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The myokine decorin is regulated by contraction and involved in muscle hypertrophy
Abstract
The health-promoting effects of regular exercise are well known, and myokines may mediate some of these effects. The small leucine-rich proteoglycan decorin has been described as a myokine for some time. However, its regulation and impact on skeletal muscle has not been investigated in detail. In this study, we report decorin to be differentially expressed and released in response to muscle contraction using different approaches. Decorin is released from contracting human myotubes, and circulating decorin levels are increased in response to acute resistance exercise in humans. Moreover, decorin expression in skeletal muscle is increased in humans and mice after chronic training. Because decorin directly binds myostatin, a potent inhibitor of muscle growth, we investigated a potential function of decorin in the regulation of skeletal muscle growth. In vivo overexpression of decorin in murine skeletal muscle promoted expression of the pro-myogenic factor Mighty, which is negatively regulated by myostatin. We also found Myod1 and follistatin to be increased in response to decorin overexpression. Moreover, muscle-specific ubiquitin ligases atrogin1 and MuRF1, which are involved in atrophic pathways, were reduced by decorin overexpression. In summary, our findings suggest that decorin secreted from myotubes in response to exercise is involved in the regulation of muscle hypertrophy and hence could play a role in exercise-related restructuring processes of skeletal muscle.
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“Circulating levels of decorin are increased in response to exercise in humans (46), whereas exercise training reduces the levels of myostatin within muscles and blood (47, 48).”
From Muscle–Organ Crosstalk: The Emerging Roles of Myokines (2020) · cites this paper as [46]
In the citing paper
“Decorin has been identified as a myokine that is regulated by exercise and acts as an antagonist to myostatin (46).”
From Muscle–Organ Crosstalk: The Emerging Roles of Myokines (2020) · cites this paper as [46]
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“Among the proteins identified in the exercise-related modules were several previously indicated in the literature as being altered with exercise, including brain-derived neurotrophic factor (BDNF), interleukin-6 (IL-6), secreted protein acidic and rich in cysteine (SPARC), decorin, heat shock proteins 60 (Hsp60) and 7…”
BackgroundLau, P., Vico, L., & Rittweger, J. (2022) · Biomedicines · doi:10.3390/biomedicines10020342 · Cited by 32
Impact of adipokines and myokines on fat browning
Rodríguez, A., Catalán, V., Ramírez, B., Unamuno, X., Portincasa, P., Gómez‐Ambrosi, J., Frühbeck, G., & Becerril, S. (2020) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-020-00736-2 · Cited by 31
“Decorin is a crucial component of the extracellular matrix and a newly characterised contraction-induced myokine [68].”
BackgroundGill transcriptomic analysis in fast- and slow-growing individuals of Mytilus galloprovincialis
Prieto, D., Markaide, P., Urrutxurtu, I., Navarro, E., Artigaud, S., Fleury, E., Ibarrola, I., & Urrutia, M. B. (2019) · Aquaculture · doi:10.1016/j.aquaculture.2019.734242 · Cited by 29
Impact of Decorin on the Physical Function and Prognosis of Patients with Hepatocellular Carcinoma
Kawaguchi, T., Yoshio, S., Sakamoto, Y., Hashida, R., Koya, S., Hirota, K., Nakano, D., Yamamura, S., Niizeki, T., Matsuse, H., et al. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9040936 · Cited by 29
“Meanwhile, decorin is an exercise-induced myokine that suppresses muscle atrophy via inhibition of myostatin [15].”
BackgroundThe Role of Decorin Proteoglycan in Mitophagy
Neill, T., & Iozzo, R. V. (2022) · Cancers · doi:10.3390/cancers14030804 · Cited by 29
“Decorin has also been proposed to act as a myokine induced by exercise [188] and growth hormone [189].”
BackgroundMageriu, V., Manole, E., Bastian, A. E., & Stăniceanu, F. (2020) · Journal of Immunology Research · doi:10.1155/2020/9079083 · Cited by 28
“In an in vivo experimental study, it was shown that over-expression of decorin in murine skeletal muscle promoted expression of Mighty gene [123], negatively regulated by myostatin, and an increased response of myogenic factor Myod1 [124] and follistatin [112].”
