Cited by 1,583Muscle Physiology and DisordersMuscle metabolism and nutritionSignaling Pathways in Disease

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways

Rommel, Christian, Bodine, Sue C., Clarke, Brian A., Rossman, Roni, Nunez, Lorna, Stitt, Trevor N., Yancopoulos, George D., Glass, David J.·2001·Nature Cell Biology

DOI 10.1038/ncb1101-1009

Open this paper in CoChat — free account

Abstract

Skeletal muscle is composed of multinucleated fibres, formed after the differentiation and fusion of myoblast precursors. Skeletal muscle atrophy and hypertrophy refer to changes in the diameter of these pre-existing muscle fibres. The prevention of atrophy would provide an obvious clinical benefit; insulin-like growth factor 1 (IGF-1) is a promising anti-atrophy agent because of its ability to promote hypertrophy. However, the signalling pathways by which IGF-1 promotes hypertrophy remain unclear, with roles suggested for both the calcineurin/NFAT (nuclear factor of activated T cells) pathway and the PtdIns-3-OH kinase (PI(3)K)/Akt pathway. Here we employ a battery of approaches to examine these pathways during the hypertrophic response of cultured myotubes to IGF-1. We report that Akt promotes hypertrophy by activating downstream signalling pathways previously implicated in activating protein synthesis: the pathways downstream of mammalian target of rapamycin (mTOR) and the pathway activated by phosphorylating and thereby inhibiting glycogen synthase kinase 3 (GSK3). In contrast, in addition to demonstrating that calcineurin does not mediate IGF-1-induced hypertrophy, we show that IGF-1 unexpectedly acts via Akt to antagonize calcineurin signalling during myotube hypertrophy.

Integrity signals

Registry

Crossref · 10.1038/ncb1101-1009

Cites

24 of 24 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

This paper’s full text isn’t openly available, 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?

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
Regulation of neuronal survival by the serine-threonine protein kinase Akt
Dudek, H., Datta, S. R., Franke, T. F., Birnbaum, M. J., Yao, R., Cooper, G. M., Segal, R. A., Kaplan, D. R., & Greenberg, M. E. (1997) · Science · doi:10.1126/science.275.5300.661 · Cited by 2,436
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
Autonomous Control of Cell and Organ Size by CHICO, a Drosophila Homolog of Vertebrate IRS1–4
Böhni, R., Riesgo‐Escovar, J. R., Oldham, S., Brogiolo, W., Stocker, H., Andruss, B. F., Beckingham, K., & Hafen, E. (1999) · Cell · doi:10.1016/s0092-8674(00)80799-0 · Cited by 840
Drosophila S6 kinase: a regulator of cell size.
Montagne, J., Stewart, M. J., Stocker, H., Hafen, E., Kozma, S., & Thomas, G. (1999) · Science · doi:10.1126/science.285.5436.2126 · Cited by 785
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 760
Self-citation
IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1
Musarò, A., McCullagh, K. J. A., Naya, F. J., Olson, E. N., & Rosenthal, N. A. (1999) · Nature · doi:10.1038/23060 · Cited by 652
The Drosophila phosphoinositide 3‐kinase Dp110 promotes cell growth.
Leevers, S. J., Weinkove, D., MacDougall, L. K., Hafen, E., & Waterfield, M. D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01049.x · Cited by 484
Changes in muscle mass and phenotype and the expression of autocrine and systemic growth factors by muscle in response to stretch and overload
GOLDSPINK, G. (1999) · Journal of Anatomy · doi:10.1046/j.1469-7580.1999.19430323.x · Cited by 435
SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival
Liu, Q., Sasaki, T., Kozieradzki, I., Wakeham, A., Itie, A., Dumont, D. J., & Penninger, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.7.786 · Cited by 341

Show all 24 references

Research works printed but not linked: 3

Engel, A. G. & Fanzine-Armstrong, C. Myology 1937 (McGraw-Hill, New York, 1994).
Florini, J. R., Ewton, D. Z. & Coolican, S. A. Endocr. Rev. 17, 481–517 (1996).
Yu, H. & Berkel, H. J. LA State Med. Soc. 151, 218–223 (1999).

