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Glucocorticoid-induced skeletal muscle atrophy
Abstract
Many pathological states characterized by muscle atrophy (e.g., sepsis, cachexia, starvation, metabolic acidosis and severe insulinopenia) are associated with an increase in circulating glucocorticoids (GC) levels, suggesting that GC could trigger the muscle atrophy observed in these conditions. GC-induced muscle atrophy is characterized by fast-twitch, glycolytic muscles atrophy illustrated by decreased fiber cross-sectional area and reduced myofibrillar protein content. GC-induced muscle atrophy results from increased protein breakdown and decreased protein synthesis. Increased muscle proteolysis, in particular through the activation of the ubiquitin proteasome and the lysosomal systems, is considered to play a major role in the catabolic action of GC. The stimulation by GC of these two proteolytic systems is mediated through the increased expression of several Atrogenes ("genes involved in atrophy"), such as FOXO, Atrogin-1, and MuRF-1. The inhibitory effect of GC on muscle protein synthesis is thought to result mainly from the inhibition of the mTOR/S6 kinase 1 pathway. These changes in muscle protein turnover could be explained by changes in the muscle production of two growth factors, namely Insulin-like Growth Factor (IGF)-I, a muscle anabolic growth factor and Myostatin, a muscle catabolic growth factor. This review will discuss the recent progress made in the understanding of the mechanisms involved in GC-induced muscle atrophy and consider the implications of these advancements in the development of new therapeutic approaches for treating GC-induced myopathy. This article is part of a Directed Issue entitled: Molecular basis of muscle wasting.
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“Although the exact mechanism underlying glucocorticoid-induced skeletal muscle atrophy is unclear, it is considered to be multifactorial and is related to decreased protein synthesis, increased protein degradation, alterations in carbohydrate metabolism, oxidative stress, and/or decreased sarcolemmal excitability [16].”
From Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy (2021) · cites this paper as [16]
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1 retracted
FOXO1 Regulates the Expression of 4E-BP1 and Inhibits mTOR Signaling in Mammalian Skeletal Muscle
Southgate, R. J., Neill, B., Prelovsek, O., El‐Osta, A., Kamei, Y., Miura, S., Ezaki, O., McLoughlin, T. J., Zhang, W., Unterman, T. G., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702039200 · Cited by 112
RetractedmTOR Signaling in Growth Control and Disease
Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509
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
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
Double muscling in cattle due to mutations in the myostatin gene
McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039
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
Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539 · cited 1×
“…analyses of muscle atrophy due to a variety of wasting diseases are several genes (Atrogin-1, MuRF-1, Cathepsin-L, PDK4, p21, Gadd45, 4E-BP1) controlled by the FOXO transcription factors (Almon et al., 2007; Jagoe et al., 2002; Komamura et al., 2003; Lecker et al., 2004; Waddell et al., 2008).”
BackgroundMechanisms of Muscle Wasting — The Role of the Ubiquitin–Proteasome Pathway
Mitch, W. E., & Goldberg, A. L. (1996) · New England Journal of Medicine · doi:10.1056/nejm199612193352507 · Cited by 1,163
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
Myostatin, a Negative Regulator of Muscle Growth, Functions by Inhibiting Myoblast Proliferation
Thomas, M., Langley, B., Berry, C., Sharma, M., Kirk, S., Bass, J., & Kambadur, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004356200 · Cited by 1,014
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Pivonello, R., Isidori, A. M., Martino, M. C. D., Newell-Price, J. D. C., Biller, B. M. K., & Colao, A. (2016) · The Lancet Diabetes & Endocrinology · doi:10.1016/s2213-8587(16)00086-3 · Cited by 694
Cancer cachexia in adult patients: ESMO Clinical Practice Guidelines☆
Arends, J., Strasser, F., Gonella, S., Solheim, T. S., Madeddu, C., Ravasco, P., Buonaccorso, L., de van der Schueren, M. A. E., Baldwin, C., Chasen, M., et al. (2021) · ESMO Open · doi:10.1016/j.esmoop.2021.100092 · Cited by 586
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Porporato, P. E. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.3 · Cited by 562
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Kraemer, W. J., Ratamess, N. A., Hymer, W. C., Nindl, B. C., & Fragala, M. S. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00033 · Cited by 339
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The Determinants of Peak Bone Mass
Gordon, C. M., Zemel, B. S., Wren, T. A. L., Leonard, M. B., Bachrach, L. K., Rauch, F., Gilsanz, V., Rosen, C. J., & Winer, K. K. (2016) · The Journal of Pediatrics · doi:10.1016/j.jpeds.2016.09.056 · Cited by 238
Mangine, G. T., Hoffman, J. R., Gonzalez, A. M., Townsend, J. R., Wells, A. J., Jajtner, A. R., Beyer, K. S., Boone, C. H., Miramonti, A. A., Wang, R., et al. (2015) · Physiological Reports · doi:10.14814/phy2.12472 · Cited by 204
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Yang, Z., Nakagawa, K., Sarkar, A., Maruyama, J., Iwasa, H., Bao, Y., Ishigami‐Yuasa, M., Ito, S., Kagechika, H., Hata, S., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01346-13 · Cited by 58
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Beiter, T., Hoene, M., Prenzler, F., Mooren, F. C., Steinacker, J. M., Weigert, C., Niess, A. M., & Munz, B. (2026) · PubMed · doi:10.22029/eir.2015.1695 · Cited by 56
Cea, L. A., Balboa, E., Puebla, C., Vargas, A. A., Cisterna, B. A., Escamilla, R., Regueira, T., & Sáez, J. C. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.07.003 · Cited by 54
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Ulla, A., Uchida, T., Miki, Y., Sugiura, K., Higashitani, A., Kobayashi, T., Ohno, A., Nakao, R., Hirasaka, K., Sakakibara, I., et al. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108873 · Cited by 56
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Metadata
- Authors
- Schakman, O., Kalista, S., Barbé, C., Loumaye, A., & Thissen, J. P.
- Affiliations
- UCLouvain (BE)
- Corresponding author
- Thissen, J.P.
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2013-10
- Volume
- 45
- Issue
- 10
- Pages
- 2163-2172
- ISSN
- 1357-2725 (ISSN-L)
- OpenAlex
- W2092885411
- Cited by
- 705
- References
- 157
- Citations by year
- 2026: 81 · 2025: 74 · 2024: 58 · 2023: 60 · 2022: 68 · 2021: 62 · 2020: 58 · 2019: 43 · 2018: 44 · 2017: 37 · 2016: 45 · 2015: 48 · 2014: 24 · 2013: 2
- FWCI
- 3.73
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The International Journal of Biochemistry & Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Digital Access to Libraries (submittedVersion)
- Funders
- Fund for Scientific Medical Research (Belgium)
- National Fund for Scientific Research (Belgium)
- Association Française contre les Myopathies (France)
- Association Belge contre les Maladies neuro-musculaires
- Fonds Spéciaux de Recherche (Université catholique de Louvain, Belgium)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Health Sciences › Medicine › Physiology (medical) › Nutrition and Health in Aging
- Keywords
- glucocorticoid-induced muscle atrophy, skeletal muscle atrophy, muscle protein degradation, ubiquitin-proteasome system, lysosomal proteolysis, atrogenes, atrogin-1, MuRF1, FOXO, muscle protein synthesis, insulin-like growth factor I, myostatin, glucocorticoid-induced myopathy, cachexia, sepsis
- MeSH terms
- Animals, Glucocorticoids, Humans, Muscular Atrophy, Protein Biosynthesis, Signal Transduction
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