Mechanisms of glucocorticoid-induced myopathy

Schakman, O; Gilson, H; Thissen, J P

doi:10.1677/joe-07-0606

Cited by 521Muscle Physiology and DisordersMuscle metabolism and nutritionNutrition and Health in Aging

Mechanisms of glucocorticoid-induced myopathy

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Schakman, O, Gilson, H, Thissen, J P·2008·Journal of Endocrinology

DOI 10.1677/joe-07-0606

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Abstract

Glucocorticoid-induced muscle atrophy is characterized by fast-twitch or type II muscle fiber atrophy illustrated by decreased fiber cross-sectional area and reduced myofibrillar protein content. Muscle proteolysis, in particular through the ubiquitin– proteasome system (UPS), is considered to play a major role in the catabolic action of glucocorticoids. The stimulation by glucocorticoids of the UPS is mediated through the increased expression of several atrogenes (‘genes involved in atrophy’), such as atrogin-1 and MuRF-1, two ubiquitin ligases involved in the targeting of protein to be degraded by the proteasome machinery. Glucocorticoids also exert an anti-anabolic action by blunting muscle protein synthesis. These changes in protein turnover may result from changes in the production of two growth factors which control muscle mass, namely IGF-I and myostatin respectively anabolic and catabolic toward the skeletal muscle. The decreased production of IGF-I as well as the increased production of myostatin have been both demonstrated to contribute to the muscle atrophy caused by glucocorticoids. At the molecular level, IGF-I antagonizes the catabolic action of glucocorticoids by inhibiting, through the PI3-kinase/Akt pathway, the activity of the transcription factor FOXO, a major switch for the stimulation of several atrogenes. These recent progress in the understanding of the glucocorticoid-induced muscle atrophy should allow to define new therapies aiming to minimize this myopathy. Promising new therapeutic approaches for treating glucocorticoid-induced muscle atrophy are also presented in this review.

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GCs directly activated muscle ring finger-1 and atrogin-1, proteins involved in skeletal muscle proteolysis.
“GCs directly activated muscle ring finger-1 and atrogin-1, proteins involved in skeletal muscle proteolysis [43]”
From Low-dose glucocorticoid treatment affects multiple aspects of intermediary metabolism in healthy humans: a randomised controlled trial (2011) · cites this paper as [43]
The Catabolic action of glucocorticoids section says glucocorticoids stimulate expression of atrogin-1 and MuRF-1, ubiquitin ligases involved in muscle protein degradation. The FOXO section describes this as part of a transcriptional program mediated by FOXO; it does not establish that glucocorticoids directly activate the two proteins. Page numbers were not available in our copy. (LLM, conf=0.87)
Experimental — accuracy not yet measured
Hypercortisolism can present clinically with proximal muscle weakness due to endogenous glucocorticoid excess.
“Hypercortisolism can present clinically with proximal muscle weakness due to endogenous glucocorticoid excess.”
From Age-related and disease-related muscle loss: The effect of diabetes, obesity, and other diseases (2014) · cites this paper as [99]
Glucocorticoids inhibit protein synthesis and stimulate protein degradation in skeletal muscles; IGF-1 is decreased and myostatin is increased.
“Glucocorticoids inhibit protein synthesis and stimulate protein degradation in skeletal muscles. IGF-1 is decreased and myostatin is increased.99”
From Age-related and disease-related muscle loss: The effect of diabetes, obesity, and other diseases (2014) · cites this paper as [99]

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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 105 · see citing works
Retracted
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013 · see citing works
JOURNAL OF CLINICAL ENDOCRINOLOGY AND METABOLISM
Hoskins, R. G. (1953) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem-13-4-473 · Cited by 3,806 · see citing works
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 · see citing works
Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.