Sorted by citations

Items 401–500 of 1,004

Effects of Monochromatic Light on Developmental Changes in Satellite Cell Population of Pectoral Muscle in Broilers During Early Posthatch Period
Liu, W., Wang, Z., & Chen, Y. (2010) · The Anatomical Record · doi:10.1002/ar.21174 · Cited by 79
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
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
Regulating Fibrinolysis to Engineer Skeletal Muscle from the C2C12 Cell Line
Khodabukus, A., & Baar, K. (2009) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2008.0286 · Cited by 78
Elevated levels of active matrix metalloproteinase-9 cause hypertrophy in skeletal muscle of normal and dystrophin-deficient mdx mice
Dahiya, S., Bhatnagar, S., Hindi, S. M., Jiang, C., Paul, P. K., Kuang, S., & Kumar, A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr362 · Cited by 78
Maintaining proteostasis under mechanical stress
Höhfeld, J., Benzing, T. R., Bloch, W., Fürst, D. O., Gehlert, S., Hesse, M., Hoffmann, B., Hoppe, T., Huesgen, P. F., Köhn, M., et al. (2021) · EMBO Reports · doi:10.15252/embr.202152507 · Cited by 77
Skeletal myocyte hypertrophy requires mTOR kinase activity and S6K1
Park, I., Erbay, E., Nuzzi, P. D., & Chen, J. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.05.017 · Cited by 77
Rheb and mTOR Regulate Neuronal Polarity through Rap1B
Li, Y., Werner, H., & Püschel, A. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802431200 · Cited by 77
Preventive effect of dietary quercetin on disuse muscle atrophy by targeting mitochondria in denervated mice
Mukai, R., Matsui, N., Fujikura, Y., Matsumoto, N., Hou, D., Kanzaki, N., Shibata, H., Horikawa, M., Iwasa, K., Hirasaka, K., et al. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.02.001 · Cited by 76
Hypergravity and microgravity exhibited reversal effects on the bone and muscle mass in mice
Tominari, T., Ichimaru, R., Taniguchi, K., Yumoto, A., Shirakawa, M., Matsumoto, C., Watanabe, K., Hirata, M., Itoh, Y., Shiba, D., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-42829-z · Cited by 76
Glycogen Synthase Kinase 3β Suppresses Myogenic Differentiation through Negative Regulation of NFATc3
van der Velden, J. L. J., Schols, A. M. W. J., Willems, J., KELDERS, M. C. J. M., & LANGEN, R. C. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707812200 · Cited by 75
Changes in PKB/Akt and calcineurin signaling during recovery in atrophied soleus muscle induced by unloading
Sugiura, T., Abe, N., Nagano, M., Goto, K., Sakuma, K., Naıto, H., Yoshioka, T., & Powers, S. K. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00688.2004 · Cited by 75
Enhanced Development of Skeletal Myotubes from Porcine Induced Pluripotent Stem Cells
Genovese, N. J., Domeier, T. L., Telugu, B. P. V. L., & Roberts, R. M. (2017) · Scientific Reports · doi:10.1038/srep41833 · Cited by 75
Mechanisms involved in follistatin‐induced hypertrophy and increased insulin action in skeletal muscle
Han, X., Møller, L. L. V., Groote, E. D., Bojsen-Møller, K. N., Davey, J. R., Henríquez‐Olguín, C., Li, Z., Knudsen, J. R., Jensen, T. E., Madsbad, S., et al. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12474 · Cited by 75
Differential signalling mechanisms predisposing primary human skeletal muscle cells to altered proliferation and differentiation: roles of IGF-I and TNFα
Foulstone, E. J., Huser, C. A. M., Crown, A. L., Holly, J. M. P., & Stewart, C. E. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.10.034 · Cited by 75
Postexercise hypertrophic adaptations: A reexamination of the hormone hypothesis and its applicability to resistance training program design
Schoenfeld, B. J. (2013) · Journal of Strength and Conditioning Research · doi:10.1519/jsc.0b013e31828ddd53 · Cited by 74
Involvement of PI3K/Akt/TOR pathway in stretch‐induced hypertrophy of myotubes
Sasai, N., Agata, N., Inoue‐Miyazu, M., Kawakami, K., Kobayashi, K., Sokabe, M., & Hayakawa, K. (2009) · Muscle & Nerve · doi:10.1002/mus.21473 · Cited by 74
