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The Regulation of Skeletal Muscle Protein Turnover during the Progression of Cancer Cachexia in the ApcMin/+ Mouse
Open accessAbstract
Muscle wasting that occurs with cancer cachexia is caused by an imbalance in the rates of muscle protein synthesis and degradation. The Apc(Min/+) mouse is a model of colorectal cancer that develops cachexia that is dependent on circulating IL-6. However, the IL-6 regulation of muscle protein turnover during the initiation and progression of cachexia in the Apc(Min/+) mouse is not known. Cachexia progression was studied in Apc(Min/+) mice that were either weight stable (WS) or had initial (≤5%), intermediate (6-19%), or extreme (≥20%) body weight loss. The initiation of cachexia reduced %MPS 19% and a further ∼50% with additional weight loss. Muscle IGF-1 mRNA expression and mTOR targets were suppressed with the progression of body weight loss, while muscle AMPK phosphorylation (Thr 172), AMPK activity, and raptor phosphorylation (Ser 792) were not increased with the initiation of weight loss, but were induced as cachexia progressed. ATP dependent protein degradation increased during the initiation and progression of cachexia. However, ATP independent protein degradation was not increased until cachexia had progressed beyond the initial phase. IL-6 receptor antibody administration prevented body weight loss and suppressed muscle protein degradation, without any effect on muscle %MPS or IGF-1 associated signaling. In summary, the %MPS reduction during the initiation of cachexia is associated with IGF-1/mTOR signaling repression, while muscle AMPK activation and activation of ATP independent protein degradation occur later in the progression of cachexia. IL-6 receptor antibody treatment blocked cachexia progression through the suppression of muscle protein degradation, while not rescuing the suppression of muscle protein synthesis. Attenuation of IL-6 signaling was effective in blocking the progression of cachexia, but not sufficient to reverse the process.
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“The link between IL-6/STAT3 signaling and muscle and adipose tissue wasting is well established in mouse models of cachexia (White et al., 2011; Silva et al., 2015) and has been reinforced preliminarily in clinical studies.”
From Targeting Janus Kinases and Signal Transducer and Activator of Transcription 3 To Treat Inflammation, Fibrosis, and Cancer: Rationale, Progress, and Caution (2020) · cites this paper as White et al., 2011
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Self-citationIL-6 signaling blockade increases inflammation but does not affect muscle function in the mdx mouse
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BackgroundInfluentialOvarian function's role during cancer cachexia progression in the female mouse.
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MethodSelf-citationMapping transition potential with stakeholder- and policy-driven scenarios in Rotterdam City
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Exercise Counteracts the Deleterious Effects of Cancer Cachexia
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Self-citationMaster Regulators of Muscle Atrophy: Role of Costamere Components
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IL-17A contributes to skeletal muscle atrophy in lung cancer-induced cachexia via JAK2/STAT3 pathway
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“Inhibition of IL-6, IL-6 receptor, or STAT3 all reduce cachexia in experimental systems (Strassmann et al., 1992; Oldenburg et al., 1993; White et al., 2011; Silva et al., 2015).”
BackgroundRosiglitazone reduces body wasting and improves survival in a rat model of cancer cachexia.
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“Indeed, altered lysosomal function has also been reported in several myopathies (47), including muscle wasting and cachexia in cancer patients (49) and in pre-clinical models (26–28).”
BackgroundSystemic IL-6 regulation of eccentric contraction-induced muscle protein synthesis
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Self-citationExploiting provisions of land economic productivity without degrading its natural capital
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Self-citationPhytotherapy for Cachexia: Where Do We Stand?
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Soil is brown gold in the Emilia-Romagna region, Italy
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Consequences of Late-Stage Non–Small-Cell Lung Cancer Cachexia on Muscle Metabolic Processes
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Decreased miR-497-5p Suppresses IL-6 Induced Atrophy in Muscle Cells
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Self-citationPhysiological characterization of a mouse model of cachexia in colorectal liver metastases.
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“Each of these changes has been reported in animal models of cachexia in nonmetastatic cancer (6, 24, 38) and suggest that the loss of muscle mass in MoCR mice may be due to both decreased signaling of the pathways regulating protein synthesis and increased signaling of the pathways regulating protein degradation.”