Exercise, Neuroprotective Exerkines, and Parkinson’s Disease: A Narrative Review
Mitchell, A. K., Bliss, R. R., & Church, F. (2024) · Biomolecules · doi:10.3390/biom14101241 · Cited by 33
“Since many exerkines are generated in skeletal muscle, Kwon et al. [379] reported that the following myokines, regulated by exercise, were altered by aging: apelin, BAIBA, BMP-7, decorin, IGF-1, IL-15, irisin, SDF-1, sestrin, SPARC, and VEGF were decreased, while IL-6 and myostatin were increased.”
BackgroundWilloughby, D. S., Cardaci, T. D., Machek, S. B., Wilburn, D. T., & Heileson, J. L. (2022) · Journal of Sports Science and Medicine · doi:10.52082/jssm.2022.616 · Cited by 24
Decorin, a growth hormone-regulated protein in humans
Bahl, N., Stone, G., McLean, M. P., Ho, K. K. Y., & Birzniece, V. (2017) · European Journal of Endocrinology · doi:10.1530/eje-17-0844 · Cited by 24
Blanks, A. M., Rodriguez‐Miguelez, P., Looney, J. C., Tucker, M. A., Jeong, J., Thomas, J., Blackburn, M., Stepp, D. W., Weintraub, N. J., & Harris, R. A. (2019) · Brain Behavior & Immunity - Health · doi:10.1016/j.bbih.2019.100011 · Cited by 21
“Moreover, in-vitro studies have shown increased myokine production of decorin in response to low frequency (1 Hz) stretch (Kanzleiter et al., 2014).”
BackgroundPotential Mechanisms for How Long-Term Physical Activity May Reduce Insulin Resistance
Lee-Ødegård, S., Olsén, T., Norheim, F., Drevon, C. A., & Birkeland, K. I. (2022) · Metabolites · doi:10.3390/metabo12030208 · Cited by 20
“, we have shown that an increase in “immune genes” after long-term PA may be related to the SkM remodeling of the extracellular matrix [72,73,77].”
BackgroundThu, V. T., Kim, H. K., Long, L. T., Thuy, T. T., Huy, N. Q., Kim, S. H., Kim, N., Ko, K. S., Rhee, B. D., & Han, J. (2016) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2016.20.3.305 · Cited by 21
“Exercise has a various benefit for the cardiac protection by itself or combined with other medicines [49,50].”
BackgroundManagement of Oxidative Stress: Crosstalk Between Brown/Beige Adipose Tissues and Skeletal Muscles
Pan, R., & Chen, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.712372 · Cited by 22
Micielska, K., Flis, M., Kortas, J. A., Rodziewicz-Flis, E. A., Antosiewicz, J., Wochna, K., Lombardi, G., & Ziemann, E. (2021) · Nutrients · doi:10.3390/nu13124393 · Cited by 19
“described a significantly higher decorin expression in response to regular resistance and endurance training among men, as well on an animal model [18], a direct impact of exercise on decorin concentration in women is debated.”
BackgroundKnuiman, P., Hopman, M. T. E., Hangelbroek, R., & Mensink, M. (2018) · Physiological Reports · doi:10.14814/phy2.13708 · Cited by 18
“In their study, which clearly had a higher exercise load, plasma decorin peaked immediately after exercise, a time point we are lacking in our study (Kanzleiter et al. 2014).”
BackgroundResultInfluentialPagano, A. F., Arc‐Chagnaud, C., Brioche, T., Chopard, A., & Py, G. (2019) · Cellular Physiology and Biochemistry · doi:10.33594/000000121 · Cited by 19
Nguyen, T. T., Dao, T., Nguyen, H. T., Park, J.-H., Jeong, S.-J., Kim, S., Jo, Y., Thieu, N. T. H., Zhao, J., Ding, F., et al. (2026) · Endocrinology and Metabolism · doi:10.3803/enm.2025.2656 · Cited by 23
“Decorin, a muscle-se-creted proteoglycan, binds directly to myostatin and may inhibit its activity, thereby promoting muscle growth; its expression increases following exercise [71].”
Physical Activity, Obesity and Weight Loss Maintenance
Brandt, C., & Pedersen, B. K. (2022) · Handbook of experimental pharmacology · doi:10.1007/164_2021_575 · Cited by 21
Vasyukova, O. V., Kasyanova, Y. V., Okorokov, P. L., & Bezlepkina, O. B. (2021) · Problems of Endocrinology · doi:10.14341/probl12779 · Cited by 18
Schering, L., Hoene, M., Kanzleiter, T., Jähnert, M., Wimmers, K., Klaus, S., Eckel, J., Weigert, C., Schürmann, A., Maak, S., et al. (2015) · Archives of Physiology and Biochemistry · doi:10.3109/13813455.2015.1092044 · Cited by 15
“Decorin is a well-known myokine but its regulation in contracting skeletal muscle and its response to exercise have only been investigated in detail by us recently (Kanzleiter et al., 2014).”