TWEAK/Fn14 Signaling Axis Mediates Skeletal Muscle Atrophy and Metabolic Dysfunction
Sato, S., Ogura, Y., & Kumar, A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00018 · Cited by 74
Mutual Antagonism of Target of Rapamycin and Calcineurin Signaling
Mulet, J. M., Martin, D. E., Loewith, R., & Hall, M. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604244200 · Cited by 74
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
L‐Arginine Enhances Protein Synthesis by Phosphorylating mTOR (Thr 2446) in a Nitric Oxide‐Dependent Manner in C2C12 Cells
Wang, R., Jiao, H., Zhao, J., Wang, X., & Lin, H. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7569127 · Cited by 74
GSK3-β promotes calpain-1–mediated desmin filament depolymerization and myofibril loss in atrophy
Aweida, D., Rudesky, I., Volodin, A., Shimko, E., & Cohen, S. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201802018 · Cited by 73
Loss of mitochondrial energetics is associated with poor recovery of muscle function but not mass following disuse atrophy
Trevino, M. B., Zhang, X., Standley, R. A., Wang, M., Han, X., Reis, F. C. G., Periasamy, M., Yu, G., Kelly, D. P., Goodpaster, B. H., et al. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00161.2019 · Cited by 73
Cancer-Mediated Muscle Cachexia: Etiology and Clinical Management
Siff, T. E., Parajuli, P., Razzaque, M. S., & Atfi, A. (2021) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2021.03.007 · Cited by 73
An Image Analysis Method for the Precise Selection and Quantitation of Fluorescently Labeled Cellular Constituents
Agley, C. C., Velloso, C. P., Lazarus, N. R., & Harridge, S. D. R. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412442897 · Cited by 73
Delving into disability in Crohn's disease: Dysregulation of molecular pathways may explain skeletal muscle loss in Crohn's disease
van Langenberg, D. R., Gatta, P. A. D., Hill, B., Zacharewicz, E., Gibson, P. R., & Russell, A. P. (2013) · Journal of Crohn s and Colitis · doi:10.1016/j.crohns.2013.11.024 · Cited by 73
Cisplatin triggers atrophy of skeletal C2C12 myotubes via impairment of Akt signalling pathway and subsequent increment activity of proteasome and autophagy systems
Fanzani, A., Zanola, A., Rovetta, F., Rossi, S., & Aleo, M. F. (2010) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2010.11.003 · Cited by 73
Muscle length and myonuclear position are independently regulated by distinct Dynein pathways
Folker, E. S., Schulman, V. K., & Baylies, M. K. (2012) · Development · doi:10.1242/dev.079178 · Cited by 73
Insulin-Like Growth Factor I-Mediated Skeletal Muscle Hypertrophy is Characterized by Increased mTOR-p70S6K Signaling without Increased Akt Phosphorylation
Song, Y., Godard, M. P., Li, Y., Richmond, S. R., Rosenthal, N. A., & Delafontaine, P. (2005) · Journal of Investigative Medicine · doi:10.2310/6650.2005.00309 · Cited by 73
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
Microalgae Produce Antioxidant Molecules with Potential Preventive Effects on Mitochondrial Functions and Skeletal Muscular Oxidative Stress
Vignaud, J., Loiseau, C., Hérault, J., Mayer, C., Côme, M., Martin, I., & Ulmann, L. (2023) · Antioxidants · doi:10.3390/antiox12051050 · Cited by 72
Inhibition of TPO-induced MEK or mTOR activity induces opposite effects on the ploidy of human differentiating megakaryocytes
Guerriero, R., Parolini, I., Testa, U., Samoggia, P., Petrucci, E., Sargiacomo, M., Chelucci, C., Gabbianelli, M., & Peschle, C. (2006) · Journal of Cell Science · doi:10.1242/jcs.02784 · Cited by 72
Myoferlin is required for insulin‐like growth factor response and muscle growth
Demonbreun, A. R., Posey, A. D., Heretis, K., Swaggart, K. A., Earley, J. U., Pytel, P., & McNally, E. M. (2009) · The FASEB Journal · doi:10.1096/fj.09-136309 · Cited by 72
Deacetylase Inhibitors Modulate the Myostatin/Follistatin Axis without Improving Cachexia in Tumor-Bearing Mice
Bonetto, A., Penna, F., Minero, V. G., Reffo, P., Bonelli, G., Baccino, F. M., & Costelli, P. (2009) · Current Cancer Drug Targets · doi:10.2174/156800909789057015 · Cited by 72
