Cited by 183Muscle Physiology and DisordersAdipokines, Inflammation, and Metabolic DiseasesAdipose Tissue and Metabolism

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Myostatin, activin receptor IIb, and follistatin-like-3 gene expression are altered in adipose tissue and skeletal muscle of obese mice

Allen, David L., Cleary, Allison S., Speaker, Kristin J., Lindsay, Sarah F., Uyenishi, Jill, Reed, Jason M., Madden, Molly C., Mehan, Ryan S.·2008·American Journal of Physiology-Endocrinology and Metabolism

DOI 10.1152/ajpendo.00798.2007

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Abstract

Myostatin (MSTN) is a secreted growth inhibitor expressed in muscle and adipose. We sought to determine whether expression of MSTN, its receptor activin RIIb (ActRIIb), or its binding protein follistatin-like-3 (FSTL3) are altered in subcutaneous or visceral adipose or in skeletal muscle in response to obesity. MSTN and ActRIIb mRNA levels were low in subcutaneous (SQF) and visceral fat (VF) from wild-type mice but were 50- to 100-fold higher in both SQF and VF from ob/ob compared with wild-type mice. FSTL3 mRNA levels were increased in SQF but decreased in VF in ob/ob compared with wild-type mice. Moreover, MSTN mRNA levels were twofold greater in tibialis anterior (TA) from ob/ob mice, whereas ActRIIb and FSTL3 mRNA levels were unchanged. MSTN mRNA levels were also increased in TA and SQF from mice on a high-fat diet. Injection of ob/ob mice with recombinant leptin caused FSTL3 mRNA levels to decrease in both VF and SQF in ob/ob mice; MSTN and ActRIIb mRNA levels tended to decrease only in VF. Finally, MSTN mRNA levels and promoter activity were low in adipogenic 3T3-L1 cells, but an MSTN promoter-reporter construct was activated in 3T3-L1 cells by cotransfection with the adipogenic transcription factors SREBP-1c, C/EBPalpha, and PPARgamma. These results demonstrate that expression of MSTN and its associated binding proteins can be modulated in adipose tissue and skeletal muscle by chronic obesity and suggest that alterations in their expression may contribute to the changes in growth and metabolism of lean and fat tissues occurring during obesity.

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Effects of the obese Gene Product on Body Weight Regulation in ob / ob Mice
Pelleymounter, M. A., Cullen, M. J., Baker, M. B., Hecht, R., Winters, D., Boone, T., & Collins, F. (1995) · Science · doi:10.1126/science.7624776 · Cited by 4,017
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
Bone Morphogenetic Proteins
Chen, D., Zhao, M., & Mundy, G. R. (2004) · Growth Factors · doi:10.1080/08977190412331279890 · Cited by 1,921
Comparison of the Release of Adipokines by Adipose Tissue, Adipose Tissue Matrix, and Adipocytes from Visceral and Subcutaneous Abdominal Adipose Tissues of Obese Humans
Fain, J. N., Madan, A. K., Hiler, M. L., Cheema, P. S., & Bahouth, S. W. (2004) · Endocrinology · doi:10.1210/en.2003-1336 · Cited by 1,619
Regulation of myostatin activity and muscle growth
Lee, S.-J., & McPherron, A. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151270098 · Cited by 1,616
A deletion in the bovine myostatin gene causes the double–muscled phenotype in cattle
Grobet, L., Royo Martin, L. J., Poncelet, D., Pirottin, D., Brouwers, B., Riquet, J., Schoeberlein, A., Dunner, S., Ménissier, F., Massabanda, J., et al. (1997) · Nature Genetics · doi:10.1038/ng0997-71 · Cited by 1,556
Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child
Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040933 · Cited by 1,399
Induction of Cachexia in Mice by Systemically Administered Myostatin
Zimmers, T. A., Davies, M. V., Koniaris, L. G., Haynes, P. A., Esquela‐Kerscher, A., Tomkinson, K. N., McPherron, A. C., Wolfman, N. M., & Lee, S. (2002) · Science · doi:10.1126/science.1069525 · Cited by 908
Peroxisome proliferator-activated receptor gene expression in human tissues. Effects of obesity, weight loss, and regulation by insulin and glucocorticoids.
Vidal‐Puig, A., Considine, R. V., Jimenez‐Liñan, M., Werman, A., Pories, W. J., Caro, J. F., & Flier, J. S. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119424 · Cited by 785
Regulation of PPAR gamma gene expression by nutrition and obesity in rodents.
Vidal‐Puig, A., Jimenez‐Liñan, M., Lowell, B. B., Hamann, A., Hu, E., Spiegelman, B. M., Flier, J. S., & Moller, D. E. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118703 · Cited by 660