BackgroundA novel orthotopic mouse model replicates human lung cancer cachexia
van de Worp, W., Theys, J., González, A. S., van der Heyden, B., Verhaegen, F., Hauser, D., Caiment, F., Smeets, H. J. M., Schols, A., van Helvoort, A., et al. (2023) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.13222 · Cited by 17
“From experimental models of cancer cachexia, there is abundant evidence for increased protein degradation and decreased protein synthesis.(7,11,21,35) Compared with these results from animal models, evidence from human patients is rather inconclusive.”
Non-coding RNAs as Putative Biomarkers of Cancer-Associated Cachexia
Donzelli, S., Farneti, A., Marucci, L., Ganci, F., Sacconi, A., Strano, S., Sanguineti, G., & Blandino, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00257 · Cited by 17
“Different studies in animal models and cancer patients demonstrated that high levels of interleukin 6 (IL-6) correlate with muscle wasting, inhibition of protein synthesis, promotion of protein degradation and autophagy in myotubes (White et al., 2011; Pettersen et al., 2017).”
ResultEffect of Ninjin’yoeito on the Loss of Skeletal Muscle Function in Cancer-Bearing Mice
Ohsawa, M., Maruoka, J., Inami, C., Iwaki, A., Murakami, T., & Ishikura, K. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01400 · Cited by 19
“The muscle protein synthesis is suppressed under cachexia in rodents (White et al., 2011).”
BackgroundKey Questions and Recent Research Advances on Harmful Algal Blooms in Stratified Systems
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Ligand-induced rapid skeletal muscle atrophy in HSA-Fv2E-PERK transgenic mice
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Targeting cancer via ribosome biogenesis: the cachexia perspective
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Exercise—A Panacea of Metabolic Dysregulation in Cancer: Physiological and Molecular Insights
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High-Frequency Stimulation on Skeletal Muscle Maintenance in Female Cachectic Mice
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Self-citationPARP-1 and PARP-2 activity in cancer-induced cachexia: potential therapeutic implications
Barreiro, E., & Gea, J. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0158 · Cited by 12
Wheel running improves fasting‐induced AMPK signaling in skeletal muscle from tumor‐bearing mice
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“…degradation is widely studied (Hardee et al., 2017; White et al., 2011; White, Puppa, Gao, et al., 2013), there has been a focus on the classical FOXO3a control of E3 ligases, Atrogin- 1, and MuRF- 1, driven by inflammatory signaling (Blackwell et al., 2018; Reed et al., 2012; White et al., 2011).”
BackgroundInfluentialSelf-citationColardo, M., Martella, N., Varone, M., Pensabene, D., Caretti, G., Bianchini, G., Aramini, A., & Segatto, M. (2025) · Acta Physiologica · doi:10.1111/apha.70067 · Cited by 13
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Samant, V., & Prabhu, A. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.123225 · Cited by 15
Hekmatikar, A. H. A., Nelson, A. R., & Petersen, A. C. (2023) · BMC Cancer · doi:10.1186/s12885-023-11391-3 · Cited by 13
“Other studies have suggested that increased IL-6 in CC may lead to suppression of IGF-1 and inhibition of AMPK activation [50, 53] (Table 1).”
BackgroundOutlier detection in networks with missing links
Gaucher, S., Klopp, O., & Robin, G. (2020) · Computational Statistics & Data Analysis · doi:10.1016/j.csda.2021.107308 · Cited by 13
Brainstem prolactin-releasing peptide contributes to cancer anorexia-cachexia syndrome in rats
Batista, K. N. I., Schraner, M., & Riediger, T. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108289 · Cited by 12
“mTOR signalling in cancer cachexia (White et al., 2011; Puppa et al., 2014; Chen et al., 2016), other studies support the idea that mTOR inhibition counteracts cachexia by modulating mTOR-dependent autophagy (Pigna et al.”
Lima, M., Sato, S., Enos, R. T., Baynes, J., & Carson, J. (2013) · Journal of applied physiology · doi:10.1152/japplphysiol.01141.2012 · Cited by 13
Self-citationCancer Cachexia: Underlying Mechanisms and Potential Therapeutic Interventions
Directo, D. J., & Lee, S.-R. (2023) · Metabolites · doi:10.3390/metabo13091024 · Cited by 16
Sex differences in skeletal muscle alterations in a model of colorectal cancer
Greenman, A., Albrecht, D. M., Halberg, R. B., & Diffee, G. (2020) · Physiological Reports · doi:10.14814/phy2.14391 · Cited by 12
“In addition, ApcMin/+mice are often categorized by the amount of body weight lost (White et al., 2011), better representing the progressive nature of the syndrome (Fearon et al.”