Exercise-Induced Insulin-Like Growth Factor I System Concentrations after Training in Women
Gregory, S. M., Spiering, B. A., Alemany, J. A., Tuckow, A. P., Rarick, K. R., Staab, J. S., Hatfield, D. L., Kraemer, W. J., Maresh, C. M., & Nindl, B. C. (2013) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3182750bd4 · 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
Diet‐induced obesity alters anabolic signalling in mice at the onset of skeletal muscle regeneration
Brown, L. A., Lee, D. E., Patton, J. F., Perry, R. A., Brown, J. L., Baum, J., Smith‐Blair, N., Greene, N. P., & Washington, T. A. (2015) · Acta Physiologica · doi:10.1111/apha.12537 · Cited by 71
Rapamycin Ameliorates Dystrophic Phenotype in mdx Mouse Skeletal Muscle
Eghtesad, S., Jhunjhunwala, S., Little, S. R., & Clemens, P. R. (2011) · Molecular Medicine · doi:10.2119/molmed.2010.00256 · Cited by 71
Halofuginone inhibits Smad3 phosphorylation via the PI3K/Akt and MAPK/ERK pathways in muscle cells: Effect on myotube fusion
Roffe, S., Hagai, Y., Pines, M., & Halevy, O. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.01.003 · Cited by 71
Systemic administration of IGF-I enhances oxidative status and reduces contraction-induced injury in skeletal muscles of mdx dystrophic mice
Schertzer, J. D., Ryall, J. G., & Lynch, G. S. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00101.2006 · Cited by 71
Restricted epithelial proliferation by lacritin via PKCα-dependent NFAT and mTOR pathways
Wang, J., Wang, N., Xie, J., Walton, S. C., McKown, R. L., Raab, R. W., Ma, P., Beck, S. L., Coffman, G. L., Hussaini, I. M., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605140 · Cited by 71
mTOR signaling regulates myotube hypertrophy by modulating protein synthesis, rDNA transcription, and chromatin remodeling
von Walden, F., Liu, C., Aurigemma, N., & Nader, G. A. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00144.2016 · Cited by 70
Mechanism of skeletal muscle atrophy after spinal cord injury: A narrative review
Xu, X. P., Talifu, Z., Zhang, C.-J., Gao, F., Ke, H., Pan, Y., Gong, H., Du, H., Yu, Y. H., Jing, Y.-L., et al. (2023) · Frontiers in Nutrition · doi:10.3389/fnut.2023.1099143 · Cited by 70
Regulation of Akt-mTOR, ubiquitin-proteasome and autophagy-lysosome pathways in response to formoterol administration in rat skeletal muscle
Joassard, O. R., Amirouche, A., Gallot, Y. S., Desgeorges, M. M., Castells, J., Durieux, A., Berthon, P. M., & Freyssenet, D. G. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.07.019 · Cited by 70
Discovery and characterization of nutritionally regulated genes associated with muscle growth in Atlantic salmon
Bower, N. I., & Johnston, I. A. (2010) · Physiological Genomics · doi:10.1152/physiolgenomics.00065.2010 · Cited by 70
Differential Gene Expression in the Rat Skeletal and Heart Muscle in Glucocorticoid-Induced Myopathy: Analysis by Microarray
Komamura, K., Shirotani-Ikejima, H., Tatsumi, R., Tsujita-Kuroda, Y., Kitakaze, M., Miyatake, K., Sunagawa, K., & Miyata, T. (2003) · Cardiovascular Drugs and Therapy · doi:10.1023/a:1027352703783 · Cited by 70
Human and mouse skeletal muscle stem and progenitor cells in health and disease
Mierzejewski, B., Archacka, K., Grabowska, I., Florkowska, A., Ciemerych, M. A., & Brzóska, E. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.01.004 · Cited by 70
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
Acute myotube protein synthesis regulation by IL-6-related cytokines
Gao, S., Durstine, J. L., Koh, H.-J., Carver, W. E., Frizzell, N., & Carson, J. A. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00112.2017 · Cited by 69
Extracellular signal-regulated kinase pathway is differentially involved in β-agonist-induced hypertrophy in slow and fast muscles
Shi, H., Zeng, C., Ricome, A., Hannon, K., Grant, A. L., & Gerrard, D. E. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00466.2006 · Cited by 69