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
Advances in Experimental Medicine and Biology
Lunt, G. G. (1986) · Neurochemistry International · doi:10.1016/0197-0186(86)90020-3 · Cited by 1,881 · see citing works
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 · see citing works
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 · see citing works
The American Journal of Respiratory and Critical Care Medicine
Klocke, R. A., & Sylvester, J. T. (1994) · American Journal of Respiratory and Critical Care Medicine · Cited by 1,307 · see citing works
Mechanisms 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 · see citing works
Proceedings of the Society for Experimental Biology and Medicine
(2010) · Proceedings of The Society for Experimental Biology and Medicine · doi:10.1111/(issn)1525-1373 · Cited by 1,098 · see citing works
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 1,092 · see citing works
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 · see citing works
Myostatin negatively regulates satellite cell activation and self-renewal
McCroskery, S., Thomas, M., Maxwell, L., Sharma, M., & Kambadur, R. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207056 · Cited by 784 · see citing works
Muscle Protein Breakdown and the Critical Role of the Ubiquitin-Proteasome Pathway in Normal and Disease States
Lecker, S. H., Solomon, V., Mitch, W. E., & Goldberg, A. L. (1999) · Journal of Nutrition · doi:10.1093/jn/129.1.227s · Cited by 732 · see citing works
Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
Du, J., Wang, X., Miereles, C., Bailey, J. L., Debigaré, R., Zheng, B., Price, S. R., & Mitch, W. E. (2004) · Journal of Clinical Investigation · doi:10.1172/jci18330 · Cited by 730 · see citing works
European Journal of Clinical Investigation
Holgate, S. T. (2010) · European Journal of Clinical Investigation · doi:10.1111/(issn)1365-2362 · Cited by 645 · see citing works
Signaling Pathways and Molecular Mechanisms through which Branched-Chain Amino Acids Mediate Translational Control of Protein Synthesis
Kimball, S. R., & Jefferson, L. S. (2006) · Journal of Nutrition · doi:10.1093/jn/136.1.227s · Cited by 637 · see citing works
IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
Sacheck, J. M., Ohtsuka, A., McLary, S. C., & Goldberg, A. L. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00073.2004 · Cited by 606 · see citing works
Skeletal Muscle FOXO1 (FKHR) Transgenic Mice Have Less Skeletal Muscle Mass, Down-regulated Type I (Slow Twitch/Red Muscle) Fiber Genes, and Impaired Glycemic Control
Kamei, Y., Miura, S., SUZUKI, M. T., Kai, Y., Mizukami, J., Taniguchi, T., Mochida, K., Tomoko, H. A. T. A., Matsuda, J., Aburatani, H., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400674200 · Cited by 574 · see citing works
Growth hormone and the insulin-like growth factor system in myogenesis
Florini, J. R. (1996) · Endocrine Reviews · doi:10.1210/er.17.5.481 · Cited by 536 · see citing works
Testosterone administration to older men improves muscle function: molecular and physiological mechanisms
Ferrando, A. A., Sheffield-Moore, M., Yeckel, C. W., Gilkison, C., Jiang, J., Achacosa, A., Lieberman, S. A., Tipton, K., Wolfe, R. R., & Urban, R. J. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00362.2001 · Cited by 522 · see citing works
Insulin-like Growth Factor-1 (IGF-1) Inversely Regulates Atrophy-induced Genes via the Phosphatidylinositol 3-Kinase/Akt/Mammalian Target of Rapamycin (PI3K/Akt/mTOR) Pathway*
Latres, E., Amini, A. R., Amini, A. A., Griffiths, J. S., Martin, F. J., Wei, Y., Lin, H. C., Yancopouloš, G., & Glass, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m407517200 · Cited by 514 · see citing works
Corticosteroids Contribute to Muscle Weakness in Chronic Airflow Obstruction
Decramer, M., Lacquet, L. M., Fagard, R., & Rogiers, P. (1994) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.150.1.8025735 · Cited by 481 · see citing works
Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NF‐κB‐independent, FoxO1‐dependent mechanism
McFarlane, C., Plummer, E., Thomas, M., Hennebry, A., Ashby, M. G., Ling, N., Smith, H., Sharma, M., & Kambadur, R. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20757 · Cited by 480 · see citing works
Glucocorticoid-induced skeletal muscle atrophy is associated with upregulation of myostatin gene expression
Ma, K., Mallidis, C., Bhasin, S., Mahabadi, V., Artaza, J., González-Cadavid, N. F., Arias, J., & Salehian, B. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00487.2002 · Cited by 416 · see citing works
Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells
Taylor, W. E., Bhasin, S., Artaza, J., Byhower, F., Azam, M., Willard, D. H., Kull, F. C., & González-Cadavid, N. F. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.2.e221 · Cited by 410 · see citing works
Interaction and functional collaboration of p300 and C/EBPβ
Mink, S., Haenig, B., & Klempnauer, K. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6609 · Cited by 344 · see citing works
Lower skeletal muscle mass in male transgenic mice with muscle-specific overexpression of myostatin
Reisz‐Porszasz, S., Bhasin, S., Artaza, J. N., Shen, R., Sinha‐Hikim, I., Hogue, A., Fielder, T. J., & González-Cadavid, N. F. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00107.2003 · Cited by 333 · see citing works
Glucocorticoids and muscle catabolism
Hasselgren, P.-O. (1999) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-199905000-00002 · Cited by 297 · see citing works
Effect of glucocorticoid administration on the rate of muscle protein breakdown in vivo in rats, as measured by urinary excretion of Nτ-methylhistidine
Tomas, F. M., Munro, H. N., & Young, V. R. (1979) · Biochemical Journal · doi:10.1042/bj1780139 · Cited by 293 · see citing works
Muscle Cachexia: Current Concepts of Intracellular Mechanisms and Molecular Regulation
Hasselgren, P.-O., & Fischer, J. E. (2001) · Annals of Surgery · doi:10.1097/00000658-200101000-00003 · Cited by 278 · see citing works
Myostatin Gene Deletion Prevents Glucocorticoid-Induced Muscle Atrophy
Gilson, H., Schakman, O., Combaret, L., Lause, P., Grobet, L., Attaix, D., Ketelslegers, J., & Thissen, J. (2006) · Endocrinology · doi:10.1210/en.2006-0539 · Cited by 278 · see citing works
Self-citation
Dexamethasone Represses Signaling through the Mammalian Target of Rapamycin in Muscle Cells by Enhancing Expression of REDD1
Wang, H., Kubica, N., Ellisen, L. W., Jefferson, L. S., & Kimball, S. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610023200 · Cited by 262 · see citing works
Hormonal regulation of protein degradation and synthesis in skeletal muscle.
