What is The Connection Between Follistatin-344 and Muscle?
Studies suggest Follistatin 344 is a peptide that is believed to inhibit the activity of myostatin, a protein that regulates muscle growth.
Follistatin 344 is a synthetic variant of endogenous Follistatin. The protein in question is composed of a total of 323 amino acids and is classified as a glycoprotein due to the presence of a carbohydrate chain that is covalently attached to its core structure. It is noteworthy that this protein occurs naturally in this form.
Studies suggest Follistatin is a glycoprotein that is synthesized by folliculostellate cells (FS) situated in the anterior pituitary gland and operates through the autocrine signaling pathway.
Researchers speculate the composition of Follistatin 344’s amino acids may exhibit an atypical abundance of cysteine, which is classified as a non-essential amino acid. The key characteristic property of Follistatin 344 may be attributed to cysteine.
Follistatin Peptide Mechanism of Action
Studies suggest Follistatin 344 may employ various mechanisms to elicit targeted physiological alterations within the body. The protein Myostatin [i], which belongs to the growth and differentiation factor family, is synthesized by myocytes, also known as muscle cells. The principal role of myostatin is to function as a regulatory protein that restricts the hypertrophy of skeletal muscles, thereby preventing aberrant growth.
Research suggests Follistatin 344 may function as a suppressor of myostatin. Scientists hypothesize the inhibition of myostatin activity may be achieved through the subsequent blocking of myostatin by Follistatin 344 [ii]. Therefore, it can be concluded that myostatin is not capable of functioning as a highly effective inhibitor of muscle growth.
Activin proteins have been observed to augment the secretion of follicle-stimulating hormone (FSH). Elevated levels of follicle-stimulating hormone (FSH) in male test subjects have been suggested to impede muscle hypertrophy and disrupt normal testicular function. Studies suggest the inhibition of activin by Follistatin 344 may lead to a reduction in hormone secretion.
Researchers speculate Follistatin 344 may exert its action on the granulosa cells, thereby eliciting the release of progesterone [iii]. Given that progesterone is a key hormone involved in the regulation of the menstrual cycle, even minor fluctuations in its levels can disrupt the entire cycle.
While there is currently no empirical evidence from trials to corroborate these findings, research conducted on animals suggests that Follistatin may impede the proliferation and lifespan of cancerous cells, thereby mitigating the likelihood of metastasis [iv].
Follistatin 344 Peptide Properties
Studies suggest the properties of Follistatin 344 can be anticipated upon comprehending the mechanism of action that is pursued by Follistatin 344.
Scientists hypothesize the inhibition of myostatin activity by Follistatin 344 may lead to an augmentation in the growth of muscle fibers within the organism. Consequently, an increase in the growth of muscle cells may lead to a corresponding increase in overall muscle mass, thereby resulting in a significant enhancement of strength.
A study conducted on mice lacking myostatin suggested a significant augmentation of muscle fibers by 117%. The researchers implied that Follistatin 344 may operate through alternative mechanisms to enhance muscle hypertrophy.
Skeletal muscle fibrosis may arise as a consequence of heightened myostatin activity [v]. Researchers speculate the presentation of Follistatin 344 has the potential to mitigate the likelihood of the onset of said disorder.
Studies conducted on mice have speculated a noteworthy decrease in adipose tissue accumulation. This phenomenon may be associated with the potential of Follistatin 344 to inhibit myostatin.
Follistatin 344 has also been speculated to exhibit a capacity for retarding the progression of reproductive senescence through its interaction with activin.
The glycoprotein in question may play a regulatory role in the ovulation process by interacting with granulosa cells, thereby inducing the release of progesterone.
Biochemical analysis suggests seminal fluid is found to be abundant in Follistatin. Therefore, researchers posit that the presentation of Follistatin 344 may have the potential to enhance fertility in test subjects.
The findings of studies conducted on mice suggest that Follistatin 344 may have the potential to mitigate the effects of certain types of cancer, representing a significant breakthrough.
Follistatin 344 and Breast Cancer.
A recent clinical study conducted on mice suggested that Follistatin may have the potential to impede the metastatic progression of lung and ovarian cancer.
Furthermore, it is suggested that the peptide may facilitate rapid and efficacious recuperation subsequent to the surgical removal of tumors in organs such as the liver [vi].
A clinical trial was conducted with Follistatin 344. Remarkably, the test subjects appeared to exhibit a significant increase in hair density. The presentation of Follistatin 344 may have the potential to result in increased follicle density, leading to thicker and denser hair, as hypothesized by researchers.
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References
[i] Elkina Y, von Haehling S, Anker SD, Springer J. The role of myostatin in muscle wasting: an overview. J Cachexia Sarcopenia Muscle. 2011 Sep;2(3):143-151. doi: 10.1007/s13539-011-0035-5. Epub 2011 Jul 26. PMID: 21966641; PMCID: PMC3177043.
[ii] Kota J, Handy CR, Haidet AM, Montgomery CL, Eagle A, Rodino-Klapac LR, Tucker D, Shilling CJ, Therlfall WR, Walker CM, Weisbrode SE, Janssen PM, Clark KR, Sahenk Z, Mendell JR, Kaspar BK. Follistatin gene delivery enhances muscle growth and strength in nonhuman primates. Sci Transl Med. 2009 Nov 11;1(6):6ra15. doi: 10.1126/scitranslmed.3000112. PMID: 20368179; PMCID: PMC2852878.
[iii] Findlay JK. An update on the roles of inhibin, activin, and follistatin as local regulators of folliculogenesis. Biol Reprod. 1993 Jan;48(1):15-23. doi: 10.1095/biolreprod48.1.15. PMID: 8418903.
[iv] Wallner C, Drysch M, Becerikli M, Jaurich H, Wagner JM, Dittfeld S, Nagler J, Harati K, Dadras M, Philippou S, Lehnhardt M, Behr B. Interaction with the GDF8/11 pathway reveals treatment options for adenocarcinoma of the breast. Breast. 2018 Feb;37:134-141. doi: 10.1016/j.breast.2017.11.010. Epub 2017 Nov 20. PMID: 29156385.
[v] Mahdy MAA. Skeletal muscle fibrosis: an overview. Cell Tissue Res. 2019 Mar;375(3):575-588. doi: 10.1007/s00441-018-2955-2. Epub 2018 Nov 12. PMID: 30421315.
[vi] Kogure K, Zhang YQ, Kanzaki M, Omata W, Mine T, Kojima I. Intravenous administration of follistatin: delivery to the liver and effect on liver regeneration after partial hepatectomy. Hepatology. 1996 Aug;24(2):361-6. doi: 10.1002/hep.510240212. PMID: 8690405.