Differential regulation of the phosphoinositide 3-kinase and MAP kinase pathways by hepatocyte growth factor vs. insulin-like growth factor-I in myogenic cells
Halevy, O., & Cantley, L. C. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.03.024 · Cited by 69
Phasing of muscle gene expression with fasting-induced recovery growth in Atlantic salmon
Bower, N. I., Taylor, R. G., & Johnston, I. A. (2009) · Frontiers in Zoology · doi:10.1186/1742-9994-6-18 · Cited by 69
Beyond its Psychiatric Use: The Benefits of Low-dose Lithium Supplementation
Hamstra, S. I., Roy, B. D., Tiidus, P. M., MacNeil, A. J., Klentrou, P., MacPherson, R. E. K., & Fajardo, V. A. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666220302151224 · Cited by 68
Erythropoietin receptor in human skeletal muscle and the effects of acute and long-term injections with recombinant human erythropoietin on the skeletal muscle
Lundby, C., Hellsten, Y., Jensen, M. B. F., Munch, A. S., & Pilegaard, H. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01211.2007 · Cited by 68
Glucocorticoids Enhance Muscle Proteolysis through a Myostatin-Dependent Pathway at the Early Stage
Wang, R., Jiao, H., Zhao, J., Wang, X., & Lin, H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0156225 · Cited by 68
Meta-analysis of expression signatures of muscle atrophy: gene interaction networks in early and late stages
Calura, E., Cagnin, S., Raffaello, A., Laveder, P., Lanfranchi, G., & Romualdi, C. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-630 · Cited by 67
Similar acute molecular responses to equivalent volumes of isometric, lengthening, or shortening mode resistance exercise
Garma, T., Kobayashi, C., Haddad, F., Adams, G. R., Bodell, P. W., & Baldwin, K. M. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00776.2006 · Cited by 67
Role for the Pleckstrin Homology Domain-Containing Protein CKIP-1 in Phosphatidylinositol 3-Kinase-Regulated Muscle Differentiation
Safi, A., Vandromme, M., Caussanel-Boude, S., Valdacci, L., Baas, D., Vidal, M., Brun, G., Schaeffer, L., & Goillot, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.1245-1255.2004 · Cited by 67
Myogenic Akt signaling attenuates muscular degeneration, promotes myofiber regeneration and improves muscle function in dystrophin-deficient mdx mice
Kim, M. H., Kay, D. I., Rudra, R. T., Chen, B. M., Hsu, N., Izumiya, Y., Martinez, L., Spencer, M. J., Walsh, K. X., Grinnell, A. D., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr015 · Cited by 67
Denervation atrophy is independent from Akt and mTOR activation and is not rescued by myostatin inhibition
MacDonald, E. M., Andrés‐Mateos, E., Mejías, R., Simmers, J. L., Mi, R., Park, J.-S., Ying, S., Höke, A., Lee, S., & Cohn, R. D. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.014126 · Cited by 67
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
Permissive Roles of Phosphatidyl Inositol 3-Kinase and Akt in Skeletal Myocyte Maturation
Wilson, E. M., Turečková, J., & Rotwein, P. S. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-05-0351 · 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
Muscle-specific GSK-3β ablation accelerates regeneration of disuse-atrophied skeletal muscle
Pansters, N. A. M., Schols, A. M. W. J., Verhees, K. J. P., de Theije, C. C., Snepvangers, F. J. M., KELDERS, M. C. J. M., Ubags, N. D. J., Haegens, A., & LANGEN, R. C. J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.12.006 · Cited by 66
Inpp5f Is a Polyphosphoinositide Phosphatase That Regulates Cardiac Hypertrophic Responsiveness
Zhu, W., Trivedi, C. M., Zhou, D. D., Yuan, L., Lu, M. M., & Epstein, J. A. (2009) · Circulation Research · doi:10.1161/circresaha.109.208785 · Cited by 66
Skeletal Muscle Recovery from Disuse Atrophy: Protein Turnover Signaling and Strategies for Accelerating Muscle Regrowth
Mirzoev, T. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217940 · Cited by 65
Adenovirus Entry From the Apical Surface of Polarized Epithelia Is Facilitated by the Host Innate Immune Response
