Muscle hypertrophy in athlete training from a medical point of view - what do we know
DOI:
https://doi.org/10.12775/JEHS.2023.50.01.007Keywords
skeletal muscle, hypertrophy, testosteron, growth hormone, cortisol, IGF1Abstract
Introduction
Hypertrophy is the process of increasing the mass of a tissue. In this article, we focused on the impact of the mechanisms of muscle hypertrophy, its effect on the human body, correlation with the course of diseases and tolerance of treatment. We considered the benefits of having well-developed, and also touched on the problems of underdeveloped muscle mass.
Results
The main factors causing hypertrophy are resistance exercise training, mechanotransduction, metabolic pathways, ribosomal biogenesis, gene expression and the impact of hormones. The beneficial effect of high concentrations of testosterone and growth hormone, also IGF1, on skeletal muscle hypertrophy has been proven. On the other side, the studies have shown that high concentrations of glucocorticoids, such as cortisol are associated with reduced muscle mass.
There are many positive aspects of a well-developed muscle mass such as an impact on the prognosis in patients with cancers and sometimes reduces mortality among them. The problems of low muscle mass and sarcopenia are also mentioned. Low muscle mass can affect the poor prognosis of diseases such as cancer, hepatic cirrhosis and COVID-19. Postoperative complications are more common in patients with low muscle mass. One way to prevent this process may be to introduce resistance exercise training in patients struggling with problems of muscular atrophy.
Conclusion
Skeletal muscles have multiple functions in the human body. In addition to movement, they play a role in molecular processes like hormonal regulation. In addition, they can, when well developed, positively influence healing processes and the course of disease.
References
J. McKendry, T. Stokes, J. C. McLeod, and S. M. Phillips, “Resistance Exercise, Aging, Disuse, and Muscle Protein Metabolism,” Compr Physiol, vol. 11, no. 3, pp. 2249–2278, Jul. 2021, doi: 10.1002/CPHY.C200029.
C. Lim, E. A. Nunes, B. S. Currier, J. C. McLeod, A. C. Q. Thomas, and S. M. Phillips, “An Evidence-Based Narrative Review of Mechanisms of Resistance Exercise–Induced Human Skeletal Muscle Hypertrophy,” Med Sci Sports Exerc, vol. 54, no. 9, p. 1546, Sep. 2022, doi: 10.1249/MSS.0000000000002929.
S. Schiaffino, C. Reggiani, T. Akimoto, and B. Blaauw, “Molecular Mechanisms of Skeletal Muscle Hypertrophy,” J Neuromuscul Dis, vol. 8, no. 2, p. 169, 2021, doi: 10.3233/JND-200568.
A. C. Durieux, D. Desplanches, O. Freyssenet, and M. Flück, “Mechanotransduction in striated muscle via focal adhesion kinase,” Biochem Soc Trans, vol. 35, no. Pt 5, pp. 1312–1313, Nov. 2007, doi: 10.1042/BST0351312.
M. Vitadello et al., “Loss of melusin is a novel, neuronal NO synthase/FoxO3‐independent master switch of unloading‐induced muscle atrophy,” J Cachexia Sarcopenia Muscle, vol. 11, no. 3, p. 802, Jun. 2020, doi: 10.1002/JCSM.12546.
P. Joanne et al., “Impaired Adaptive Response to Mechanical Overloading in Dystrophic Skeletal Muscle,” PLoS One, vol. 7, no. 4, p. 35346, 2012, doi: 10.1371/JOURNAL.PONE.0035346.
Y. Eid Mutlak et al., “A signaling hub of insulin receptor, dystrophin glycoprotein complex and plakoglobin regulates muscle size,” Nat Commun, vol. 11, no. 1, Dec. 2020, doi: 10.1038/S41467-020-14895-9.
Z. Meng et al., “RAP2 Mediates Mechano-responses of Hippo Pathway,” Nature, vol. 560, no. 7720, p. 655, Aug. 2018, doi: 10.1038/S41586-018-0444-0.
H. Wackerhage, B. J. Schoenfeld, D. L. Hamilton, M. Lehti, and J. J. Hulmi, “Stimuli and sensors that initiate skeletal muscle hypertrophy following resistance exercise,” J Appl Physiol, vol. 126, no. 1, pp. 30–43, Jan. 2019, doi: 10.1152/JAPPLPHYSIOL.00685.2018/ASSET/IMAGES/LARGE/ZDG0121828450001.JPEG.