BackgroundAmano, T., & Toichi, M. (2016) · Scientific Reports · doi:10.1038/srep34610 · Cited by 15
Re-Thinking the Role of Compensation in Urban Land Acquisition: Empirical Evidence from South Asia
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MMP12 knockout prevents weight and muscle loss in tumor-bearing mice
Jiang, L., Yang, M.-M., He, S., Li, Z., Li, H.-B., Niu, T., Xie, D.-H., Mei, Y., He, X.-D., Wei, L., et al. (2021) · BMC Cancer · doi:10.1186/s12885-021-09004-y · Cited by 9
Counts, B. R., Hardee, J. P., Fix, D. K., VanderVeen, B. N., Montalvo, R. N., & Carson, J. A. (2019) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000002166 · Cited by 23
Self-citationBayesian methods to estimate urban growth potential
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Evaluation of connectivity estimates using spiking neuronal network models
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Mechanism-Based Therapeutic Approaches to Cachexia
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“Of interest, increased AMPK activation is detectable in the skeletal muscle of tumor-bearing animals (Penna, Bonetto et al., 2010; White et al., 2011), where it is associated with marked alterations of mitochondrial morphology (Penna et al., unpublished observations).”
BackgroundMassart, I. S., Kouakou, A. F., Pelet, N., Lause, P., Schakman, O., Loumaye, A., Abou‐Samra, M., Deldicque, L., Bindels, L. B., Brichard, S. M., et al. (2024) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13454 · Cited by 8
The Etiology and Impact of Muscle Wasting in Metastatic CancerPreprint
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Counts, B., Zhang, Q., Halle, J. L., Puppa, M. J., Alway, S. E., Mohamed, J. S., Loenneke, J., & Carson, J. A. (2025) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.70064 · Cited by 6
Self-citationIntegrin-linked kinase expression in myeloid cells promotes colon tumorigenesis
Ahmed, A. U., Almasabi, S., Firestein, R., & Williams, B. R. G. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1270194 · Cited by 6
“…loss, poor survival and splenomegaly in APC min/+ mice The APC min/+ mouse is not only an established model of CRC but also presents with cancer cachexia, a wasting syndrome due to body weight loss associated with the skeletal muscle wasting with or without the loss in adipose tissue (32 – 34).”
BackgroundMiyazaki, M., Sawada, A., Sawamura, D., & Yoshida, S. (2023) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2023.101536 · Cited by 6
Cardiac Complications: The Understudied Aspect of Cancer Cachexia
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“Furthermore, muscle wasting in ApcMin/+ is associated with increase in IL-6 levels [39].”
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Walker‐256 tumor alters morphology of intestinal myenteric plexus in rats
Marega, P., Liberti, E. A., Freitas, J. S., & Kietzer, K. (2018) · Neurogastroenterology and Motility · doi:10.1111/nmo.13322 · Cited by 6
Adaptation for multisensory relative timing
Linares, D., Cos, I., & Roseboom, W. (2016) · Current Opinion in Behavioral Sciences · doi:10.1016/j.cobeha.2016.01.005 · Cited by 8
Urbanisation and earthquake disturbance influence microbial nutrient limitation in streams
Moffett, E., Simon, K., & Harding, J. (2015) · doi:10.1111/fwb.12600 · Cited by 6
Li, Y.-C., Yin, G., Li, S., Zheng, Q., Jiang, Y., Li, C.-Y., Yang, L., Li, H., Chen, X., Yang, P., et al. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-025-07527-7 · Cited by 5
Gugel, J. F., Currie, J., Alamillo, L., Flint, J., Kim, K.-Y., Debliqui, M., Ellisman, M., Lam, M. P. Y., Lau, E., Drigo, R. A., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116768 · Cited by 5
“14,15 Additionally, protein homeostasis is known to be disrupted in a variety of muscle diseases, including muscular dystrophies, 16,17 cancer cachexia, 18,19 aging, 20 and heart disease.”