Kotha, P. L. N., Sharma, P., Kolawole, A. O., Yan, R., Alghamri, M. S., Brockman, T. L., Gómez-Cambronero, J., & Excoffon, K. J. D. A. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004696 · Cited by 65
Longitudinal characterization of functional, morphologic, and biochemical adaptations in mouse skeletal muscle with hindlimb suspension
Hanson, A. M., Harrison, B. C., Young, M. H., Stodieck, L., & Ferguson, V. L. (2012) · Muscle & Nerve · doi:10.1002/mus.23753 · Cited by 65
Paralogs of Atlantic salmon myoblast determination factor genes are distinctly regulated in proliferating and differentiating myogenic cells
Bower, N. I., & Johnston, I. A. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00114.2010 · Cited by 65
Translational Control Mechanisms Modulate Skeletal Muscle Gene Expression During Hypertrophy
Bolster, D. R., Kimball, S. R., & Jefferson, L. S. (2003) · Exercise and Sport Sciences Reviews · doi:10.1097/00003677-200307000-00002 · Cited by 65
Biology of Activating Transcription Factor 4 (ATF4) and Its Role in Skeletal Muscle Atrophy
Ebert, S. M., Rasmussen, B. B., Judge, A. R., Judge, S. M., Larsson, L., Wek, R. C., Anthony, T. G., Marcotte, G. R., Miller, M. J., Yorek, M. A., et al. (2021) · Journal of Nutrition · doi:10.1093/jn/nxab440 · Cited by 64
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
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
Reduced AMPK-ACC and mTOR signaling in muscle from older men, and effect of resistance exercise
Li, M., Verdijk, L. B., Sakamoto, K., Ely, B. A., van Loon, L. J. C., & Musi, N. (2012) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2012.09.001 · Cited by 64
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
Constitutively active Akt1 expression in mouse pancreas requires S6 kinase 1 for insulinoma formation
Alliouachene, S., Tuttle, R. L., Boumard, S., Lapointe, T., Bérissi, S., Germain, S., Jaubert, F., Tosh, D., Birnbaum, M. J., & Pende, M. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35237 · Cited by 64
Cellular Prion Protein Promotes Regeneration of Adult Muscle Tissue
Stella, R., Massimino, M. L., Sandri, M., Sorgato, M. C., & Bertoli, A. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01040-09 · Cited by 64
Pten Deficiency Activates Distinct Downstream Signaling Pathways in a Tissue-Specific Manner
Yoo, L. I., Liu, D. W., Vu, S. L., Bronson, R. T., Wu, H., & Yuan, J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-1986 · Cited by 64
RNA processing in skeletal muscle biology and disease
Hinkle, E. R., Wiedner, H. J., Black, A. J., & Giudice, J. (2018) · Transcription · doi:10.1080/21541264.2018.1558677 · Cited by 63
Osteocyte-Mediated Translation of Mechanical Stimuli to Cellular Signaling and Its Role in Bone and Non-bone-Related Clinical Complications
Yan, Y., Wang, L., Ge, L., & Pathak, J. L. (2020) · Current Osteoporosis Reports · doi:10.1007/s11914-020-00564-9 · Cited by 63
Insulin-like growth factor (IGF) signalling and genome-wide transcriptional regulation in fast muscle of zebrafish following a single-satiating meal
do Amaral, I. P. G., & Johnston, I. A. (2011) · Journal of Experimental Biology · doi:10.1242/jeb.053298 · Cited by 63
Inactivation of glycogen synthase kinase-3β (GSK-3β) enhances skeletal muscle oxidative metabolism
Theeuwes, W. F., Gosker, H. R., LANGEN, R. C. J., Verhees, K. J. P., Pansters, N., Schols, A. M. W. J., & Remels, A. H. V. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.018 · Cited by 63
Molecular therapeutic strategies targeting pancreatic cancer induced cachexia
Yakovenko, A., Cameron, M. E., & Trevino, J. (2018) · World Journal of Gastrointestinal Surgery · doi:10.4240/wjgs.v10.i9.95 · Cited by 63
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
The Role of GSK-3β in the Regulation of Protein Turnover, Myosin Phenotype, and Oxidative Capacity in Skeletal Muscle under Disuse Conditions
Mirzoev, T. M., Sharlo, K. A., & Shenkman, B. S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105081 · Cited by 63