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Wang, F., Liao, Y., Li, X., Ren, C., Cheng, C., & Ren, Y. (2012) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-012-0092-9 · Cited by 39
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Sarcopenia and Appendicular Muscle Mass as Predictors of Impaired Fasting Glucose/Type 2 Diabetes in Elderly Women
Buscemi, C., Ferro, Y., Pujia, R., Mazza, E., Boragina, G., Sciacqua, A., Piro, S., Pujia, A., Sesti, G., Buscemi, S., et al. (2021) · Nutrients · doi:10.3390/nu13061909 · Cited by 38
Masticatory muscle function affects the pathological conditions of dentofacial deformities
Yamada, T., Sugiyama, G., & Mori, Y. (2020) · Japanese Dental Science Review · doi:10.1016/j.jdsr.2019.12.001 · Cited by 39
Myostatin: a potential therapeutic target for metabolic syndrome
Yang, M., Liu, C., Jiang, N., Liu, Y., Luo, S., Li, C., Zhao, H., Han, Y., Chen, W., Li, L., et al. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1181913 · Cited by 33
Leucine alters hepatic glucose/lipid homeostasis via the myostatin-AMP-activated protein kinase pathway - potential implications for nonalcoholic fatty liver disease
Zarfeshani, A., Ngo, S., & Sheppard, A. M. (2014) · Clinical Epigenetics · doi:10.1186/1868-7083-6-27 · Cited by 32
The correlation of resistance exercise-induced myostatin with insulin resistance and plasma cytokines in healthy young men
Kazemi, F. (2015) · Journal of Endocrinological Investigation · doi:10.1007/s40618-015-0373-9 · Cited by 33
Decreasing Lean Body Mass with Age: Challenges and Opportunities for Novel Therapies
Boutari, C., & Mantzoros, C. S. (2017) · Endocrinology and Metabolism · doi:10.3803/enm.2017.32.4.422 · Cited by 34
Myostatin Attenuation In Vivo Reduces Adiposity, but Activates Adipogenesis
Li, N., Yang, Q., Walker, R. G., Thompson, T. B., Du, ‬., & Rodgers, B. D. (2015) · Endocrinology · doi:10.1210/en.2015-1546 · Cited by 29
Hormone Therapy and Maximal Eccentric Exercise Alters Myostatin-Related Gene Expression in Postmenopausal Women
Dieli-Conwright, C. M., Spektor, T. M., Rice, J. C., Sattler, F. R., & Schroeder, E. T. (2012) · The Journal of Strength and Conditioning Research · doi:10.1519/jsc.0b013e318251083f · Cited by 29
Can Exercise Training Alter Human Skeletal Muscle DNA Methylation?
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Local myostatin inhibition improves skeletal muscle glucose uptake in insulin-resistant high-fat diet-fed mice
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Retracted
Fighting obesity: When muscle meets fat
Yang, X., Bi, P., & Kuang, S. (2014) · Adipocyte · doi:10.4161/21623945.2014.964075 · Cited by 25
Leptin signaling in skeletal muscle after bed rest in healthy humans
Guerra, B., Ponce‐González, J. G., Morales‐Álamo, D., Guadalupe‐Grau, A., Kiilerich, K., Fuentes, T., Ringholm, S., Biensø, R. S., Santana, A., Lundby, C., et al. (2013) · European Journal of Applied Physiology · doi:10.1007/s00421-013-2779-4 · Cited by 25
Myostatin/SMAD4 signaling-mediated regulation of miR-124-3p represses glucocorticoid receptor expression and inhibits adipocyte differentiation
Liu, K., Zhang, X., Wei, W., Liu, X., Tian, Y., Han, H., Zhang, L., Wu, W., & Chen, J. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00405.2018 · Cited by 25
Crosstalk between bone and other organs
Yuan, W., & Song, C. (2022) · Medical Review · doi:10.1515/mr-2022-0018 · Cited by 27
AAV-Mediated Administration of Myostatin Pro-Peptide Mutant in Adult Ldlr Null Mice Reduces Diet-Induced Hepatosteatosis and Arteriosclerosis
Guo, W., Wong, S., & Bhasin, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071017 · Cited by 24
Expression of myostatin, myostatin receptors and follistatin in diabetic rats submitted to exercise
Dibai, D. B., Bueno, P. G., Silva, R. N., Nakahara, N. H., Selistre-de-Araújo, H. S., Nonaka, K. O., & Leal, A. M. O. (2012) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2012.05690.x · Cited by 24
Muscle as an Endocrine Organ
Legaard, G. E., & Pedersen, B. K. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-814593-7.00013-x · Cited by 24
Obesity and Low-Grade Inflammation Increase Plasma Follistatin-Like 3 in Humans
Brandt, C., Pedersen, M., Rinnov, A., Andreasen, A. S., Møller, K., Højman, P., Pedersen, B. K., & Plomgaard, P. (2014) · Mediators of Inflammation · doi:10.1155/2014/364209 · Cited by 22
Fruit of Schisandra chinensis and its bioactive component schizandrin B ameliorate obesity-induced skeletal muscle atrophy
Yoo, A., Ahn, J., Kim, M. J., Seo, H., Hahm, J., Jung, C. H., & Ha, T. Y. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111439 · Cited by 22
Decreased myostatin in response to a controlled DASH diet is associated with improved body composition and cardiometabolic biomarkers in older adults: results from a controlled-feeding diet intervention study
Perry, C. A., Van Guilder, G. P., & Butterick, T. A. (2022) · BMC Nutrition · doi:10.1186/s40795-022-00516-9 · Cited by 16