BackgroundMethodInfluentialPharmacology of doping agents—mechanisms promoting muscle hypertrophy
Parr, M. K., & Laughlin, A. M. M. (2018) · AIMS molecular science · doi:10.3934/molsci.2018.2.131 · Cited by 14
Emphasizing Task-Specific Hypertrophy to Enhance Sequential Strength and Power Performance
Travis, S. K., Ishida, A., Taber, C. B., Fry, A. C., & Stone, M. H. (2020) · Journal of Functional Morphology and Kinesiology · doi:10.3390/jfmk5040076 · Cited by 22
R-spondin3 is a myokine that differentiates myoblasts to type I fibres
Mita, Y., Zhu, H., Furuichi, Y., Hamaguchi, H., Manabe, Y., & FUJII, N. L. (2022) · Scientific Reports · doi:10.1038/s41598-022-16640-2 · Cited by 15
Review of the health-promoting effects of exercise and the involvement of myokines.
Nishii, K., Aizu, N., & Yamada, K. (2023) · PubMed Central · doi:10.20407/fmj.2022-020 · Cited by 17
Calcaterra, V., Magenes, V. C., Bianchi, A., Rossi, V., Gatti, A., Marin, L., Vandoni, M., & Zuccotti, G. (2024) · Life · doi:10.3390/life14091198 · Cited by 20
“Additionally, Myogenic Differentiation 1 (Myod1) and follistatin expression are elevated in response to decorin overexpression [33,46].”
BackgroundBekki, M., Hashida, R., Kawaguchi, T., Goshima, N., Yoshiyama, T., Otsuka, T., Koya, S., Hirota, K., Matsuse, H., Niizeki, T., et al. (2018) · JCSM Rapid Communications · doi:10.1002/j.2617-1619.2018.tb00009.x · Cited by 14
Hormonal, immune, and oxidative stress responses to blood flow‐restricted exercise
Hjortshoej, M. H., Aagaard, P., Storgaard, C. D., Juneja, H., Lundbye‐Jensen, J., Magnusson, S. P., & Couppé, C. (2023) · Acta Physiologica · doi:10.1111/apha.14030 · Cited by 13
Metadata
- Authors
- Kanzleiter, T., Rath, M., Görgens, S. W., Jensen, J., Tangen, D. S., Kolnes, A. J., Kolnes, K. J., Lee, S., Eckel, J., Schürmann, A., & Eckardt, K.
- Affiliations
- German Center for Diabetes Research (DE)
- Deutsches Diabetes-Zentrum e.V. (DE)
- Norwegian School of Sport Sciences (NO)
- Charles University (CZ)
- University of Oslo (NO)
- Corresponding author
- Eckardt, Kristin
- ORCID
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2014-07
- Volume
- 450
- Issue
- 2
- Pages
- 1089-1094
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2050986782
- Cited by
- 209
- References
- 32
- Citations by year
- 2026: 20 · 2025: 22 · 2024: 24 · 2023: 16 · 2022: 35 · 2021: 22 · 2020: 16 · 2019: 12 · 2018: 10 · 2017: 7 · 2016: 16 · 2015: 8 · 2014: 1
- FWCI
- 4.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Bundesministerium für Bildung und Forschung
- Bundesministerium für Gesundheit
- Deutsche Forschungsgemeinschaft (EC 440/1-1)
- Leibniz-Gemeinschaft (SAW-FBN-2013-3)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology (medical) › Exercise and Physiological Responses
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- decorin, myokines, muscle contraction, muscle hypertrophy, resistance training, skeletal muscle growth, myostatin, MyoD, follistatin, atrogin-1, MuRF1, ubiquitin ligase, muscle atrophy, myotubes, exercise training
- MeSH terms
- Adolescent, Adult, Animals, Cells, Cultured, Female, Humans, Male, Muscle Contraction, Physical Conditioning, Animal, Exercise, Muscle, Skeletal, Muscle Fibers, Skeletal, Muscle Development, Mice, Decorin
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