Goldberg, A. L., Tischler, M., Demartino, G., & Griffin, G. E. (1980) · PubMed · Cited by 253 · see citing works
Energy-ubiquitin-dependent muscle proteolysis during sepsis in rats is regulated by glucocorticoids.
Tiao, G. M., Fagan, J. M., Roegner, V., Lieberman, M. A., Wang, J. J., Fischer, J. E., & Hasselgren, P. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118421 · Cited by 248 · see citing works
Randomized Placebo-Controlled Trial of Androgen Effects on Muscle and Bone in Men Requiring Long-Term Systemic Glucocorticoid Treatment
Crawford, B. A. L., Liu, P. Y., Kean, M. T., Bleasel, J. F., & Handelsman, D. J. (2003) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2002-021827 · Cited by 235 · see citing works
Characterization of 5′-regulatory region of human myostatin gene: regulation by dexamethasone in vitro
Ma, K., Mallidis, C., Artaza, J., Taylor, W. E., González-Cadavid, N. F., & Bhasin, S. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.281.6.e1128 · Cited by 208 · see citing works
CORTICOSTEROID MYOPATHY: A CLINICAL AND PATHOLOGICAL STUDY
Khaleeli, A. A., Edwards, R. H. T., Gohil, K., McPhail, G., Rennie, M. J., Round, J. M., & Ross, E. J. (1983) · Clinical Endocrinology · doi:10.1111/j.1365-2265.1983.tb03198.x · Cited by 190 · see citing works
Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting
Deval, C., Mordier, S. B., Obled, C., Béchet, D., Combaret, L., Attaix, D., & Ferrara, M. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3600143 · Cited by 184 · see citing works
Modulating skeletal muscle mass by postnatal, muscle‐specific inactivation of the myostatin gene
Grobet, L., Pirottin, D., Farnir, F., Poncelet, D. A., Royo, L. J., Brouwers, B., Christians, E., Desmecht, D. J.-M., Coignoul, F. L., Kahn, R., et al. (2003) · genesis · doi:10.1002/gene.10188 · Cited by 182 · see citing works
Role of the Transcription Factor ATF4 in the Anabolic Actions of Insulin and the Anti-anabolic Actions of Glucocorticoids
Adams, C. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610510200 · Cited by 165 · see citing works
Role of leucine in the regulation of mTOR by amino acids: revelations from structure-activity studies.