K. Powers, G. Schappacher-Tilp, A. Jinha, T. Leonard, K. Nishikawa, and W. Herzog, “Titin force is enhanced in actively stretched skeletal muscle,” Journal of Experimental Biology, vol. 217, no. 20, pp. 3629–3636, Oct. 2014, doi: 10.1242/JEB.105361/258055/AM/TITIN-FORCE-IS-ENHANCED-IN-ACTIVELY-STRETCHED.
S. Schiaffino and C. Mammucari, “Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models,” Skelet Muscle, vol. 1, no. 1, p. 4, Jan. 2011, doi: 10.1186/2044-5040-1-4.
G. Y. Liu and D. M. Sabatini, “mTOR at the nexus of nutrition, growth, ageing and disease,” Nat Rev Mol Cell Biol, vol. 21, no. 4, p. 183, Apr. 2020, doi: 10.1038/S41580-019-0199-Y.
M. Murgia, A. L. Serrano, E. Calabria, G. Pallafacchina, T. Lømo, and S. Schiaffino, “Ras is involved in nerve-activity-dependent regulation of muscle genes,” Nature Cell Biology 2000 2:3, vol. 2, no. 3, pp. 142–147, Feb. 2000, doi: 10.1038/35004013.
T. J. Kirby, J. D. Lee, J. H. England, T. Chaillou, K. A. Esser, and J. J. McCarthy, “Blunted hypertrophic response in aged skeletal muscle is associated with decreased ribosome biogenesis,” J Appl Physiol, vol. 119, no. 4, p. 321, Aug. 2015, doi: 10.1152/JAPPLPHYSIOL.00296.2015.
D. Hammarström et al., “Benefits of higher resistance-training volume are related to ribosome biogenesis,” J Physiol, vol. 598, no. 3, pp. 543–565, Feb. 2020, doi: 10.1113/JP278455.
C. McGlory, M. C. Devries, and S. M. Phillips, “Recovery from Exercise: Skeletal muscle and resistance exercise training; the role of protein synthesis in recovery and remodeling,” J Appl Physiol, vol. 122, no. 3, p. 541, Mar. 2017, doi: 10.1152/JAPPLPHYSIOL.00613.2016.
M. J. Stec, N. A. Kelly, G. M. Many, S. T. Windham, S. C. Tuggle, and M. M. Bamman, “Ribosome biogenesis may augment resistance training-induced myofiber hypertrophy and is required for myotube growth in vitro,” Am J Physiol Endocrinol Metab, vol. 310, no. 8, p. E652, Apr. 2016, doi: 10.1152/AJPENDO.00486.2015.
D. Hammarström et al., “Benefits of higher resistance-training volume are related to ribosome biogenesis,” J Physiol, vol. 598, no. 3, pp. 543–565, Feb. 2020, doi: 10.1113/JP278455.
M. M. Robinson et al., “Enhanced Protein Translation Underlies Improved Metabolic and Physical Adaptations to Different Exercise Training Modes in Young and Old Humans,” Cell Metab, vol. 25, no. 3, p. 581, Mar. 2017, doi: 10.1016/J.CMET.2017.02.009.
N. D. Steinert et al., “Mapping of the contraction-induced phosphoproteome identifies TRIM28 as a significant regulator of skeletal muscle size and function,” Cell Rep, vol. 34, no. 9, p. 108796, Mar. 2021, doi: 10.1016/J.CELREP.2021.108796.
U. Raue et al., “Transcriptome signature of resistance exercise adaptations: mixed muscle and fiber type specific profiles in young and old adults,” J Appl Physiol, vol. 112, no. 10, p. 1625, May 2012, doi: 10.1152/JAPPLPHYSIOL.00435.2011.
K. Aizawa et al., “Acute exercise activates local bioactive androgen metabolism in skeletal muscle,” Steroids, vol. 75, no. 3, pp. 219–223, Mar. 2010, doi: 10.1016/J.STEROIDS.2009.12.002.
N. R. Young, H. W. G. Baker, G. Liu, and E. Seeman, “Body composition and muscle strength in healthy men receiving testosterone enanthate for contraception,” J Clin Endocrinol Metab, vol. 77, no. 4, pp. 1028–1032, 1993, doi: 10.1210/JCEM.77.4.8408450.
N. Gharahdaghi, B. E. Phillips, N. J. Szewczyk, K. Smith, D. J. Wilkinson, and P. J. Atherton, “Links Between Testosterone, Oestrogen, and the Growth Hormone/Insulin-Like Growth Factor Axis and Resistance Exercise Muscle Adaptations,” Front Physiol, vol. 11, p. 621226, Jan. 2020, doi: 10.3389/FPHYS.2020.621226.
