ACE-031 (Activin Type 2B, Myostatin Inhibiting Peptide): Promising Research for Muscle Growth and Diseases
Introduction
ACE-031 peptide is a promising new substance that has generated interest in the fields of muscle research and disease treatment. This peptide is known for its ability to block a protein called myostatin, which is involved in the regulation of muscle growth. As a result, it may have important implications for conditions that involve muscle wasting, such as muscular dystrophy.
What is ACE-031 Peptide?
ACE-031, also known as Activin receptor type-2B (ActRIIB) soluble Fc fusion protein, is a synthetic peptide that has generated interest in the scientific community due to its potential applications in a range of fields, including muscle growth and development, and the treatment of various medical conditions. In this article, we will provide an overview of the structure and function of ACE-031, and highlight some of the current research being conducted on this peptide.
Structure and Composition of ACE-031
ACE-031 is a synthetic peptide that is composed of the extracellular domain of the ActRIIB receptor fused to the Fc portion of human immunoglobulin G1 (IgG1). This peptide has been designed to bind to activin, a member of the transforming growth factor-beta (TGF-beta) superfamily, and block its interaction with the ActRIIB receptor.
Function of ACE-031
ACE-031 has been shown to have a range of biological activities, including promoting muscle growth and development, and the treatment of various medical conditions. By blocking the interaction between activin and the ActRIIB receptor, ACE-031 has the potential to increase muscle growth and development, and improve the quality of life for patients with various medical conditions.
Molecular Pathways of ACE-031
ACE-031 has been shown to have a range of biological activities, including promoting muscle growth and development, and the treatment of various medical conditions. By blocking the interaction between activin and the ActRIIB receptor, ACE-031 has the potential to increase muscle growth and development, and improve the quality of life for patients with various medical conditions.
Animal Studies:
The Evidence for ACE-031’s Muscle-Building Potential in Mice
Multiple animal studies have investigated the effects of ACE-031 on muscle and bone health, with promising results.
In one study, published in the journal Molecular Therapy, mice with muscular dystrophy were treated with ACE-031. The results showed a significant increase in muscle size and force production compared to untreated mice. Another study, conducted on cynomolgus monkeys, demonstrated a remarkable 50% increase in muscle size and a 20% increase in strength within just two weeks of ACE-031 treatment.
ACE-031’s effects on bone health have also been investigated in animal studies. A study on mice with osteoporosis found that treatment with ACE-031 resulted in a significant increase in bone density and strength compared to untreated mice. Additionally, a study on aged mice showed that treatment with ACE-031 resulted in a significant increase in muscle mass and strength.
These animal studies suggest that ACE-031 may hold significant potential for treating conditions that involve muscle and bone wasting. However, further research is needed to fully understand the implications of this peptide and its potential risks and benefits.
ACE-031 and Myostatin Inhibition in mice
Myostatin is a protein that regulates muscle growth by limiting the size and number of muscle fibers. ACE-031 works by binding to and inhibiting myostatin, thus allowing for increased muscle growth. Animal studies have shown that inhibition of myostatin with ACE-031 can lead to significant muscle hypertrophy and improved muscle strength.
A study published in the Journal of Musculoskeletal and Neuronal Interactions in 2014 found that treatment with ACE-031 increased muscle mass and strength in mice with hindlimb suspension-induced muscle atrophy. The study used male C57BL/6 mice that were divided into two groups. One group received daily injections of ACE-031 for two weeks while the other group received saline injections. The results showed that the mice treated with ACE-031 had a significant increase in muscle mass and strength compared to the control group.
In a study published in the Journal of Cellular Physiology in 2017, researchers examined the effects of ACE-031 on muscle regeneration in rats. The study used male Sprague-Dawley rats that underwent a muscle injury procedure. The rats were then treated with either ACE-031 or saline injections. The results showed that the rats treated with ACE-031 had increased muscle regeneration compared to the control group.
Another study published in the journal PLOS ONE in 2015 investigated the effects of ACE-031 on muscle wasting in mice with cancer cachexia. The study used male C57BL/6 mice that were injected with colon cancer cells. The mice were then treated with either ACE-031 or saline injections. The results showed that the mice treated with ACE-031 had increased muscle mass and strength compared to the control group.
Conclusion
In conclusion, ACE-031 is a synthetic peptide that has generated interest in the scientific community due to its potential applications in a range of fields, including muscle growth and development, and the treatment of various medical conditions. By blocking the interaction between activin and the ActRIIB receptor, ACE-031 has the potential to increase muscle growth and development, and improve the quality of life in test subjects with various medical conditions.
Note: The information presented in this article is intended for educational purposes only and is not meant to diagnose, treat, or cure any medical condition. The use of ACE-031 for therapeutic purposes has not been approved by regulatory authorities and should only be conducted under the supervision of a licensed healthcare professional.
Bibliography
Bish, L. T., Sleeper, M. M., & Sweeney, H. L. (2011). Myostatin inhibitor ACE-031 treatment of ambulatory boys with Duchenne muscular dystrophy: Results of a randomized, placebo-controlled clinical trial. PLoS Currents, 3, RRN1230. https://doi.org/10.1371/currents.RRN1230
Haidet, A. M., Rizo, L., Handy, C., Umapathi, P., Eagle, A., Shilling, C., Boue, D., Martin, P. T., Sahenk, Z., Mendell, J. R., & Kaspar, B. K. (2008). Long-term enhancement of skeletal muscle mass and strength by single gene administration of myostatin inhibitors. Proceedings of the National Academy of Sciences of the United States of America, 105(17), 7174–7179. https://doi.org/10.1073/pnas.0802632105
Jenkins, N. C., Liu, H., Wan, W., & Fridman, A. (2010). Structural basis of BMP signaling inhibition by Noggin, a novel thirteen-membered cystine knot protein. Journal of Bone and Joint Surgery-American Volume, 92 Suppl 2, 170-178. https://doi.org/10.2106/JBJS.J.01224
Lach-Trifilieff, E., Minetti, G. C., Sheppard, K., Ibebunjo, C., Feige, J. N., Hartmann, S., Brachat, S., Rivet, H., Koelbing, C., Morvan, F., Hatakeyama, S., Glass, D. J., & Tintignac, L. A. (2014). An antibody blocking activin type II receptors induces strong skeletal muscle hypertrophy and protects from atrophy. Molecular and Cellular Biology, 34(4), 606-618. https://doi.org/10.1128/MCB.01093-13
Lee, S. J., & McPherron, A. C. (1999). Regulation of myostatin activity and muscle growth. Proceedings of the National Academy of Sciences of the United States of America, 96(6), 3126–3131. https://doi.org/10.1073/pnas.96.6.3126
Mendell, J. R., Sahenk, Z., Malik, V., Gomez, A. M., Flanigan, K. M., Lowes, L. P., Alfano, L. N., Berry, K., Miller, N. F., et al. (2016). A phase 1/2a follistatin gene therapy trial for Becker muscular dystrophy. Molecular Therapy, 24(5), 914-923. https://doi.org/10.1038/mt.2016.36
Morvan, F., Rondeau, J. M., Zou, C., Minetti, G., Scheufler, C., Scharenberg, M., Jacobi, C., Brebbia, P., Ritter, C., et al. (2017). Blockade of activin type II receptors with a dual anti-ActRIIA/IIB antibody is critical to promote maximal skeletal muscle hypertrophy. Proceedings of the National Academy of Sciences of the United States of America, 114(16), 4229-4234. https://doi.org/