Cheng, M., Li, Y., Liang, D., & Wu, C. (2025) · Frontiers in Nutrition · doi:10.3389/fnut.2025.1640092 · Cited by 5
Jin, C.-Y., Wang, S., Sui, X., Meng, Q., & Wu, G.-H. (2024) · Lipids in Health and Disease · doi:10.1186/s12944-024-02126-9 · Cited by 5
Intramuscular CMT-167 Tumors Produce a Mild Cachexia Phenotype in C57BL/6J Mice
Remaily, B. C., Vu, T., Thomas, J., Kim, K., Stanton, C., Xie, Z.-L., Granchie, L., Manna, M., Gregorevic, P., Mo, X., et al. (2025) · JCSM communications · doi:10.1002/rco2.117 · Cited by 4
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“Similar to other models of cancer cachexia (Brown et al., 2018; Manne et al., 2013; White et al., 2011), Yoshida tumors caused a significant decrease in 4E-BP1 phosphorylation in both skeletal and cardiac muscle.”
ResultDunlap, K. R., Steiner, J., Hickner, R., Chase, P., & Gordon, B. S. (2023) · Journal of applied physiology · doi:10.1152/japplphysiol.00113.2023 · Cited by 4
Saroul, N., Tardif, N., Pereira, B., Dissard, A., Montrieul, L., Sanchez, P., Salles, J., Petersen, J., Jakobson, T., Gilain, L., et al. (2023) · Cancers · doi:10.3390/cancers15061843 · Cited by 4
Khamoui, A. V., Tokmina‐Roszyk, D., Feresin, R. G., Fields, G. B., & Visavadiya, N. P. (2022) · Proteomics · doi:10.1002/pmic.202100157 · Cited by 4
“Tissue was collected from C26 mice between days 14–21 after tumor cell injection, and classified according to weight loss in accordance with previous literature [14, 27].”
MethodDunlap, K. R., Steiner, J. L., Rossetti, M. L., Kimball, S. R., & Gordon, B. S. (2021) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01064.2020 · Cited by 6
Khamoui, A. V., Halle, J. L., Pena, G. S., Paez, H., Rossiter, H. B., Visavadiya, N. P., & Whitehurst, M. (2018) · bioRxiv · doi:10.1101/493056 · Cited by 4
Abundance and size change of Hannaea baicalensis in Lake Baikal
Jewson, D., & Bixby, R. (2016) · doi:10.1080/09670262.2015.1110860 · Cited by 4
Metadata
- Authors
- White, J. P., Baynes, J. W., Welle, S. L., Kostek, M. C., Matesic, L. E., Sato, S., & Carson, J. A.
- Affiliations
- University of South Carolina (US)
- University of Rochester Medicine (US)
- Corresponding author
- Carson, James A.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2011-09-19
- Volume
- 6
- Issue
- 9
- Pages
- e24650
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3176277
- OpenAlex
- W2151316758
- Cited by
- 260
- References
- 82
- Citations by year
- 2026: 8 · 2025: 16 · 2024: 21 · 2023: 22 · 2022: 20 · 2021: 29 · 2020: 24 · 2019: 18 · 2018: 18 · 2017: 19 · 2016: 11 · 2015: 11 · 2014: 12 · 2013: 17 · 2012: 12
- FWCI
- 5.59
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Scholar Commons (University of South Carolina) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- National Institutes of Health
- Chugai Pharmaceutical
- National Cancer Institute (R01CA121249)
- National Center for Research Resources (P20RR017698)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology (medical) › Nutrition and Health in Aging
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- cancer cachexia, skeletal muscle protein turnover, muscle protein synthesis, muscle protein degradation, colorectal cancer, IL-6 signaling, AMPK, Raptor phosphorylation, muscle atrophy, weight loss, IL-6 receptor antibody
- MeSH terms
- Adenosine Triphosphate, Animals, Body Weight, Cachexia, Enzyme Activation, Inflammation, Insulin-Like Growth Factor I, Mice, Inbred C57BL, Mice, Mutant Strains, Muscle Proteins, Myofibrils, Neoplasms, Organ Size, Phosphorylation, Protein Biosynthesis, Signal Transduction, Interleukin-6, Disease Progression, Muscle, Skeletal, Adiposity, Mice, AMP-Activated Protein Kinases, TOR Serine-Threonine Kinases, Proteolysis
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