Differential role of insulin/IGF-1 receptor signaling in muscle growth and glucose homeostasis
Open accessAbstract
Insulin and insulin-like growth factor 1 (IGF-1) are major regulators of muscle protein and glucose homeostasis. To determine how these pathways interact, we generated mice with muscle-specific knockout of IGF-1 receptor (IGF1R) and insulin receptor (IR). These MIGIRKO mice showed >60% decrease in muscle mass. Despite a complete lack of insulin/IGF-1 signaling in muscle, MIGIRKO mice displayed normal glucose and insulin tolerance. Indeed, MIGIRKO mice showed fasting hypoglycemia and increased basal glucose uptake. This was secondary to decreased TBC1D1 resulting in increased Glut4 and Glut1 membrane localization. Interestingly, overexpression of a dominant-negative IGF1R in muscle induced glucose intolerance in MIGIRKO animals. Thus, loss of insulin/IGF-1 signaling impairs muscle growth, but not whole-body glucose tolerance due to increased membrane localization of glucose transporters. Nonetheless, presence of a dominant-negative receptor, even in the absence of functional IR/IGF1R, induces glucose intolerance, indicating that interactions between these receptors and other proteins in muscle can impair glucose homeostasis.
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The IGF-IR/IR knockout mice showed decreased skeletal muscle mass.
“The IGF-IR/IR knockout mice showed decreased skeletal muscle mass [50].”
From Sarcopenic obesity, insulin resistance, and their implications in cardiovascular and metabolic consequences (2020) · cites this paper as [50]
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“We previously published that spontaneous activity of MIGIRKO was decreased 30% in the dark cycle (19) and MIGIRKO mice were unable to perform spontaneous wheel running (20); thus, mitochondrial defects in MIGIRKO may be partly due to inactivity.”
BackgroundMethodInfluentialSelf-citationDifferential roles of FOXO transcription factors on insulin action in brown and white adipose tissue
Homan, E. P., Brandão, B. B., Softic, S., Ouaamari, A. E., O'Neill, B. T., Kulkarni, R. N., Kim, J. K., & Kahn, C. R. (2021) · Journal of Clinical Investigation · doi:10.1172/jci143328 · Cited by 51 · see citing works
“Similarly, mice lacking both IR and IGF1R in muscle or with insulin-deficient diabetes display a marked reduction in muscle mass because of increased proteasomal and autophagy-mediated protein degradation (12).”
BackgroundSelf-citationEndothelial IGF-1 Receptor Signalling in Diabetes and Insulin Resistance
Cubbon, R. M., Kearney, M. T., & Wheatcroft, S. B. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.11.009 · Cited by 51 · see citing works
“Equally, recent data from Ronald Kahn's laboratory also suggest that the nonligand-bound IGF-1R is not functionally inert, since total IGF-1R deletion in skeletal muscle is associated with a more favourable metabolic phenotype than when a dominant negative IGF-1R is re-expressed [60].”
BackgroundConnecting the Dots Between the Gut–IGF-1–Prostate Axis: A Role of IGF-1 in Prostate Carcinogenesis
Matsushita, M., Fujita, K., Hatano, K., Velasco, M. A. D., Uemura, H., & Nonomura, N. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.852382 · Cited by 44 · see citing works
“Muscle-specific IGF1R knockout mice display disrupted muscle fiber formation and reduced muscle weight early in development (22).”
BackgroundInsulin‐Like Growth Factor I Regulation and Its Actions in Skeletal Muscle
Vassilakos, G., & Barton, E. R. (2018) · Comprehensive physiology · doi:10.1002/cphy.c180010 · Cited by 47 · see citing works
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Differential Effects of Hormones on Cellular Metabolism in Keratoconus In Vitro
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Mice with gene alterations in the GH and IGF family
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“, in 2015, was generated via the use of a Cre/LoxP system using a skeletal muscle actin promoter/enhancer [281].”
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“In skeletal muscle, IGF1 is critical for muscle development [72] but is dispensable in the control of glucose metabolism in mature myocyte [73].”
BackgroundLoss of FoxOs in muscle increases strength and mitochondrial function during aging
Penniman, C. M., Bhardwaj, G., Nowers, C. J., Brown, C. U., Junck, T. L., Boyer, C. K., Jena, J., Fuqua, J. D., Lira, V. A., & O'Neill, B. T. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13124 · Cited by 39 · see citing works
“5 mg/ mL nitro blue tetrazolium for 15 min at 37°C and quantified as previously described.(29) Briefly, 300–900 plantaris fibres were manually counted and normalized to total number of fibres in the field of interest.”
