Myostatin, activin receptor IIb, and follistatin-like-3 gene expression are altered in adipose tissue and skeletal muscle of obese mice
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.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Circulating and skeletal muscle myostatin levels are present in obese subjects compared to non-obese subjects.
“so both circulating and SkM myostatin levels are present in obese subjects when compared to non-obese subjects (Allen et al., 2008; Hittel et al., 2009).”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Allen et al., 2008
Myostatin mRNA levels increase substantially in genetically modified obese mice (leptin-deficient ob/ob) and in mice receiving a high-fat diet.
“Myostatin mRNA levels increase substantially in genetically-modified obese mice (leptin-deficient ob/ob mice) and also in those receiving a high fat diet (HFD)”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Allen et al., 2008
Cites
Effects of the <i>obese</i> Gene Product on Body Weight Regulation in <i>ob</i> / <i>ob</i> 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 · see citing works
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 · see citing works
Chen, D., Zhao, M., & Mundy, G. R. (2004) · Growth Factors · doi:10.1080/08977190412331279890 · Cited by 1,921 · see citing works
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 · see citing works
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 1,571 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 656 · see citing works
(1996) · PubMed · Cited by 643 · see citing works
Gonzalez-Cadavid, N. F., Taylor, W. E., Yarasheski, K., Sinha-Hikim, I., Ma, K., Ezzat, S., Shen, R., Lalani, R., Asa, S., Mamita, M., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14938 · Cited by 571 · see citing works
Rebbapragada, A., Benchabane, H., Wrana, J. L., Celeste, A. J., & Attisano, L. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7230-7242.2003 · Cited by 566 · see citing works
Suppression of body fat accumulation in myostatin-deficient mice
McPherron, A. C., & Lee, S.-J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0213562 · Cited by 505 · see citing works
Hill, J. J., Davies, M. V., Pearson, A. A., Wang, J. H., Hewick, R. M., Wolfman, N. M., & Qiu, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206379200 · Cited by 444 · see citing works
Recombinant ob protein reduces feeding and body weight in the ob/ob mouse.
Weigle, D. S., Bukowski, T. R., Foster, D. C., Holderman, S. D., Kramer, J. M., Lasser, G. W., Lofton–Day, C., Prunkard, D. E., Raymond, C. K., & Kuijper, J. L. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118254 · Cited by 420 · see citing works
Ma, K., Mallidis, C., Bhasin, S., Mahabadi, V., Artaza, J., González-Cadavid, N. F., Arias, J., & Salehian, B. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00487.2002 · Cited by 416 · see citing works
Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells
Taylor, W. E., Bhasin, S., Artaza, J., Byhower, F., Azam, M., Willard, D. H., Kull, F. C., & González-Cadavid, N. F. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.2.e221 · Cited by 410 · see citing works
WAJCHENBERG, B. L., Giannella‐Neto, D., Silva, M., & Santos, R. F. (2002) · Hormone and Metabolic Research · doi:10.1055/s-2002-38256 · Cited by 394 · see citing works
Carlson, C. J., Booth, F. W., & Gordon, S. E. (1999) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1999.277.2.r601 · Cited by 358 · see citing works
Lower skeletal muscle mass in male transgenic mice with muscle-specific overexpression of myostatin
Reisz‐Porszasz, S., Bhasin, S., Artaza, J. N., Shen, R., Sinha‐Hikim, I., Hogue, A., Fielder, T. J., & González-Cadavid, N. F. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00107.2003 · Cited by 333 · see citing works
Myostatin is an inhibitor of myogenic differentiation
Rı́os, R., Carneiro, I., Arce, V. M., & Devesa, J. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00372.2001 · Cited by 324 · see citing works