Lynch, C. J. (2001) · Journal of NutriLife · doi:10.1093/jn/131.3.861s · Cited by 163 · see citing works
GSK-3β negatively regulates skeletal myotube hypertrophy
Vyas, D. R., Spangenburg, E. E., Abraha, T. W., Childs, T. E., & Booth, F. W. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00049.2002 · Cited by 149 · see citing works
Role of the Insulin-Like Growth Factor I Decline in the Induction of Atrogin-1/MAFbx during Fasting and Diabetes
Dehoux, M., Beneden, R. V., Pasko, N., Lause, P., Verniers, J., Underwood, L. E., Ketelslegers, J., & Thissen, J. (2004) · Endocrinology · doi:10.1210/en.2004-0406 · Cited by 147 · see citing works
Self-citation
Effects of high doses of glucocorticoids on free amino acids, ribosomes and protein turnover in human muscle
Löfberg, E., Gutiérrez, A., Wernerman, J., Anderstam, B., Mitch, W. E., Price, S. R., Bergström, J. P., & Alvestrand, A. (2002) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2002.00993.x · Cited by 142 · see citing works
Increased IGF mRNA in Human Skeletal Muscle after Creatine Supplementation
DELDICQUE, L., LOUIS, M., THEISEN, D., NIELENS, H., DEHOUX, M., THISSEN, J.-P., RENNIE, M. J., & FRANCAUX, M. (2005) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000162690.39830.27 · Cited by 141 · see citing works
Self-citation
The Coactivator p300 Directly Acetylates the Forkhead Transcription Factor Foxo1 and Stimulates Foxo1-Induced Transcription
Perrot, V., & Rechler, M. M. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0292 · Cited by 127 · see citing works
Acute attenuation of translation initiation and protein synthesis by glucocorticoids in skeletal muscle
Shah, O. J., Kimball, S. R., & Jefferson, L. S. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.278.1.e76 · Cited by 127 · see citing works
Recruitment of p300 by C/EBPβ triggers phosphorylation of p300 and modulates coactivator activity
Schwartz, C., Schachtrup, K., Mink, S., Schmolke, M., Budde, B., Wenning, D., & Klempnauer, K.-H. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg076 · Cited by 122 · see citing works
The Orphan Nuclear Receptor, NOR-1, Is a Target of β-Adrenergic Signaling in Skeletal Muscle
Pearen, M. A., Ryall, J. G., Maxwell, M., Ohkura, N., Lynch, G. S., & Muscat, G. E. O. (2006) · Endocrinology · doi:10.1210/en.2006-0447 · Cited by 120 · see citing works
Identification of Androgen Response Elements in the Insulin-Like Growth Factor I Upstream Promoter
Wu, Y., Zhao, W., Zhao, J., Pan, J., Wu, Q., Zhang, Y., Bauman, W. A., & Cardozo, C. P. (2007) · Endocrinology · doi:10.1210/en.2006-1653 · Cited by 117 · see citing works
Glycogen synthase kinase-3 is the predominant insulin-regulated eukaryotic initiation factor 2B kinase in skeletal muscle
Jefferson, L. S., Fabian, J. R., & Kimball, S. R. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(98)00141-1 · Cited by 116 · see citing works
Endogenous expression and localization of myostatin and its relation to myosin heavy chain distribution in C2C12 skeletal muscle cells
Artaza, J. N., Bhasin, S., Mallidis, C., Taylor, W. E., Ma, K., & González-Cadavid, N. F. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10044 · Cited by 115 · see citing works
The deleterious effects of bed rest on human skeletal muscle fibers are exacerbated by hypercortisolemia and ameliorated by dietary supplementation
Fitts, R. H., Romatowski, J. G., Peters, J., Paddon‐Jones, D., Wolfe, R. R., & Ferrando, A. A. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00573.2006 · Cited by 113 · see citing works
Differential regulation of cyclooxygenase-2 (COX-2) mRNA stability by interleukin-1β (IL-1β) and tumor necrosis factor-α (TNF-α) in human in vitro differentiated macrophages
Huang, Z.-F., Massey, J. B., & Via, D. P. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00312-3 · Cited by 110 · see citing works
Nutritional and hormonal factors control the gene expression of FoxOs, the mammalian homologues of DAF-16
Imae, M., Fu, Z., Yoshida, A., Noguchi, T., & Kato, H. (2003) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0300253 · Cited by 110 · see citing works
Inhibition of glycogen synthase kinase-3β activity is sufficient to stimulate myogenic differentiation
van der Velden, J. L. J., LANGEN, R. C. J., KELDERS, M. C. J. M., Wouters, E. F. �., Janssen-Heininger, Y. M. W., & Schols, A. M. W. J. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00068.2005 · Cited by 105 · see citing works
Insulin-like growth factor-I (IGF-I) and especially IGF-I variants are anabolic in dexamethasone-treated rats
Tomas, F. M., Knowles, S. E., Owens, P. C., Chandler, C. S., Francis, G. L., Read, L. C., & Ballard, F. J. (1992) · Biochemical Journal · doi:10.1042/bj2820091 · Cited by 105 · see citing works
Myofibrillar protein synthesis in myostatin-deficient mice.