Expression of β-catenin is necessary for physiological growth of adult skeletal muscle
Armstrong, D., Wong, V. L., & Esser, K. A. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00644.2005 · Cited by 63
Betaine improves the growth performance and muscle growth of partridge shank broiler chickens via altering myogenic gene expression and insulin-like growth factor-1 signaling pathway
Chen, R., Zhuang, S., Chen, Y. P., Cheng, Y., Wen, C., & Zhou, Y. (2018) · Poultry Science · doi:10.3382/ps/pey303 · Cited by 62
Variable resistance training promotes greater fatigue resistance but not hypertrophy versus constant resistance training
Walker, S., Hulmi, J. J., Wernbom, M., Nyman, K., Kraemer, W. J., Ahtiainen, J. P., & Häkkinen, K. (2013) · European Journal of Applied Physiology · doi:10.1007/s00421-013-2653-4 · Cited by 62
Myogenic differentiation during regrowth of atrophied skeletal muscle is associated with inactivation of GSK-3β
van der Velden, J. L. J., LANGEN, R. C. J., KELDERS, M. C. J. M., Willems, J., Wouters, E. F. �., Janssen-Heininger, Y. M. W., & Schols, A. M. W. J. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00504.2006 · Cited by 62
GSK-3β inhibitors reduce protein degradation in muscles from septic rats and in dexamethasone-treated myotubes
Evenson, A. R., Fareed, M. U., Menconi, M. J., Mitchell, J. C., & Hasselgren, P.-O. J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.06.002 · Cited by 62
Gene expression and muscle fiber function in a porcine ICU model
Banduseela, V. C., Ochala, J., Chen, Y., Göransson, H., Norman, H. S., Radell, P. J., Eriksson, L. I., Hoffman, E. P., & Larsson, L. (2009) · Physiological Genomics · doi:10.1152/physiolgenomics.00026.2009 · Cited by 62
Cancer‐ and Chemotherapy‐Induced Musculoskeletal Degradation
Sturgeon, K. M., Mathis, K. M., Rogers, C. J., Schmitz, K. H., & Waning, D. L. (2019) · JBMR Plus · doi:10.1002/jbm4.10187 · Cited by 61
Andrographolide suppresses melanin synthesis through Akt/GSK3β/β-catenin signal pathway
Zhu, P., Yin, W.-H., Wang, M., Dang, Y., & Ye, X. (2015) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2015.03.013 · Cited by 61
The secretome of the working human skeletal muscle—A promising opportunity to combat the metabolic disaster?
Weigert, C., Lehmann, R., Hartwig, S., & Lehr, S. (2013) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201300094 · Cited by 61
Effects of paternal obesity on growth and adiposity of male rat offspring
Lecomte, V., Maloney, C., Wang, K. W., & Morris, M. J. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00262.2016 · Cited by 61
TAK1 regulates skeletal muscle mass and mitochondrial function
Hindi, S. M., Sato, S., Xiong, G., Bohnert, K. R., Gibb, A., Gallot, Y. S., McMillan, J. D., Hill, B. G., Uchida, S., & Kumar, A. (2018) · JCI Insight · doi:10.1172/jci.insight.98441 · Cited by 61
Redox modulation of muscle mass and function
Gómez‐Cabrera, M. C., Arc‐Chagnaud, C., Salvador‐Pascual, A., Brioche, T., Chopard, A., González, G. O., & Viña, J. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101531 · Cited by 61
Review article: the aetiology of fatigue in inflammatory bowel disease and potential therapeutic management strategies
McGing, J. J., Radford, S. J., Francis, S. T., Serres, S., Greenhaff, P. L., & Moran, G. W. (2021) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.16465 · Cited by 60
miR‐29c improves skeletal muscle mass and function throughout myocyte proliferation and differentiation and by repressing atrophy‐related genes
Silva, W. J., Graça, F. A., Cruz, A., Silvestre, J. G., Labeit, S., Miyabara, E. H., Yan, C. Y. I., Wang, D. Z., & Moriscot, A. S. (2019) · Acta Physiologica · doi:10.1111/apha.13278 · Cited by 60
Blood Flow Restriction During Futsal Training Increases Muscle Activation and Strength
Amani-Shalamzari, S., Farhani, F., Rajabi, H., Abbasi, A., Sarikhani, A., Paton, C. D., Bayati, M., Berdejo-del-Fresno, D., Rosemann, T. J., Nikolaidis, P. Τ., et al. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00614 · Cited by 60