Myostatin Knockout in Mice Increases Myogenesis and Decreases Adipogenesis
Lin, J., Arnold, H. B., Della-Fera, M. A., Azain, M. J., Hartzell, D. L., & Baile, C. A. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6500 · Cited by 313 · see citing works
Allen, D. L., & Unterman, T. G. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00542.2005 · Cited by 264 · see citing works
Modulation of myostatin expression during modified muscle use
Wehling, M., Cai, B.-Y., & Tidball, J. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.1.103 · Cited by 238 · see citing works
Myostatin modulates adipogenesis to generate adipocytes with favorable metabolic effects
Feldman, B. J., Streeper, R. S., Farese, R. V., & Yamamoto, K. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607501103 · Cited by 210 · see citing works
Ma, K., Mallidis, C., Artaza, J., Taylor, W. E., González-Cadavid, N. F., & Bhasin, S. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.281.6.e1128 · Cited by 208 · see citing works
Leptin Rapidly Lowers Food Intake and Elevates Metabolic Rates in Lean and ob/ob Mice ,
Mistry, A. M., Swick, A. G., & Romsos, D. R. (1997) · The Journal of Nutrition · doi:10.1093/jn/127.10.2065 · Cited by 188 · see citing works
Transgenic expression of myostatin propeptide prevents diet-induced obesity and insulin resistance
Zhao, B., Wall, R. J., & Yang, J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.09.044 · Cited by 186 · see citing works
Roth, S. M., Martel, G. F., Ferrell, R. E., Metter, E. J., Hurley, B. F., & Rogers, M. A. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800609 · Cited by 184 · see citing works
FSTL3 deletion reveals roles for TGF-β family ligands in glucose and fat homeostasis in adults
Mukherjee, A., Sidis, Y., Mahan, A. L., Raher, M. J., Xia, Y. Y., Rosen, E. D., Bloch, K. D., Thomas, M. K., & Schneyer, A. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607966104 · Cited by 157 · see citing works
Different Pathways Regulate Expression of the Skeletal Myosin Heavy Chain Genes
Allen, D. L., Sartorius, C. A., Sycuro, L. K., & Leinwand, L. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108017200 · Cited by 152 · see citing works
Floyd, Z. E., & Stephens, J. M. (2003) · Diabetes · doi:10.2337/diabetes.52.2.308 · Cited by 140 · see citing works
Inhibition of Preadipocyte Differentiation by Myostatin Treatment in 3T3-L1 Cultures
Kim, H., Liang, L., Dean, R. G., Hausman, D. B., Hartzell, D. L., & Baile, C. A. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4435 · Cited by 127 · see citing works
Schroeder‐Gloeckler, J. M., Rahman, S. M., Janssen, R. C., Qiao, L., Shao, J., Roper, M. D., Fischer, S. J., Lowe, E., Orlicky, D. J., McManaman, J. L., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701329200 · Cited by 126 · see citing works
Intracellular Calcium and Myosin Isoform Transitions
Allen, D. L., & Leinwand, L. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208302200 · Cited by 106 · see citing works
Millward, C. A., Heaney, J. D., Sinasac, D. S., Chu, E. C., Bederman, I. R., Gilge, D. A., Previs, S. F., & Croniger, C. M. (2006) · Diabetes · doi:10.2337/db06-0310 · Cited by 103 · see citing works
Myostatin expression in age and denervation-induced skeletal muscle atrophy.
Baumann, A. P., Ibebunjo, C., GRASSER, W. A., & Paralkar, V. M. (2003) · PubMed · Cited by 99 · see citing works
Gene expression in visceral and subcutaneous adipose tissues
Vidal, H. (2001) · Annals of Medicine · doi:10.3109/07853890108995965 · Cited by 97 · see citing works
Jones, R. L. (2002) · Molecular Human Reproduction · doi:10.1093/molehr/8.4.363 · Cited by 88 · see citing works
Tsuchida, K. (2004) · Current Drug Targets - Immune Endocrine & Metabolic Disorders · doi:10.2174/1568008043339901 · Cited by 87 · see citing works
