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

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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

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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.

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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).

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Siddiqui, J. A., Pothuraju, R., Jain, M., Batra, S. K., & Nasser, M. W. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188359 · Cited by 126
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Calpain activation causes a proteasome‐dependent increase in protein degradation and inhibits the Akt signalling pathway in rat diaphragm muscle
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Inhibition of MAP/ERK kinase prevents IGF-I-induced hypertrophy in rat muscles
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Self-citation

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

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

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