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Role of myostatin protein in sarcopenia (aging muscle) after conditioned medium umbilical cord mesenchymal stem cells (secretome) therapy: mini review

Abstract

Umbilical Cord Mesenchyme stem cell (UC-MSCs) /secretome has been applied for treating several diseases, such as cardio-protection and diabetes. Secretome-derived paracrine modulating effects of various growth factors, cytokines, chemokines, angiogenic factors, and exosomes are used in aging therapy. In recent clinical trials on sarcopenia therapy such as pharmaceutical interventions, nutrition, and physical exercise are reported to be effective strategies to reduce sarcopenia.

The pathomechanism of the secretome in the treatment of sarcopenia is unclear. This study looked into how secretome might affect myostatin, a biomarker of sarcopenia, at the molecular level. Myostatin, a member of the TGF-family, significantly increases muscle growth when it is absent while suppressing muscle growth when it is present. A bioactive substance called secretome is secreted by MSCs in conditioned conditions. It is rich in growth factors and cytokines, which are crucial for speeding up tissue regeneration. Secretome intervention is a promising approach for treating sarcopenia as showed by its ability to prevent muscle loss and to improve molecular biomarkers.

References

  1. Sjöström M, Lexell J, Downham DY. Differences in fiber number and fiber type proportion within fascicles. A quantitative morphological study of whole vastus lateralis muscle from childhood to old age. Anat Rec. 1992;234(2):183–9. Available from: http://dx.doi.org/10.1002/ar.1092340205
  2. Rosenberg IH. Sarcopenia: Origins and Clinical Relevance. J Nutr. 1997;127(5):990S-991S. Available from: http://dx.doi.org/10.1093/jn/127.5.990s
  3. Beaudart C, Zakaria M, Pasleau F, Reginster J-Y, Bruyère O. Health Outcomes of Sarcopenia: A Systematic Review and Meta-Analysis. PLoS One. 2017;12(1):e0169548–e0169548. Available from: https://pubmed.ncbi.nlm.nih.gov/28095426
  4. Yarasheski KE, Bhasin S, Sinha-Hakim I, Pak-Loduca J, Gonzalez-Cadavid NF. Serum myostatin-immunoreactive protein is increased in 60-92 year old women and men with muscle wasting. J Nutr Health Aging. 2002;6(5):343–8.
  5. Carnac G, Vernus B, Bonnie A. Myostatin in the pathophysiology of skeletal muscle. Curr Genomics. 2007;8(7):415–22. Available from: https://pubmed.ncbi.nlm.nih.gov/19412331
  6. Han HQ, Mitch WE. Targeting the myostatin signaling pathway to treat muscle wasting diseases. Curr Opin Support Palliat Care. 2011;5(4):334–41. Available from: https://pubmed.ncbi.nlm.nih.gov/22025090
  7. Rebbapragada A, Benchabane H, Wrana JL, Celeste AJ, Attisano L. Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis. Mol Cell Biol. 2003;23(20):7230–42. Available from: https://pubmed.ncbi.nlm.nih.gov/14517293
  8. Saneyasu T, Honda K, Kamisoyama H. Myostatin Increases Smad2 Phosphorylation and Atrogin-1 Expression in Chick Embryonic Myotubes. J Poult Sci. 2019;56(3):224–30. Available from: https://pubmed.ncbi.nlm.nih.gov/32055218
  9. McPherron AC, Lawler AM, Lee S-J. Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member. Nature. 1997;387(6628):83–90. Available from: http://dx.doi.org/10.1038/387083a0
  10. Sharma M, Kambadur R, Matthews KG, Somers WG, Devlin GP, Conaglen J V, et al. Myostatin, a transforming growth factor-? superfamily member, is expressed in heart muscle and is upregulated in cardiomyocytes after infarct. J Cell Physiol. 1999;180(1):1–9. Available from: http://dx.doi.org/10.1002/(sici)1097-4652(199907)180:1%3C1::aid-jcp1%3E3.0.co
  11. Kazemi F. The correlation of resistance exercise-induced myostatin with insulin resistance and plasma cytokines in healthy young men. J Endocrinol Invest. 2015;39(4):383–8. Available from: http://dx.doi.org/10.1007/s40618-015-0373-9
  12. Han HQ, Zhou X, Mitch WE, Goldberg AL. Myostatin/activin pathway antagonism: Molecular basis and therapeutic potential. Int J Biochem & Cell Biol. 2013;45(10):2333–47. Available from: http://dx.doi.org/10.1016/j.biocel.2013.05.019
  13. Bergen 3rd HR, Farr JN, Vanderboom PM, Atkinson EJ, White TA, Singh RJ, et al. Myostatin as a mediator of sarcopenia versus homeostatic regulator of muscle mass: insights using a new mass spectrometry-based assay. Skelet Muscle. 2015;5:21. Available from: https://pubmed.ncbi.nlm.nih.gov/26180626
  14. Consitt LA, Clark BC. The Vicious Cycle of Myostatin Signaling in Sarcopenic Obesity: Myostatin Role in Skeletal Muscle Growth, Insulin Signaling and Implications for Clinical Trials. J frailty aging. 2018;7(1):21–7. Available from: https://pubmed.ncbi.nlm.nih.gov/29412438
  15. Attie KM, Borgstein NG, Yang Y, Condon CH, Wilson DM, Pearsall AE, et al. A single ascending-dose study of muscle regulator ace-031 in healthy volunteers. Muscle & Nerve. 2012;47(3):416–23. Available from: http://dx.doi.org/10.1002/mus.23539
  16. Wilkes JJ, Lloyd DJ, Gekakis N. Loss-of-function mutation in myostatin reduces tumor necrosis factor alpha production and protects liver against obesity-induced insulin resistance. Diabetes. 2009/02/10. 2009;58(5):1133–43. Available from: https://pubmed.ncbi.nlm.nih.gov/19208906
  17. Tu P, Bhasin S, Hruz PW, Herbst KL, Castellani LW, Hua N, et al. Genetic disruption of myostatin reduces the development of proatherogenic dyslipidemia and atherogenic lesions in Ldlr null mice. Diabetes. 2009/06/09. 2009;58(8):1739–48. Available from: https://pubmed.ncbi.nlm.nih.gov/19509018
  18. El Shafey N, Guesnon M, Simon F, Deprez E, Cosette J, Stockholm D, et al. Inhibition of the myostatin/Smad signaling pathway by short decorin-derived peptides. Exp Cell Res. 2016;341(2):187–95. Available from: http://dx.doi.org/10.1016/j.yexcr.2016.01.019

How to Cite

Ronald Winardi Kartika, Veronika Maria Sidharta, Djuartina, T., Rika, I., Cynthia Retna Sartika, & Kris Herawan Timotius. (2022). Role of myostatin protein in sarcopenia (aging muscle) after conditioned medium umbilical cord mesenchymal stem cells (secretome) therapy: mini review. Bali Medical Journal, 12(1), 7–10. https://doi.org/10.15562/bmj.v12i1.3790

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Ronald Winardi Kartika
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Veronika Maria Sidharta
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Tena Djuartina
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Ignatio Rika
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Cynthia Retna Sartika
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Kris Herawan Timotius
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