Allen, D. L., Weber, J. N., Sycuro, L. K., & Leinwand, L. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501207200 · Cited by 50 · see citing works
Effect of glycogen synthase overexpression on insulin-stimulated muscle glucose uptake and storage
Fogt, D. L., Pan, S., Lee, S., Ding, Z., Scrimgeour, A. G., Lawrence, J. C., & Ivy, J. L. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00115.2003 · Cited by 48 · see citing works
Seeing the trees in the forest: selective electroporation of adipocytes within adipose tissue
Granneman, J. G., Li, P., Lu, Y., & Tilak, J. P. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00567.2003 · Cited by 46 · see citing works
Yang, J., & Zhao, B. (2006) · Molecular Reproduction and Development · doi:10.1002/mrd.20452 · Cited by 38 · see citing works
Joshi, A. V., Day, D., Lubowski, T. J., & Ambegaonkar, A. J. (2005) · Current Medical Research and Opinion · doi:10.1185/030079905x65231 · Cited by 32 · see citing works
A histochemical and morphological study of skeletal muscle from obese hyperglycaemic ob/ob mice
Almond, R., & Enser, M. B. (1984) · Diabetologia · doi:10.1007/bf00304859 · Cited by 25 · see citing works
Weight loss reduces expression of SREBP1c/ADD1 and PPARγ2 in adipose tissue of obese women
Ribot, J., Rantala, M., Kesäniemi, Y. A., Palou, A., & Savolainen, M. J. (2001) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s004240000454 · Cited by 19 · see citing works
Flagged first, then by citations
2 of the 50 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Muscles, exercise and obesity: skeletal muscle as a secretory organ
Pedersen, B. K., & Febbraio, M. A. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2012.49 · Cited by 2,909 · see citing works
Pedersen, B. K. (2013) · Comprehensive physiology · doi:10.1002/cphy.c120033 · Cited by 516 · see citing works
Guo, T., Jou, W., Chanturiya, T., Portas, J., Gavrilova, O., & McPherron, A. C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004937 · Cited by 402 · see citing works
Leal, L. G., Lopes, M. A., & Batista, M. L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01307 · Cited by 382 · see citing works
“Myostatin mRNA levels increase substantially in genetically-modified obese mice (leptin-deficient ob/ob mice) and also in those receiving a high fat diet (HFD), so both circulating and SkMmyostatin levels are present in obese subjects when compared to non-obese subjects (Allen et al., 2008; Hittel et al., 2009).”
BackgroundBone and muscle: Interactions beyond mechanical
Brotto, M. A. P., & Bonewald, L. F. (2015) · Bone · doi:10.1016/j.bone.2015.02.010 · Cited by 347 · see citing works
The role of myostatin in muscle wasting: an overview
Elkina, Y., von Haehling, S., Anker, S. D., & Springer, J. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0035-5 · Cited by 349 · see citing works
Increased secretion and expression of myostatin in skeletal muscle from extremely obese women
Hittel, D. S., Berggren, J. R., Shearer, J., Boyle, K., & Houmard, J. A. (2009) · Diabetes · doi:10.2337/db08-0943 · Cited by 324 · see citing works
Myokines and Adipokines: Involvement in the Crosstalk between Skeletal Muscle and Adipose Tissue
Li, F., Li, Y., Duan, Y., Hu, C.-A. A., Tang, Y., & Yin, Y. (2017) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2016.10.003 · Cited by 288 · see citing works
Activins and Inhibins: Roles in Development, Physiology, and Disease
Namwanje, M., & Brown, C. W. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021881 · Cited by 294 · see citing works
Myostatin decreases with aerobic exercise and associates with insulin resistance
HITTEL, D. S., AXELSON, M., SARNA, N., SHEARER, J., HUFFMAN, K. M., & KRAUS, W. E. (2010) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3181e0b9a8 · Cited by 271 · see citing works
Myostatin Directly Regulates Skeletal Muscle Fibrosis
Li, Z. B., Kollias, H. D., & Wagner, K. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802585200 · Cited by 259 · see citing works