Authors: Allen, D. L., Cleary, A. S., Speaker, K. J., Lindsay, S. F., Uyenishi, J., Reed, J. M., Madden, M. C., & Mehan, R. S.
Affiliations: University of Colorado Boulder (US)
ORCID: Speaker, Kristin J.
Lindsay, Sarah F.
Madden, Molly C.
Venue: American Journal of Physiology-Endocrinology and Metabolism
Publisher: American Physiological Society
Published: 2008-05
Volume: 294
Issue: 5
Pages: E918-E927
ISSN: 0193-1849 (ISSN-L)
1522-1555
DOI: 10.1152/ajpendo.00798.2007
OpenAlex: W1986156265
Cited by: 183
References: 50
Citations by year: 2026: 3 · 2025: 5 · 2024: 7 · 2023: 5 · 2022: 11 · 2021: 11 · 2020: 8 · 2019: 10 · 2018: 9 · 2017: 8 · 2016: 8 · 2015: 17 · 2014: 18 · 2013: 17 · 2012: 14
FWCI: 4.38
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Arthritis and Musculoskeletal and Skin Diseases (K01 AR-0505-01)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
Keywords: myostatin, FSTL3, obesity, adipose tissue, skeletal muscle, subcutaneous adipose tissue, visceral fat, ob/ob mice, leptin, high-fat diet, adipogenic transcription factors, SREBP-1c, C/EBPα, PPARγ, 3T3-L1 cells, gene expression regulation
MeSH terms: Adipose Tissue, Animals, Cells, Cultured, Cloning, Molecular, Diet, Dietary Fats, DNA, Male, Mice, Inbred C57BL, Mice, Obese, Obesity, Proteins, RNA, Messenger, Transfection, Signal Transduction, Transforming Growth Factor beta, 3T3 Cells, Muscle, Skeletal, Reverse Transcriptase Polymerase Chain Reaction, Leptin, Activin Receptors, Type II, Follistatin-Related Proteins, Mice, Myostatin

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Myostatin, activin receptor IIb, and follistatin-like-3 gene expression are altered in adipose tissue and skeletal muscle of obese mice

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