MethodSelf-citationMohammadinejad, F., Mohammadabadi, M., Roudbari, Z., & Sadkowski, T. (2022) · Animals · doi:10.3390/ani12243471 · Cited by 38 · see citing works
Viral Hormones: Expanding Dimensions in Endocrinology
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Self-citationRabGAPs in skeletal muscle function and exercise
Espelage, L., Al‐Hasani, H., & Chadt, A. (2019) · Journal of Molecular Endocrinology · doi:10.1530/jme-19-0143 · Cited by 33 · see citing works
“Ablation of IR and IGF1R specifically in murine skeletal muscle (MIGIRKO) led to a >60% decrease in muscle mass, severe muscle atrophy with spinal deformities and obvious kyphosis (O’Neill et al. 2015).”
BackgroundVav2 catalysis-dependent pathways contribute to skeletal muscle growth and metabolic homeostasis
Rodríguez‐Fdez, S., Lorenzo‐Martín, L. F., Fernández‐Pisonero, I., Porteiro, B., Veyrat‐Durebex, C., Beiroa, D., Al–Massadi, O., Abad, A., Diéguez, C., Coppari, R., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19489-z · Cited by 32 · see citing works
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“In brain homeostasis and glucose control, IGF-1 plays a vital role [75].”
BackgroundMetabolic Complications of Acromegaly
Mercado, M., & Ramírez‐Rentería, C. (2018) · Frontiers of hormone research · doi:10.1159/000486001 · Cited by 33 · see citing works
The regulation of skeletal muscle fiber-type composition by betaine is associated with NFATc1/MyoD
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“Skeletal muscle is an important and complex organ composed of many different cell types, and it accounts for ~ 40% of the body weight of lean men and women [1, 2].”
BackgroundActions and interactions of IGF-I and MMPs during muscle regeneration
Kok, H. J., & Barton, E. R. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.04.018 · Cited by 30 · see citing works
Role of p110a subunit of PI3-kinase in skeletal muscle mitochondrial homeostasis and metabolism
Li, M. E., Lauritzen, H. P. M. M., O'Neill, B. T., Wang, C., Cai, W., Brandão, B. B., Sakaguchi, M., Tao, R., Hirshman, M. F., Softic, S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11265-y · Cited by 29 · see citing works
Self-citationRole of the HSP70 Co-Chaperone SIL1 in Health and Disease
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“A similar compensation has been observed in mice with a muscle-specific dual knockout of IR and IGF1R (MIGIRKO), which display basal activation of PI3K-AKT-mTOR signaling and increased surface expression of the GLUT1 and GLUT4 glucose transporters [89].”
BackgroundOkuyama, T., Kyohara, M., Terauchi, Y., & Shirakawa, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136817 · Cited by 30 · see citing works
“[25] also created the muscle-specific IR and IGF-IR double knockout mice using ACTA1 promoter in transgenic mice, which exhibited severe muscle atrophy but normal glucose tolerance.”
BackgroundPenniman, C. M., Beltran, P. A. S., Bhardwaj, G., Junck, T. L., Jena, J., Poro, K., Hirshman, M. F., Goodyear, L. J., & O'Neill, B. T. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.10.001 · Cited by 27 · see citing works
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Insulin and IGF-1 elicit robust transcriptional regulation to modulate autophagy in astrocytes
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“Loss of IR and IGF1R in skeletal muscle leads to uncontrolled autophagy and proteolysis, contributing to severe muscle atrophy in these mice [69].”
BackgroundInsulin-Like Growth Factor 1 in the Cardiovascular System
Aguirre, G. A., González-Guerra, J. L., Espinosa, L., & Castilla‐Cortázar, I. (2018) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2017_8 · Cited by 25 · see citing works
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Characterization of Skeletal Muscle Endocrine Control in an In Vitro Model of Myogenesis
Romagnoli, C., Zonefrati, R., Sharma, P., Innocenti, M., Cianferotti, L., & Brandi, M. L. (2020) · Calcified Tissue International · doi:10.1007/s00223-020-00678-3 · Cited by 22 · see citing works
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Insulin Resistance and the IGF-I-Cortical Bone Relationship in Children Ages 9 to 13 Years
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“As implied in the current study, lean body mass is a facilitator of the relationship between IGF-I and bone and is the primary site of insulin-mediated glucose uptake,((46)) thus being most prone to fluctuations in insulin sensitivity.”