The effects of obesity on skeletal muscle regeneration
Akhmedov, D., & Berdeaux, R. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00371 · Cited by 241 · see citing works
Genetic deletion of myostatin from the heart prevents skeletal muscle atrophy in heart failure
Heineke, J., Auger-Messier, M., Xu, J., Sargent, M., York, A., Welle, S., & Molkentin, J. D. (2010) · Circulation · doi:10.1161/circulationaha.109.882068 · Cited by 238 · see citing works
The effects of obesity on skeletal muscle contractile function
Tallis, J. A., James, R. S., & Seebacher, F. (2018) · Journal of Experimental Biology · doi:10.1242/jeb.163840 · Cited by 214 · see citing works
Metabolic adaptation in obesity and type ii diabetes: myokines, adipokines and hepatokines
Oh, K.-J., Lee, D., Kim, W., Han, B., Lee, S., & Bae, K.-H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms18010008 · Cited by 210 · see citing works
Expression and function of myostatin in obesity, diabetes, and exercise adaptation
ALLEN, D. L., HITTEL, D. S., & MCPHERRON, A. C. (2011) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3182178bb4 · Cited by 207 · see citing works
Self-citationZamani, N., & Brown, C. (2010) · Endocrine Reviews · doi:10.1210/er.2010-0018 · Cited by 198 · see citing works
Activin signaling as an emerging target for therapeutic interventions
Tsuchida, K., Nakatani, M., Hitachi, K., Uezumi, A., Sunada, Y., Ageta, H., & Inokuchi, K. (2009) · Cell Communication and Signaling · doi:10.1186/1478-811x-7-15 · Cited by 195 · see citing works
Qian, L., Tang, M., Yang, J., Wang, Q., Cai, C., Jiang, S., Li, H., Jiang, K., Gao, P., Ma, D., et al. (2015) · Scientific Reports · doi:10.1038/srep14435 · Cited by 190 · see citing works
Amelioration of muscle wasting by glucagon‐like peptide‐1 receptor agonist in muscle atrophy
Hong, Y., Lee, J. H., Jeong, K. W., Choi, C. S., & Jun, H. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12434 · Cited by 188 · see citing works
Inhibin at 90: From Discovery to Clinical Application, a Historical Review
Makanji, Y., Zhu, J., Mishra, R. K., Holmquist, C., Wong, W. P. S., Schwartz, N. B., Mayo, K. E., & Woodruff, T. K. (2014) · Endocrine Reviews · doi:10.1210/er.2014-1003 · Cited by 187 · see citing works
Muscle‐bone crosstalk and potential therapies for sarco‐osteoporosis
Li, G., Zhang, L., Wang, D., AIQudsy, L., Jiang, J. X., Xu, H., & Shang, P. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28946 · Cited by 166 · see citing works
Hamrick, M. W., Herberg, S., Arounleut, P., He, H.-Z., Shiver, A. L., Qi, R.-Q., Zhou, L., Isales, C. M., & Mi, Q. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.079 · Cited by 157 · see citing works
The effects of a soluble activin type IIB receptor on obesity and insulin sensitivity
Akpan, I., Goncalves, M. D., Dhir, R., Yin, X., Pistilli, E. E., Bogdanovich, S., Khurana, T. S., Ucran, J., Lachey, J., & Ahima, R. S. (2009) · International Journal of Obesity · doi:10.1038/ijo.2009.162 · Cited by 140 · see citing works
Myostatin and its Regulation: A Comprehensive Review of Myostatin Inhibiting Strategies
Baig, M. H., Ahmad, K., Moon, J. S., Park, S.-Y., Ho Lim, J., Chun, H. J., Qadri, A. F., Hwang, Y. C., Jan, A. T., Ahmad, S. S., et al. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.876078 · Cited by 135 · see citing works
Sáinz, N., Rodríguez, A., Catalán, V., Becerril, S., Ramírez, B., Gómez-Ambrosi, J., & Frühbeck, G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006808 · Cited by 135 · see citing works
Myostatin from the heart: local and systemic actions in cardiac failure and muscle wasting
Breitbart, A., Auger‐Messier, M., Molkentin, J. D., & Heineke, J. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00200.2011 · Cited by 131 · see citing works
Mechanisms by Which Skeletal Muscle Myokines Ameliorate Insulin Resistance
Balakrishnan, R., & Thurmond, D. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094636 · Cited by 132 · see citing works
