Almost all tissues are considered by scientists to exhibit the presence of a naturally occurring glycoprotein called Follistatin-344. When a cell creates a chemical messenger in response to a signal, it may attach to its autocrine receptors and causes the cell to change. [i] Two forms of Follistatin are found in nature, designated FST 317 and FST 344, with corresponding amino acid sequences 317 and 344. These two variants might originate from an alternate mRNA splicing mechanism. [ii]
Studies suggest that synthetic Follistatin-344 may mimic the natural protein isoform of the same name. Follistatin isoforms vary in the number of amino acids they contain, but at their core, all Follistatin proteins consist of 63 amino acid residues organized into three domains called FSD1, FSD2, and FSD3. [iii]
Follistatin-344 Peptide Overview
Researchers speculate that Follistatin’s main potential impact is in activin binding. [iv] Studies suggest Follistatin and other substances like activin and inhibins have been proposed to have a collaborative role in reproductive functioning. Follicles in the ovary are thought to secrete activin primarily to stimulate the production of follicle-stimulating hormone. Researchers suggest that Follistatin may bind to activin, thereby reducing the hormone’s ability to suppress FSH release.
Follistatin-344 has been hypothesized to be created locally in the pituitary gland, gonads, testes, and ovaries, while its precise origin and mechanism remain unknown. Follistatin, secreted by the blood vessels, may also be widely transported to other organs and present in the blood circulation.
Follistatin-344 Research and Clinical Investigations
Follistatin-344 and Muscle
Myostatin thought to be generated by muscle cells, may inhibit the differentiation and development of muscle cells. Studies suggest the TGF-beta family of proteins, which includes myostatin, may be inhibited by Follistatin. One research from 1997 [v] suggested that increased skeletal muscle mass and overall weight in mice given Follistatin-344 might be due to decreased myostatin levels.
Another research [vi] used a nanoparticle-mediated method of mRNA delivery in the liver to stimulate Follistatin-344 expression in animals. The hepatic liver cells’ natural synthesis and secretion of Follistatin were suggested to have been stimulated by the mRNA messenger. The findings speculated the blood levels of Follistatin in the peptide animals appeared significantly higher than those in the control mice to the mRNA-containing nanoparticle was given.
Follistatin-344 and Cell Division
Studies suggest Follistatin has a paradoxical mechanism of action in that it has been suggested to suppress metastasis and stimulate cell growth. This is why the peptide is the subject of study in investigations into carcinogenesis and tumor dissemination. [vii] Hepatocytes (liver cells) may need Follistatin to divide, as suggested by the findings of a recent study. Researchers hypothesized that Follistatin-344 may have inactivated activin in experimental rats, suggesting that activin inactivation may be necessary for cell growth. They hypothesized that cells might exchange energy with one another, diverting migratory energy to growth and proliferation.
Follistatin-344 and the Liver
Only one study [viii] on the possible action of Follistatin on pre-existing liver fibrosis was considered statistically significant. This research split rats into control, and Follistatin delivered groups for four weeks. The findings suggested that compared to the control group, liver fibrosis, most often caused by inflammation, injury or infection, seemed to be reduced by 32% in the peptide group. Researchers also suggested that hepatocytic apoptosis appeared to be reduced by about 90% in the Follistatin animals.
Follistatin-344 and Hair
Research suggests that by possibly stimulating interfollicular stem cells, Follistatin may exhibit some wound-healing capacity and contribute to enhanced hair growth. Hair Stimulating Complex (HSC) is a synthetic protein composition whose action on balding was investigated in a clinical trial [viii]. For 52 weeks, 26 subjects were exposed to the peptide. The histopathological analysis of the tissues suggested hair growth was better than in placebo subjects. Researchers speculated that in addition to hair growth, there seemed to be an increase in hair thickness and density of about 13%.
Follistatin-344 and Diabetes
Studies on diabetic mice suggest that presenting them with Follistatin-344 may increase the number of pancreatic beta cells, decrease blood sugar levels, and mitigate other disease symptoms by possible overexpression of the protein in the pancreatic cells. [ix]
More investigation is required to explore its potential in scientific research, and these studies must continue. Only academic and scientific institutions are allowed to use Follistatin-344 peptides. If you are a licensed professional interested in buyingpeptides for your clinical studies, click here to be redirected to the Biotech Peptides website. Please note that none of the items mentioned are approved for human or animal ingestion. 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] Hiroyuki Kaneko, Handbook of Hormones, 2016. https://www.sciencedirect.com/topics/neuroscience/follistatin
[ii] FST follistatin [Homo sapiens (human)]. https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=DetailsSearch&Term=10468
[iii] Shi, L., Resaul, J., Owen, S., Ye, L., & Jiang, W. G. (2016). Clinical and Therapeutic Implications of Follistatin in Solid Tumours. Cancer genomics & proteomics, 13(6), 425–435. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5219916/
[iv] Rodino-Klapac, L. R., Haidet, A. M., Kota, J., Handy, C., Kaspar, B. K., & Mendell, J. R. (2009). Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease. Muscle & nerve, 39(3), 283–296. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2717722/
[v] McPherron AC, Lawler AM, Lee SJ. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature. 1997 May 1;387(6628):83-90. https://pubmed.ncbi.nlm.nih.gov/9139826/
[vi] Schumann C, Nguyen DX, Norgard M, Bortnyak Y, Korzun T, Chan S, Lorenz AS, Moses AS, Albarqi HA, Wong L, Michaelis K, Zhu X, Alani AWG, Taratula OR, Krasnow S, Marks DL, Taratula O. Increasing lean muscle mass in mice via nanoparticle-mediated hepatic delivery of follistatin mRNA. Theranostics 2018; 8(19):5276-5288. doi:10.7150/thno.27847. https://www.thno.org/v08p5276.htm
[vii] Ooe H, Chen Q, Kon J, Sasaki K, Miyoshi H, Ichinohe N, Tanimizu N, Mitaka T. Proliferation of rat small hepatocytes requires follistatin expression. J Cell Physiol. 2012 Jun;227(6):2363-70. https://pubmed.ncbi.nlm.nih.gov/21826650/
[viii] Zimber MP, Ziering C, Zeigler F, Hubka M, Mansbridge JN, Baumgartner M, Hubka K, Kellar R, Perez-Meza D, Sadick N, Naughton GK. Hair regrowth following a Wnt- and follistatin containing treatment: safety and efficacy in a first-in-man phase 1 clinical trial. J Drugs Dermatol. 2011 Nov;10(11):1308-12. https://pubmed.ncbi.nlm.nih.gov/22052313/
[ix] Zhao C, Qiao C, Tang RH, Jiang J, Li J, Martin CB, Bulaklak K, Li J, Wang DW, Xiao X. Overcoming Insulin Insufficiency by Forced Follistatin Expression in β-cells of db/db Mice. Mol Ther. 2015 May;23(5):866-874. doi: 10.1038/mt.2015.29. Epub 2015 Feb 13. PMID: 25676679; PMCID: PMC4427879. https://pubmed.ncbi.nlm.nih.gov/25676679/
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