BackgroundFrançois, J., Aïd, S., Chaker, Z., Lacube, P., Xu, J., Fayad, R., Côté, F., Even, P. C., & Holzenberger, M. (2017) · Endocrinology · doi:10.1210/en.2017-00261 · Cited by 22 · see citing works
Leucine-973 is a crucial residue differentiating insulin and IGF-1 receptor signaling
Nagao, H., Cai, W., Brandão, B. B., Albrechtsen, N. J. W., Steger, M., Gattu, A. K., Pan, H., Dreyfuss, J. M., Wunderlich, F. T., Mann, M., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci161472 · Cited by 21 · see citing works
“For example, muscle mass shows only a small reduction by muscle-specific single deletion of either IR or IGF1R, but is markedly decreased by muscle-specific deletion of both IR and IGF1R (47).”
Self-citationReduced insulin signaling in neurons induces sex-specific health benefits
Baghdadi, M., Nespital, T., Mesaros, A., Buschbaum, S., Withers, D. J., Grönke, S., & Partridge, L. (2023) · Science Advances · doi:10.1126/sciadv.ade8137 · Cited by 22 · see citing works
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Targeting IGF1R pathway in cancer with microRNAs: How close are we?
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“IGF1R interaction and cross talk with other growth factor receptors are studied to have a major role in cells; interactions between IR and IGF1R in muscle were found to have significance in glucose homeostasis in mice models [5].”
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“org 12 homeostasis (33), tumor cell survival and the formation of metastasis.”
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CDR1as/miRNAs-related regulatory mechanisms in muscle development and diseases
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“Knockout of the IGF1R and IR results in a 60% reduction in muscle mass in mice [30].”
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“Insulin-like growth factor 1 receptor (IGF1R) is an important component of the insulin-like growth factor (IGF) system that is widely expressed in animal muscles and is a key gene affecting growth and development [50].”
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“Indeed, these MIGIRKOmice not only display normal whole-body glucose tolerance when fed with HFD but also have fasting hypoglycemia reflecting increased basal glucose uptake (9).”
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Role of PDK1 in skeletal muscle hypertrophy induced by mechanical load
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“Other stimuli, such as high glucose and fatty acids, can also cause muscle cells to produce lipids to varying degrees [40].”
BackgroundPost-natal muscle growth and protein turnover: a narrative review of current understanding
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“Additionally, as already described, the action of insulin in the signaling pathway of IGF-1 to control glucose metabolism leading to lower values of blood glucose, which would result in lower values of HOMA-IR [34].”
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“40 Although our study did not monitor blood glucose in mice injected with rmIGF-1, no significant changes in body weight or hypoglycemic symptoms were observed during the period of the rmIGF-1 administration, which implied that the doses we used were relatively safe.”
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SINE Insertion in the Intron of Pig GHR May Decrease Its Expression by Acting as a Repressor
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“IGF1R is a tyrosine kinase receptor for IGF1 and regulates cell metabolism, growth, and differentiation in various mammalian tissues [9], and can be activated by IGF1.”
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- Authors
- O’Neill, B. T., Lauritzen, H. P. M. M., Hirshman, M. F., Smyth, G., Goodyear, L. J., & Kahn, C. R.
- Affiliations
- Joslin Diabetes Center (US)
- Corresponding author
- Kahn, C. Ronald
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2015-05
- Volume
- 11
- Issue
- 8
- Pages
- 1220-1235
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC4449334
- OpenAlex
- W1578864848
- Cited by
- 171
- References
- 45
- Citations by year
- 2026: 12 · 2025: 14 · 2024: 17 · 2023: 14 · 2022: 20 · 2021: 21 · 2020: 17 · 2019: 24 · 2018: 16 · 2017: 9 · 2016: 5 · 2015: 2
- FWCI
- 3.77
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Mayo Clinic
- Joslin Diabetes Center
- Georgia Clinical and Translational Science Alliance
- National Institutes of Health (UL1TR000135)
- Diabetes Research Center
- National Institute of Diabetes and Digestive and Kidney Diseases (R37DK031036, R01DK031036, R01DK033201, U24DK100469, K08DK100543, T32DK007260, P30DK036836)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR042238)
- National Center for Advancing Translational Sciences
- Common Fund
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Growth Hormone and Insulin-like Growth Factors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- insulin receptor, IGF-1 receptor, muscle growth, glucose homeostasis, glucose tolerance, impaired glucose tolerance, hypoglycemia, glucose transporters, GLUT4, GLUT1, TBC1D1, dominant negative receptor, muscle-specific knockout, insulin/IGF-1 signaling
- MeSH terms
- Animals, Female, Glucose, Homeostasis, Male, Muscle Proteins, Phosphorylation, Receptor, Insulin, Signal Transduction, Receptor, IGF Type 1, Mice, Knockout, Muscle, Skeletal, Mice
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