Myostatin: more than just a regulator of muscle mass
Argilés, J. M., Orpí, M., Busquets, S., & López-Soriano, F. J. (2012) · Drug Discovery Today · doi:10.1016/j.drudis.2012.02.001 · Cited by 125 · see citing works
Metabolic Functions of Myostatin and GDF11
McPherron, A. C. (2010) · Immunology Endocrine & Metabolic Agents - Medicinal Chemistry · doi:10.2174/187152210793663810 · Cited by 125 · see citing works
Maurel, D. B., Jähn, K., & Lara-Castillo, N. (2017) · Biomedicines · doi:10.3390/biomedicines5040062 · Cited by 122 · see citing works
Sharma, M., McFarlane, C., Kambadur, R., Kukreti, H., Bonala, S., & Srinivasan, S. (2015) · IUBMB Life · doi:10.1002/iub.1392 · Cited by 116 · see citing works
Endocrine Crosstalk Between Muscle and Bone
Brotto, M. A. P., & Johnson, M. L. (2014) · Current Osteoporosis Reports · doi:10.1007/s11914-014-0209-0 · Cited by 118 · see citing works
Allen, D. L., & Loh, A. S. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00142.2010 · Cited by 111 · see citing works
Family-Based Analysis of Candidate Genes for Polycystic Ovary Syndrome
Ewens, K. G., Stewart, D. R., Ankener, W., Urbanek, M., McAllister, J. M., Chen, C., Baig, K. M., Parker, S. C. J., Margulies, E. H., Legro, R. S., et al. (2010) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2009-2703 · Cited by 110 · see citing works
Wong, C. Y. J., Al‐Salami, H., & Dass, C. R. (2020) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.13359 · Cited by 112 · see citing works
A Novel Therapeutic Approach to Treating Obesity through Modulation of TGFβ Signaling
Koncarevic, A., Kajimura, S., Cornwall-Brady, M. R., Andreucci, A., Pullen, A. E., Sako, D., Kumar, R., Grinberg, A. V., Liharska, K., Ucran, J. A., et al. (2012) · Endocrinology · doi:10.1210/en.2012-1016 · Cited by 109 · see citing works
Role of microRNAs in skeletal muscle hypertrophy
Hitachi, K., & Tsuchida, K. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2013.00408 · Cited by 106 · see citing works
Plasma and Muscle Myostatin in Relation to Type 2 Diabetes
Brandt, C., Nielsen, A. R., Fischer, C. P., Hansen, J. B., Pedersen, B. K., & Plomgaard, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037236 · Cited by 103 · see citing works
New insights into the mechanisms of activin action and inhibition
Walton, K. L., Makanji, Y., & Harrison, C. A. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.06.030 · Cited by 97 · see citing works
Serum Myostatin is Upregulated in Obesity and Correlates with Insulin Resistance in Humans
Amor, M., Itariu, B. K., Moreno-Viedma, V., Keindl, M., Jürets, A., Prager, G., Langer, F., Grablowitz, V., Zeyda, M., & Stulnig, T. M. (2019) · Experimental and Clinical Endocrinology & Diabetes · doi:10.1055/a-0641-5546 · Cited by 93 · see citing works
BMPs and their clinical potentials
Kim, M.-J., & Choe, S. (2011) · BMB Reports · doi:10.5483/bmbrep.2011.44.10.619 · Cited by 92 · see citing works
Subdiaphragmatic vagal afferent nerves modulate visceral pain
Chen, S., Wu, X.-Y., Cao, Z. J., Fan, J., Wang, M., Owyang, C., & Li, Y. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00588.2007 · Cited by 89 · see citing works
Metabolism and the heart: An overview of muscle, fat, and bone metabolism in heart failure
Loncar, G., Fülster, S., von Haehling, S., & POPOVIC, V. M. (2011) · International Journal of Cardiology · doi:10.1016/j.ijcard.2011.09.079 · Cited by 84 · see citing works
Hjorth, M., Pourteymour, S., Görgens, S. W., Langleite, T. M., Lee, S., Holen, T., Gulseth, H. L., Birkeland, K. I., Jensen, J., Drevon, C. A., et al. (2016) · Acta Physiologica · doi:10.1111/apha.12631 · Cited by 83 · see citing works
Bagheri, R., Moghadam, B. H., Church, D. D., Tinsley, G. M., Eskandari, M., Moghadam, B. H., Motevalli, M. S., Baker, J. S., Robergs, R. A., & Wong, A. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.110869 · Cited by 81 · see citing works
Myostatin – The Holy Grail for Muscle, Bone, and Fat?
Buehring, B., & Binkley, N. (2013) · Current Osteoporosis Reports · doi:10.1007/s11914-013-0160-5 · Cited by 79 · see citing works
Mastrocola, R., Collino, M., Nigro, D., Chiazza, F., D’Antona, G., Aragno, M., & Minetto, M. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119587 · Cited by 75 · see citing works
Sheng, R., Cao, M., Song, M., Wang, M., Zhang, Y., Shi, L., Xie, T., Li, Y., Wang, J., & Rui, Y. (2023) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2023.09.007 · Cited by 74 · see citing works
Myostatin Inhibition Prevents Diabetes and Hyperphagia in a Mouse Model of Lipodystrophy
Guo, T., Bond, N. D., Jou, W., Gavrilova, O., Portas, J., & McPherron, A. C. (2012) · Diabetes · doi:10.2337/db11-0915 · Cited by 68 · see citing works
Wetzlich, B., Nyakundi, B. B., & Yang, J. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05120-y · Cited by 70 · see citing works
Lee, S.-J., Lehar, A., Liu, Y., Ly, C. H., Pham, Q.-M., Michaud, M., Rydzik, R., Youngstrom, D. W., Shen, M. M., Kaartinen, V., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2019263117 · Cited by 59 · see citing works
Myokines as possible therapeutic targets in cancer cachexia
Manole, E., Ceafalan, L. C., Popescu, B. O., Dumitru, C., & Bastian, A. E. (2018) · Journal of Immunology Research · doi:10.1155/2018/8260742 · Cited by 60 · see citing works
Pedersen, B. K. (2013) · Comprehensive physiology · doi:10.1002/j.2040-4603.2013.tb00522.x · Cited by 59 · see citing works
Allen, D. L., Cleary, A. S., Lindsay, S. F., Loh, A. S., & Reed, J. M. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00504.2010 · Cited by 59 · see citing works
Liu, X., Bauman, W. A., & Cardozo, C. P. (2018) · Physiological Reports · doi:10.14814/phy2.13837 · Cited by 59 · see citing works
Myokines: Metabolic regulation in obesity and type 2 diabetes
Chen, Z.-T., Weng, Z.-X., Lin, J. D., & Meng, Z.-X. (2024) · Life Metabolism · doi:10.1093/lifemeta/loae006 · Cited by 58 · see citing works
Myostatin — From the Mighty Mouse to cardiovascular disease and cachexia
Dschietzig, T. B. (2014) · Clinica Chimica Acta · doi:10.1016/j.cca.2014.03.021 · Cited by 55 · see citing works
Cleasby, M. E., Jarmin, S., Eilers, W., Elashry, M. I., Andersen, D. K., Dickson, G., & Foster, K. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00586.2013 · Cited by 55 · see citing works
Activins in adipogenesis and obesity
Dani, C. (2012) · International Journal of Obesity · doi:10.1038/ijo.2012.28 · Cited by 53 · see citing works
Allen, D. L., McCall, G. E., Loh, A. S., Madden, M. C., & Mehan, R. S. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00296.2010 · Cited by 53 · see citing works
Qi, H., Ren, J., Ba, L., Song, C., Zhang, Q., Cao, Y., Shi, P., Fu, B., Liu, Y., & Sun, H. (2019) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.12.003 · Cited by 54 · see citing works
Myostatin gene promoter: structure, conservation and importance as a target for muscle modulation
Grade, C. V. C., Mantovani, C. S., & Alvares, L. E. (2019) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-019-0338-5 · Cited by 52 · see citing works
Increased Smad signaling and reduced MRF expression in skeletal muscle from obese subjects
Watts, R., McAinch, A. J., Dixon, J. B., O’Brien, P. E., & Cameron‐Smith, D. (2013) · Obesity · doi:10.1002/oby.20070 · Cited by 50 · see citing works
Arounleut, P., Bowser, M., Upadhyay, S. K., Shi, X., Fulzele, S., Johnson, M. H., Stranahan, A. M., Hill, W., Isales, C. M., & Hamrick, M. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072330 · Cited by 49 · see citing works
Cai, C., Qian, L., Jiang, S., Sun, Y., Wang, Q., Ma, D., Xiao, G., Li, B., Xie, S., Gao, T., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.16822 · Cited by 49 · see citing works
Physical activity and its mechanistic effects on prostate cancer
Wekesa, A., Harrison, M., & Watson, R. W. G. (2015) · Prostate Cancer and Prostatic Diseases · doi:10.1038/pcan.2015.9 · Cited by 47 · see citing works
Bonala, S., Lokireddy, S., McFarlane, C., Patnam, S., Sharma, M., & Kambadur, R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.529925 · Cited by 47 · see citing works
RetractedAllen, D. L., Cleary, A. S., Hanson, A. M., Lindsay, S. F., & Reed, J. M. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00247.2010 · Cited by 44 · see citing works
Chen, M., Han, D., Yang, J., Yang, Y., Ho, H., & Yang, W. (2012) · Human Reproduction · doi:10.1093/humrep/des209 · Cited by 44 · see citing works
Chang, H., Pan, H.-H., Cheng, J., Zhu, Y., & Leung, P. C. K. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.11.009 · Cited by 43 · see citing works