Welle, S., Bhatt, K., & Pinkert, C. (2006) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.00433.2005 · Cited by 104 · see citing works
USP19 is a ubiquitin-specific protease regulated in rat skeletal muscle during catabolic states
Combaret, L., Adegoke, O. A. J., Bedard, N., Baracos, V. E., Attaix, D., & Wing, S. S. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00281.2004 · Cited by 104 · see citing works
Acute Treatment with Corticosteroids Decreases IGF-1 and IGF-2 Expression in the Rat Diaphragm and Gastrocnemius
Gayan‐Ramirez, G., Vanderhoydonc, F., Verhoeven, G., & Decramer, M. (1999) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.159.1.9803021 · Cited by 102 · see citing works
Skeletal muscle mRNA levels for cathepsin B, but not components of the ubiquitin‒proteasome pathway, are increased in patients with lung cancer referred for thoracotomy
Jagoe, R. T., Redfern, C. P. F., Roberts, R. G., Gibson, G. J., & Goodship, T. H. J. (2002) · Clinical Science · doi:10.1042/cs1020353 · Cited by 102 · see citing works
Corticosteroid treatment and nutritional deprivation cause a different pattern of atrophy in rat diaphragm
Dekhuijzen, P. N. R., Gayan‐Ramirez, G., Bisschop, A., de Bock, V., Dom, R., & Decramer, M. (1995) · Journal of Applied Physiology · doi:10.1152/jappl.1995.78.2.629 · Cited by 96 · see citing works
Insulin-Like Growth Factor-I Gene Transfer by Electroporation Prevents Skeletal Muscle Atrophy in Glucocorticoid-Treated Rats
Schakman, O., Gilson, H., de Coninck, V., Lause, P., Verniers, J., Havaux, X., Ketelslegers, J., & Thissen, J. (2005) · Endocrinology · doi:10.1210/en.2004-1594 · Cited by 95 · see citing works
Self-citation
Corticosteroids and skeletal muscle function in cystic fibrosis
Barry, S. C., & Gallagher, C. G. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00506.2002 · Cited by 89 · see citing works
Branched Chain Amino Acids Activate Messenger Ribonucleic Acid Translation Regulatory Proteins in Human Skeletal Muscle, and Glucocorticoids Blunt This Action1
Liu, Z., Jahn, L. A., Long, W., Fryburg, D. A., Wei, L., & Barrett, E. J. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.86.5.7481 · Cited by 87 · see citing works
C/EBP DNA-binding activity is upregulated by a glucocorticoid-dependent mechanism in septic muscle
Penner, G. C., Gang, G., Sun, X., Wray, C. J., & Hasselgren, P. (2002) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00512.2001 · Cited by 85 · see citing works
Role of IGF-I and IGFBPs in the changes of mass and phenotype induced in rat soleus muscle by clenbuterol
Awede, B. L., Thissen, J., & Lebacq, J. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2002.282.1.e31 · Cited by 78 · see citing works
Self-citation
Among translational effectors, p70S6k is uniquely sensitive to inhibition by glucocorticoids
Shah, O. J., Kimball, S. R., & Jefferson, L. S. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3470389 · Cited by 75 · see citing works
Glucocorticoid effects on insulin- and IGF-I-regulated muscle protein metabolism during aging
Dardevet, D. P., Sornet, C., Savary‐Auzeloux, I., Debras, E., Patureau-Mirand, P., & Grizard, J. (1998) · Journal of Endocrinology · doi:10.1677/joe.0.1560083 · Cited by 75 · see citing works
Role of Protein Synthesis in the Inhibitory Action of Adrenal Steroid Hormones on Amino Acid Transport by Muscle1
Kostyo, J. L., & Redmond, A. F. (1966) · Endocrinology · doi:10.1210/endo-79-3-531 · Cited by 73 · see citing works
Modulations of Muscle Protein Metabolism by Branched-Chain AminoAcids in Normal and Muscle-Atrophying Rats,
Kobayashi, H., Kato, H., Hirabayashi, Y., Murakami, H., & Suzuki, H. (2006) · Journal of Nutrition · doi:10.1093/jn/136.1.234s · Cited by 70 · see citing works
The Effect of Glutamine on Prevention of Glucocorticoid-Induced Skeletal Muscle Atrophy Is Associated with Myostatin Suppression
Salehian, B., Mahabadi, V., Bilas, J., Taylor, W. E., & Ma, K. (2006) · Metabolism · doi:10.1016/j.metabol.2006.05.009 · Cited by 69 · see citing works
Regulation of insulin-like growth factor-I in skeletal muscle and muscle cells.