Authors: Rommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J.
Affiliations: Regeneron (United States) (US)
Corresponding author: Glass, David J.
ORCID: Bodine, Sue C.
Clarke, Brian A.
Stitt, Trevor N.
Glass, David J.
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2001-10-05
Volume: 3
Issue: 11
Pages: 1009-1013
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/ncb1101-1009
OpenAlex: W1530473805
Cited by: 1,583
References: 24
Citations by year: 2026: 29 · 2025: 37 · 2024: 60 · 2023: 48 · 2022: 73 · 2021: 72 · 2020: 60 · 2019: 63 · 2018: 75 · 2017: 68 · 2016: 71 · 2015: 78 · 2014: 82 · 2013: 107 · 2012: 101
FWCI: 12.69
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
Funders: 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 › Signaling Pathways in Disease
Keywords: insulin-like growth factor I, skeletal muscle hypertrophy, myotubes, PI3K/Akt signaling, mTOR, glycogen synthase kinase-3, calcineurin, NFAT, muscle atrophy, protein synthesis
MeSH terms: Phosphoinositide-3 Kinase Inhibitors, Animals, Carrier Proteins, Cell Differentiation, Cell Line, Insulin-Like Growth Factor I, Muscular Atrophy, Phosphoproteins, Phosphorylation, Protein Kinases, Proto-Oncogene Proteins, Signal Transduction, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Muscle, Skeletal, Cell Cycle Proteins, Calcineurin, Phosphatidylinositol 3-Kinases, Ribosomal Protein S6 Kinases, Glycogen Synthase Kinases, Glycogen Synthase Kinase 3, Eukaryotic Initiation Factors, Protein Kinase Inhibitors, Adaptor Proteins, Signal Transducing, Proto-Oncogene Proteins c-akt, Mice, 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 ›

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

Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways

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