D. W. D. West et al., “Elevations in ostensibly anabolic hormones with resistance exercise enhance neither training-induced muscle hypertrophy nor strength of the elbow flexors,” J Appl Physiol, vol. 108, no. 1, p. 60, Jan. 2010, doi: 10.1152/JAPPLPHYSIOL.01147.2009.
S. Katsuhara et al., “Impact of Cortisol on Reduction in Muscle Strength and Mass: A Mendelian Randomization Study,” J Clin Endocrinol Metab, vol. 107, no. 4, pp. e1477–e1487, Mar. 2022, doi: 10.1210/CLINEM/DGAB862.
D. A. Gonçalves et al., “Insulin/IGF1 signalling mediates the effects of β2‐adrenergic agonist on muscle proteostasis and growth,” J Cachexia Sarcopenia Muscle, vol. 10, no. 2, p. 455, Apr. 2019, doi: 10.1002/JCSM.12395.
P. Mera, K. Laue, J. Wei, J. M. Berger, and G. Karsenty, “Osteocalcin is necessary and sufficient to maintain muscle mass in older mice,” Mol Metab, vol. 5, no. 10, p. 1042, Oct. 2016, doi: 10.1016/J.MOLMET.2016.07.002.
F. Damas et al., “Early- and later-phases satellite cell responses and myonuclear content with resistance training in young men,” PLoS One, vol. 13, no. 1, Jan. 2018, doi: 10.1371/JOURNAL.PONE.0191039.
B. J. Schoenfeld, “Potential Mechanisms for a Role of Metabolic Stress in Hypertrophic Adaptations to Resistance Training,” Sports Medicine 2013 43:3, vol. 43, no. 3, pp. 179–194, Jan. 2013, doi: 10.1007/S40279-013-0017-1.
P. Moctezuma-Velázquez, “The Importance of Muscle Mass Analysis in Acute Diseases,” Chest, vol. 164, no. 2, pp. 269–270, Aug. 2023, doi: 10.1016/j.chest.2023.04.010.
Y. M. T. Siahaan, V. Hartoyo, T. I. Hariyanto, and A. Kurniawan, “Coronavirus disease 2019 (Covid-19) outcomes in patients with sarcopenia: A meta-analysis and meta-regression,” Clin Nutr ESPEN, vol. 48, pp. 158–166, Apr. 2022, doi: 10.1016/j.clnesp.2022.01.016.
A. S. Tagliafico, B. Bignotti, L. Torri, and F. Rossi, “Sarcopenia: how to measure, when and why,” Radiol Med, vol. 127, no. 3, p. 228, Mar. 2022, doi: 10.1007/S11547-022-01450-3.
P. K. Durkee et al., “Men’s Bodily Attractiveness: Muscles as Fitness Indicators,” Evolutionary Psychology, vol. 17, no. 2, Apr. 2019, doi: 10.1177/1474704919852918.
M. Koeppel, K. Mathis, K. H. Schmitz, and J. Wiskemann, “Muscle hypertrophy in cancer patients and survivors via strength training. A meta-analysis and meta-regression,” Crit Rev Oncol Hematol, vol. 163, p. 103371, Jul. 2021, doi: 10.1016/J.CRITREVONC.2021.103371.
S. W. Moon et al., “Low muscle mass, low muscle function, and sarcopenia in the urban and rural elderly,” Sci Rep, vol. 12, no. 1, p. 14314, Dec. 2022, doi: 10.1038/S41598-022-18167-Y.
Z. Hu, H. Wang, H. L. In, J. Du, and W. E. Mitch, “Endogenous glucocorticoids and impaired insulin signaling are both required to stimulate muscle wasting under pathophysiological conditions in mice,” J Clin Invest, vol. 119, no. 10, p. 3059, Oct. 2009, doi: 10.1172/JCI38770.
C. Lim et al., “Both Traditional and Stair Climbing-based HIIT Cardiac Rehabilitation Induce Beneficial Muscle Adaptations,” Med Sci Sports Exerc, vol. 53, no. 6, pp. 1114–1124, Jun. 2021, doi: 10.1249/MSS.0000000000002573.
Downloads
Published
How to Cite
Issue
Section
License
Copyright (c) 2023 Jan Biłogras, Katarzyna Kostelecka, Łukasz Bryliński, Marcin Wais, Dariusz Gruca, Konrad Warchoł
This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.
The periodical offers access to content in the Open Access system under the Creative Commons Attribution-NonCommercial-ShareAlike 4.0
Stats
Number of views and downloads: 1004
Number of citations: 0