Frost, R. A., & Lang, C. H. (2003) · PubMed · Cited by 67 · see citing works
Elimination of Myostatin Does Not Combat Muscular Dystrophy in dy Mice but Increases Postnatal Lethality
Li, Z., Shelton, G. D., & Engvall, E. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62271-7 · Cited by 66 · see citing works
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 64 · see citing works
Clenbuterol antagonizes glucocorticoid‐induced atrophy and fibre type transformation in mice
Pellegrino, M. A., D’Antona, G., Bortolotto, S. K., Boschi, F., Pastoris, O., Bottinelli, R., Polla, B., & Reggiani, C. (2003) · Experimental Physiology · doi:10.1113/expphysiol.2003.002609 · Cited by 63 · see citing works
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 59 · see citing works
Glucocorticoid inhibition of C2C12 proliferation rate and differentiation capacity in relation to mRNA levels of the MRF gene family
PAS, M. F. W. T., de Jong, P. R., & Verburg, F. J. (2000) · Molecular Biology Reports · doi:10.1023/a:1007120921064 · Cited by 58 · see citing works
The effect of interleukin-1α and the glucocorticoid receptor blocker RU 38486 on total and myofibrillar protein breakdown in skeletal muscle
Zamir, O., Hasselgren, P.-O., von Allmen, D., & Fischer, J. E. (1991) · Journal of Surgical Research · doi:10.1016/0022-4804(91)90045-n · Cited by 57 · see citing works
Insulin-like growth factor I prevents corticosteroid-induced diaphragm muscle atrophy in emphysematous hamsters
Fournier, M., Huang, Z.-S., Li, H., Da, X., Cercek, B., & Lewis, M. I. (2003) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00177.2002 · Cited by 53 · see citing works
Microarray analysis of the temporal response of skeletal muscle to methylprednisolone: comparative analysis of two dosing regimens
Almon, R. R., DuBois, D. C., Yao, Z., Hoffman, E. P., Ghimbovschi, S. D., & Jusko, W. J. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00242.2006 · Cited by 52 · see citing works
Glucocorticoids modulate amino acid-induced translation initiation in human skeletal muscle
Liu, Z., Li, G., Kimball, S. R., Jahn, L. A., & Barrett, E. J. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00457.2003 · Cited by 51 · see citing works
Protein Breakdown in Muscle from Burned Rats Is Blocked by Insulin-Like Growth Factor I and Glycogen Synthase Kinase-3β Inhibitors
Fang, C., Li, B.-G., James, J. H., King, J.-K., Evenson, A. R., Warden, G. D., & Hasselgren, P.-O. (2005) · Endocrinology · doi:10.1210/en.2004-0869 · Cited by 51 · see citing works
Dexamethasone-induced protein degradation in cultured myotubes is p300/HAT dependent
Yang, H., Wei, W., Menconi, M. J., & Hasselgren, P.-O. (2006) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00230.2006 · Cited by 51 · see citing works
Creatine supplementation attenuates corticosteroid-induced muscle wasting and impairment of exercise performance in rats
Menezes, L. G., Sobreira, C., Neder, L., Rodrigues, A. L., & Martínez, J. A. B. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01188.2005 · Cited by 50 · see citing works
Glutamine prevents downregulation of myosin heavy chain synthesis and muscle atrophy from glucocorticoids
Hickson, R. C., Czerwinski, S. M., & Wegrzyn, L. E. (1995) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1995.268.4.e730 · Cited by 50 · see citing works
Dexamethasone upregulates the expression of the nuclear cofactor p300 and its interaction with C/EBPβ in cultured myotubes
Yang, H., Menconi, M. J., Wei, W., Petkova, V., & Hasselgren, P. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20371 · Cited by 49 · see citing works
Branched Chain Amino Acids Activate Messenger Ribonucleic Acid Translation Regulatory Proteins in Human Skeletal Muscle, and Glucocorticoids Blunt This Action
Liu, Z. (2001) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.86.5.2136 · Cited by 46 · see citing works
Among translational effectors, p70S6k is uniquely sensitive to inhibition by glucocorticoids
Shah, O. J., Kimball, S. R., & Jefferson, L. S. (2000) · Biochemical Journal · doi:10.1042/bj3470389 · Cited by 45 · see citing works
Effect of clenbuterol on skeletal muscle atrophy in mice induced by the glucocorticoid dexamethasone
Agbenyega, E. T., & Wareham, A. C. (1992) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(92)90026-m · Cited by 43 · see citing works
Myogenic differentiation induces taurine transporter in association with taurine-mediated cytoprotection in skeletal muscles
Uozumi, Y., Ito, T., Hoshino, Y., Mohri, T., Maeda, M., Takahashi, K., Fujio, Y., & Azuma, J. (2006) · Biochemical Journal · doi:10.1042/bj20051303 · Cited by 42 · see citing works
Glucocorticoid excess induces a prolonged leucine resistance on muscle protein synthesis in old rats
Rieu, I., Sornet, C., Grizard, J., & Dardevet, D. P. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.06.005 · Cited by 41 · see citing works
Skeletal muscle mRNA levels for cathepsin B, but not components of the ubiquitin‒proteasome pathway, are increased in patients with lung cancer referred for thoracotomy
Jagoe, R. T., Redfern, C. P. F., Roberts, R. G., et al. (2002) · Clinical Science · doi:10.1042/cs20010270 · Cited by 41 · see citing works
Insulin-Like Growth Factor-I Blocks Dexamethasone-Induced Protein Degradation in Cultured Myotubes by Inhibiting Multiple Proteolytic Pathways
Li, B.-G., Hasselgren, P.-O., Fang, C., & Warden, G. D. (2004) · Journal of Burn Care & Rehabilitation · doi:10.1097/01.bcr.0000105100.44745.36 · Cited by 36 · see citing works
Dietary supplementation with creatine monohydrate prevents corticosteroid-induced attenuation of growth in young rats
Roy, B. D., Bourgeois, J. M., Mahoney, D. J., & Tarnopolsky, M. A. (2002) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y02-129 · Cited by 34 · see citing works
Alanyl-glutamine prevents muscle atrophy and glutamine synthetase induction by glucocorticoids
Hickson, R. C., Wegrzyn, L. E., Osborne, D. F., & Karl, I. E. (1996) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1996.271.5.r1165 · Cited by 32 · see citing works
Assessing acetylation of NF-κB
Chen, L., & Greene, W. C. (2005) · Methods · doi:10.1016/j.ymeth.2005.03.011 · Cited by 31 · see citing works
Respiratory Muscle Strength in Cushing's Syndrome
MILLS, G. H., Kyroussis, D., JENKINS, P., Hamnegård, C., Polkey, M. I., Wass, J. A. H., BESSER, G. M., Moxham, J., & Green, M. (1999) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.160.5.9810028 · Cited by 30 · see citing works
Prednisolone-Induced Muscle Dysfunction Is Caused More by Atrophy than by Altered Acetylcholine Receptor Expression
Shin, Y. S., Fink, H., Khiroya, R., Ibebunjo, C., & Martyn, J. A. (2000) · Anesthesia & Analgesia · doi:10.1097/00000539-200008000-00017 · Cited by 30 · see citing works
Anabolic steroids in part reverse glucocorticoid-induced alterations in rat diaphragm
van Balkom, R. H. H., Dekhuijzen, P. N. R., Folgering, H. T. M., Veerkamp, J. H., van Moerkerk, H. T. B., Fransen, J. A. M., & van Herwaarden, C. (1998) · Journal of Applied Physiology · doi:10.1152/jappl.1998.84.5.1492 · Cited by 28 · see citing works
Necrotizing myopathy induced by overexpression of interferon-? in transgenic mice
Shelton, G. D., Calcutt, N. A., Garrett, R. S., Gu, D., Sarvetnick, N., Campana, W. M., & Powell, H. C. (1999) · Muscle & Nerve · doi:10.1002/(sici)1097-4598(199902)22:2 · Cited by 24 · see citing works
Protective Effect of Glutamine from Glucocorticoid-Induced Muscle Atrophy Occurs without Alterations in Circulating Insulin-Like Growth Factor (IGF)-I and IGF-Binding Protein Levels
Hickson, R. C., OEHLER, D. T., Byerly, R., & Unterman, T. G. (1997) · Experimental Biology and Medicine · doi:10.3181/00379727-216-44157 · Cited by 21 · see citing works
Effect of the antiglucocorticoid RU38486 on protein metabolism in unweighted soleus muscle
Tischler, M. E. (1994) · Metabolism · doi:10.1016/0026-0495(94)90044-2 · Cited by 18 · see citing works
The anti-catabolic efficacy of insulin-like growth factor-I is enhanced by its early administration to rats receiving dexamethasone
Tomas, F. (1998) · Journal of Endocrinology · doi:10.1677/joe.0.1570089 · Cited by 17 · see citing works
Effect of the Beta-Agonist Clenbuterol on Dexamethasone-Induced Diaphragm Dysfunction in Rabbits
Jiang, T. X., Cairns, A., ROAD, J. D., & Wilcox, P. (1996) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.154.6.8970370 · Cited by 16 · see citing works
Myogenic Induction of Taurine Transporter Prevents Dexamethasone-Induced Muscle Atrophy
Uozumi, Y., Ito, T., Takahashi, K., Matsuda, T., Mohri, T., Kimura, Y., Fujio, Y., & Azuma, J. (2006) · Springer eBooks · doi:10.1007/978-0-387-33504-9_29 · Cited by 13 · see citing works
Creatine intake attenuates corticosteroid-induced impairment of voluntary running in hamsters
Campos, A. R., Serafini, L. N., Sobreira, C. F. D. R., Menezes, L. G., & Martínez, J. A. B. (2006) · Applied Physiology Nutrition and Metabolism · doi:10.1139/h06-025 · Cited by 10 · see citing works
Prednisolone-Induced Muscle Dysfunction Is Caused More by Atrophy than by Altered Acetylcholine Receptor Expression
