & Blough, E. R. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00330.2009 · Cited by 42
Metformin Treatment Prevents Sedentariness Related Damages in Mice
Senesi, P., Montesano, A., Luzi, L., Codella, R., Benedini, S., & Terruzzi, I. (2015) · Journal of Diabetes Research · doi:10.1155/2016/8274689 · Cited by 40
Whey Protein Ingestion Activates mTOR-dependent Signalling after Resistance Exercise in Young Men: A Double-Blinded Randomized Controlled Trial
Farnfield, M. M., Carey, K. A., Gran, P., Caldow, M. K., & Cameron‐Smith, D. (2009) · Nutrients · doi:10.3390/nu1020263 · Cited by 40
Repression of phosphatidylinositol transfer protein α ameliorates the pathology of Duchenne muscular dystrophy
Vieira, N. M., Spinazzola, J. M., Alexander, M. S., Moreira, Y. B., Kawahara, G., Gibbs, D. E., Mead, L., Verjovski‐Almeida, S., Zatz, M., & Kunkel, L. M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1703556114 · Cited by 41
Regulation of myogenesis by environmental hypoxia
Beaudry, M., Hidalgo, M., Launay, T., Bello, V., & Darribère, T. (2016) · Journal of Cell Science · doi:10.1242/jcs.188904 · Cited by 40
Maintaining skeletal muscle mass: lessons learned from hibernation
Ivakine, E. A., & Cohn, R. D. (2014) · Experimental Physiology · doi:10.1113/expphysiol.2013.074344 · Cited by 39
Effects of γ-aminobutyric acid-enriched fermented sea tangle (Laminaria japonica) on brain derived neurotrophic factor-related muscle growth and lipolysis in middle aged women
Choi, W.-C., Reid, S. N. S., Ryu, J.-K., Kim, Y., Jo, Y.-H., & Jeon, B. H. (2016) · ALGAE · doi:10.4490/algae.2016.31.6.12 · Cited by 39
Coffee consumption promotes skeletal muscle hypertrophy and myoblast differentiation
Jang, Y. J., Son, H. J., Kim, J., Jung, C. H., Ahn, J., Hur, J., & Ha, T. Y. (2018) · Food & Function · doi:10.1039/c7fo01683b · Cited by 39
Aging-Associated Changes in Physical Performance and Energy Metabolism in the Senescence-Accelerated Mouse
Haramizu, S., Ota, N., Hase, T., & Murase, T. (2011) · The Journals of Gerontology Series A · doi:10.1093/gerona/glr037 · Cited by 39
Therapeutic prospects to treat skeletal muscle wasting in COPD (chronic obstructive lung disease)
Hansen, M. J., Gualano, R. C., Bozinovski, S., Vlahos, R., & Anderson, G. P. (2005) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.06.007 · Cited by 36
Akt1 deficiency diminishes skeletal muscle hypertrophy by reducing satellite cell proliferation
Moriya, N., & Miyazaki, M. (2018) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00336.2017 · Cited by 39
Group I Paks Promote Skeletal Myoblast Differentiation In Vivo and In Vitro
Joseph, G. A., Lü, M., Radu, M., Lee, J. K., Burden, S. J., Chernoff, J., & Krauss, R. S. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00222-16 · Cited by 36
Granulocyte Colony-Stimulating Factor and Its Potential Application for Skeletal Muscle Repair and Regeneration
Wright, C. R., Ward, A. C., & Russell, A. P. (2017) · Mediators of Inflammation · doi:10.1155/2017/7517350 · Cited by 36
Nicotinamide protects against skeletal muscle atrophy in streptozotocin-induced diabetic mice
Guo, S., Chen, Q., Sun, Y., & Chen, J. (2019) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2019.1638414 · Cited by 37

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.
ORCID: Poueymirou, William T.
Stitt, Trevor N.
Economides, Aris N.
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
DOI: 10.1128/mcb.24.21.9295-9304.2004
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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

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 ›

Are you an author, or do you see a problem with this page? Request a review

Conditional Activation of Akt in Adult Skeletal Muscle Induces Rapid Hypertrophy

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks