Studies on the Connection Between Follistatin and Cell Proliferation

This article will focus on the Follistatin-344 peptide and the multiple cell proliferation studies conducted over the years.

Muscle cells are considered to secrete a protein called myostatin, which may block other muscle cells from dividing and developing. Studies suggest Follistatin may block its activity as it is contributed to the family of TGF-beta proteins. Animals deficient in myostatin have been suggested to have much more muscle mass and strength than typical. Because of this finding, researchers theorized that Follistatin might boost muscle growth and aid in mitigating the effects of various dysfunctions that affect muscle development and strength, such as muscular dystrophy.

Follistatin has been suggested to enhance lean muscle mass in mouse models without requiring adjustments to the mice’s diet or exercise routine. Muscle mass in mice given the peptide appeared to increase by 10% in only eight weeks after Follistatin compared to control animals [i]. Again, this is a result reached without exercising the mice or exposing them to specific diets, suggesting that much greater improvements are possible with proper training.

Studies on animals as diverse as mice and monkeys have suggested that Follistatin may increase muscle growth and strength. Follistatin has been speculated to increase skeletal muscle growth and decrease inflammation and fibrosis in Duchenne muscular dystrophy (DMD) animal models. 

Gene delivery of Follistatin at any age may result in long-term properties on muscular hypertrophy, as suggested by studies looking into the action of Follistatin in muscle development. 

The research literature suggests Follistatin may stimulate muscle development due to a potential impact on the insulin/IGF-1 pathway. Interestingly, the researchers suggest the protein’s real anabolic impact only requires the presence of a single one of these signaling molecules. Researchers were puzzled by Follistatin’s apparent potential to reduce IGF-1 expression in muscles until they realized that Follistatin’s actions might also be mediated via insulin [ii]. Studies have suggested that Follistatin may stimulate insulin production in the pancreas, linking the protein closely to insulin signaling.

Follistatin and the Esophagus

The development of Barrett’s esophagus, a precancerous condition, from otherwise healthy esophageal tissue has been linked to bone morphogenic protein (BMP). Barrett’s esophagus may be avoided, research suggests, by counteracting the over-activation of BMP in the esophagus, which occurs due to acid reflux.

Several types of cancer have a reported similar feature: BMP misregulation. Defects in BMP signaling, for instance, have reportedly displayed a role in the development of colon cancer. Follistatin may exhibit potential preventative action in BMP misregulation, but more study is needed.

Follistatin and Cell Proliferation

Studies suggest Follistatin may encourage cell growth and limit metastasis. It turns out that this seeming contradiction in Follistatin is widespread. Research suggests hepatocytes found in the liver can only divide and multiply if Follistatin is expressed. Researchers speculate proliferation may need activin to be inactive by Follistatin [iii]. Researchers suggest this may be a possible explanation of Follistatin studies reporting tumor development and other studies reporting inhibition of tumor invasion and spread. During development, scientists consider cells to be consciously deciding to divert resources away from their mobile capabilities and onto their capacity for growth and reproduction.

Follistatin and the Liver  

Research suggests liver fibrosis may be prevented or delayed by Follistatin. After four weeks of Follistatin introduction to rat test models, fibrosis appeared to be reduced by 32% in a rat study [iv], a property thought to be due to a decrease of 87% in the mortality of hepatocytes in the test groups. The transition from liver fibrosis to cancer has been related to Follistatin dysregulation [v].

Follistatin and Congenital Blindness

The capacity to fuse the optic nerve in early development is considered to be essential for vision. TGF-beta signaling’s importance in extracellular matrix remodeling and optic nerve fusion has been considered for some time. The suppression of ocular fusion and subsequent blindness has been linked to elevated levels of TGF-beta proteins, including bone morphogenic protein (BMP). By blocking these proteins’ activity, the risk of blindness may be drastically reduced and the optic nerve preserved [vi]. In order to guarantee proper optic nerve fusion during pregnancy, a preliminary study is investigating the potential properties of Follistatin supplementation throughout crucial development phases on test models.

Follistatin and Hair 

Studies suggest that Follistatin, especially when combined with external hair-growth compounds, may lead to dramatic increases in hair density. In a small study with just 26 subjects, researchers speculated that hair density appeared to increase by 20% and thickness by approximately 13%. [vii]

More investigation is required to explore its potential in scientific research, and these studies must continue. Only academic and scientific institutions can handle peptides. If you are a licensed academic interested in peptides, visit the  CorePeptides.com.  Please be aware that none of the compounds mentioned are approved for human or animal consumption. Laboratory research compounds are only for in-vitro and in-lab use. Any kind of physical introduction is illegal. Only authorized professionals and working scientists may make purchases. The content of this piece is intended only for instructional purposes.

References

[i] C. Schumann et al., “Increasing lean muscle mass in mice via nanoparticle-mediated hepatic delivery of follistatin mRNA,” Theranostics, vol. 8, no. 19, pp. 5276–5288, Oct. 2018.

[ii] C. Barbé et al., “Role of IGF-I in follistatin-induced skeletal muscle hypertrophy,” Am. J. Physiol. – Endocrinol. Metab., vol. 309, no. 6, pp. E557–E567, Sep. 2015.

[iii] H. Ooe et al., “Proliferation of rat small hepatocytes requires follistatin expression,” J. Cell. Physiol., vol. 227, no. 6, pp. 2363–2370, Jun. 2012.

[iv] S. Patella, D. J. Phillips, J. Tchongue, D. M. de Kretser, and W. Sievert, “Follistatin attenuates early liver fibrosis: effects on hepatic stellate cell activation and hepatocyte apoptosis,” Am. J. Physiol. Gastrointest. Liver Physiol., vol. 290, no. 1, pp. G137-144, Jan. 2006.

[v] M. Grusch et al., “Deregulation of the activin/follistatin system in hepatocarcinogenesis,” J. Hepatol., vol. 45, no. 5, pp. 673–680, Nov. 2006.

[vi] M. D. Knickmeyer et al., “TGFβ-facilitated optic fissure fusion and the role of bone morphogenetic protein antagonism,” Open Biol., vol. 8, no. 3, 2018.

[vii] M. P. Zimber et al., “Hair regrowth following a Wnt- and follistatin containing treatment: safety and efficacy in a first-in-man phase 1 clinical trial,” J. Drugs Dermatol. JDD, vol. 10, no. 11, pp. 1308–1312, Nov. 2011.

Disclaimer: The views and opinions expressed in the above article are independent professional judgment of the experts and The Tribune does not take any responsibility, in any manner whatsoever, for the accuracy of their views. This should not be considered as a substitute for medical advice. Please consult your physician for more details. Follistatin-344 shall solely liable for the correctness, reliability of the content and/or compliance of applicable laws. The above is non-editorial content and The Tribune does not vouch, endorse or guarantee any of the above content, nor is it responsible for them in any manner whatsoever. Please take all steps necessary to ascertain that any information and content provided is correct, updated, and verified.