Shin, Y. S., Fink, H., Khiroya, R. H., et al. (2000) · Anesthesia & Analgesia · doi:10.1213/00000539-200008000-00017 · Cited by 10 · see citing works

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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
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Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284 · see citing works
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Kalyani, R. R., Corriere, M., & Ferrucci, L. (2014) · The Lancet Diabetes & Endocrinology · doi:10.1016/s2213-8587(14)70034-8 · Cited by 1,102 · see citing works
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Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089 · see citing works
Regulation of glucose homeostasis by glucocorticoids
Kuo, T., McQueen, A., Chen, T.-C., & Wang, J.-C. (2015) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4939-2895-8_5 · Cited by 723 · see citing works
Widespread negative response elements mediate direct repression by agonist-liganded glucocorticoid receptor
Surjit, M., Ganti, K. P., Mukherji, A., Ye, T., Hua, G., Metzger, D., Li, M., & Chambon, P. (2011) · Cell · doi:10.1016/j.cell.2011.03.027 · Cited by 551 · see citing works
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Shimizu, N., Yoshikawa, N., Ito, N., Maruyama, T., Suzuki, Y., Takeda, S.-I., Nakae, J., Tagata, Y., Nishitani, S., Takehana, K., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.01.001 · Cited by 498 · see citing works
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Van Raalte, D. H., Ouwens, D. M., & Diamant, M. (2009) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2008.02067.x · Cited by 439 · see citing works
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So, A. Y.-L., Bernal, T. U., Pillsbury, M. L., Yamamoto, K. R., & Feldman, B. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909733106 · Cited by 431 · see citing works
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Buford, T. W., Anton, S. D., Judge, A. R., Marzetti, E., Wohlgemuth, S. E., Carter, C. S., Leeuwenburgh, C., Pahor, M., & Manini, T. M. (2010) · Ageing Research Reviews · doi:10.1016/j.arr.2010.04.004 · Cited by 295 · see citing works
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Beck, I. M. E., Vanden Berghe, W., Vermeulen, L., Yamamoto, K. R., Haegeman, G., & De Bosscher, K. (2009) · Endocrine Reviews · doi:10.1210/er.2009-0013 · Cited by 298 · see citing works
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Low-dose glucocorticoid treatment affects multiple aspects of intermediary metabolism in healthy humans: a randomised controlled trial
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“Moreover, GCs directly activated muscle ring finger-1 and atrogin-1, proteins involved in skeletal muscle proteolysis [43].”
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Myostatin Gene Deletion Prevents Glucocorticoid-Induced Muscle Atrophy
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Self-citation

Authors: Schakman, O., Gilson, H., & Thissen, J. P.
Affiliations: UCLouvain (BE)
ORCID: Schakman, O
Thissen, J P
Venue: Journal of Endocrinology
Publisher: Bioscientifica
Published: 2008-01-31
Volume: 197
Issue: 1
Pages: 1-10
ISSN: 0022-0795 (ISSN-L)
1479-6805
DOI: 10.1677/joe-07-0606
OpenAlex: W2111274663
Cited by: 521
References: 110
Citations by year: 2026: 30 · 2025: 26 · 2024: 30 · 2023: 39 · 2022: 36 · 2021: 22 · 2020: 30 · 2019: 33 · 2018: 21 · 2017: 23 · 2016: 21 · 2015: 29 · 2014: 23 · 2013: 41 · 2012: 37
FWCI: 1.96
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Endocrinology (publishedVersion)
PubMed (publishedVersion)
Digital Access to Libraries (Université catholique de Louvain (UCL), l'Université de Namur (UNamur) and the Université Saint-Louis (USL-B)) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
Keywords: glucocorticoid-induced myopathy, muscle atrophy, ubiquitin-proteasome system, atrogenes, atrogin-1, MuRF1, muscle protein synthesis, insulin-like growth factor I, myostatin, FOXO, PI3K/Akt signaling, skeletal muscle catabolism, treatment options
MeSH terms: Forkhead Box Protein O1, Glycogen Synthase Kinase 3 beta, Animals, Glucocorticoids, Humans, Insulin-Like Growth Factor I, Muscular Atrophy, Protein Kinases, Signal Transduction, CCAAT-Enhancer-Binding Protein-beta, Glycogen Synthase Kinase 3, Activating Transcription Factor 4, Forkhead Transcription Factors, Myostatin, TOR Serine-Threonine Kinases

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Mechanisms of glucocorticoid-induced myopathy

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