Sanchis‐Gomar, F., López‐López, S., Morales, C. R., Maffulli, N., Lippi, G., & Pareja-Galeano, H. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01463 · Cited by 44 · see citing works
Follistatin-Like Proteins: Structure, Functions and Biomedical Importance
Parfenova, O. K., Kukes, V. G., & Grishin, D. V. (2021) · Biomedicines · doi:10.3390/biomedicines9080999 · Cited by 40 · see citing works
Increased glial glutamate transporter EAAT2 expression reduces visceral nociceptive response in mice
Lin, Y., Tian, G., Roman, K., Handy, C. R., Travers, J. B., Lin, C.-L. G., & Stephens, R. L. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90556.2008 · Cited by 40 · see citing works
Allen, D. L., Uyenishi, J. J., Cleary, A. S., Mehan, R. S., Lindsay, S. F., & Reed, J. M. (2009) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00325.2009 · Cited by 40 · see citing works
Increased circulating myostatin in patients with type 2 diabetes mellitus
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 · see citing works
Wilhelmsen, A., Tsintzas, K., & Jones, S. W. (2021) · GeroScience · doi:10.1007/s11357-021-00322-4 · Cited by 39 · see citing works
Roseno, S. L., Davis, P. R., Bollinger, L. M., Powell, J. J. S., Witczak, C. A., & Brault, J. J. (2015) · Nutrition & Metabolism · doi:10.1186/s12986-015-0037-y · Cited by 36 · see citing works
Bolton, J. L., Montastier, É., Carayol, J., Bonnel, S., Mir, L., Marqués, M.-A., Astrup, A. V., Saris, W. H. M., Iacovoni, J. S., Vialaneix, N., et al. (2017) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2016-3997 · Cited by 35 · see citing works
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 36 · see citing works
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 · see citing works
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 · see citing works
Zarfeshani, A., Ngo, S., & Sheppard, A. M. (2014) · Clinical Epigenetics · doi:10.1186/1868-7083-6-27 · Cited by 32 · see citing works
Kazemi, F. (2015) · Journal of Endocrinological Investigation · doi:10.1007/s40618-015-0373-9 · Cited by 32 · see citing works
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 32 · see citing works
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 · see citing works
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 28 · see citing works
Can Exercise Training Alter Human Skeletal Muscle DNA Methylation?
Garcia, L. A., Bustos, R. Z., Day, S. E., Campos, B., Hamzaoui, Y., Wu, L., Leon, A. D., Krentzel, J., Coletta, R. L., Filippis, E. D., et al. (2022) · Metabolites · doi:10.3390/metabo12030222 · Cited by 28 · see citing works
Founds, S. A., Ren, D., Roberts, J. M., Jeyabalan, A., & Powers, R. W. (2014) · Reproductive Sciences · doi:10.1177/1933719114529372 · Cited by 27 · see citing works
Eilers, W., Chambers, D. J., Cleasby, M. E., & Foster, K. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00185.2019 · Cited by 26 · see citing works
Retraction: Pid1 Induces Insulin Resistance in Both Human and Mouse Skeletal Muscle during Obesity
Bonala, S., McFarlane, C., Ang, J., Lim, R., Lee, M., Chua, H., Lokireddy, S., Patnam, S., Leow, M. K., Meng, K. C., et al. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1048 · Cited by 26 · see citing works
RetractedFighting obesity: When muscle meets fat
Yang, X., Bi, P., & Kuang, S. (2014) · Adipocyte · doi:10.4161/21623945.2014.964075 · Cited by 25 · see citing works
Leptin signaling in skeletal muscle after bed rest in healthy humans
Guerra, B., Ponce-González, J., Morales‐Alamo, D., Guadalupe-Grau, A., Kiilerich, K., Fuentes, T., Ringholm, S., Biensø, R., Santana, A., Lundby, C., et al. (2013) · European Journal of Applied Physiology · doi:10.1007/s00421-013-2779-4 · Cited by 28 · see citing works
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 · see citing works
Crosstalk between bone and other organs
Yuan, W., & Song, C. (2022) · Medical Review · doi:10.1515/mr-2022-0018 · Cited by 25 · see citing works
Guo, W., Wong, S., & Bhasin, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071017 · Cited by 24 · see citing works
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 · see citing works
Legaard, G. E., & Pedersen, B. K. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-814593-7.00013-x · Cited by 24 · see citing works
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 · see citing works
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 · see citing works
- 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)
- 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
- 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 › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Health Sciences › Medicine › Physiology › 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review