MGF

MGF Peptide

Mechano Growth Factor (MGF) is a naturally occurring splice variant of the insulin-like growth factor-1 (IGF-1) gene, expressed in response to mechanical stress or muscle damage. It is a synthetic peptide corresponding to the unique E-domain of the IGF-1 gene transcript, comprising 24 amino acids. Researchers suggest that MGF may play a role in the activation and proliferation of satellite cells, which are key to muscle repair and regeneration processes in experimental systems.

In laboratory studies, MGF has been observed to initiate autocrine and paracrine signaling cascades distinct from those mediated by systemic IGF-1. The peptide’s localized expression following mechanical loading or muscle injury has led to investigations into its potential role in tissue repair, neuroprotection, and recovery from cellular stress.

Overview

IGF-1 is known to exist in multiple isoforms arising from alternative splicing of the IGF-1 gene. Among these, MGF (IGF-1Ec in human sequence nomenclature) contains a unique E-domain sequence that differentiates it functionally from other IGF-1 variants. Research indicates that while systemic IGF-1 promotes cell differentiation and growth, MGF may primarily influence progenitor cell activation and tissue remodeling at the site of mechanical strain.

MGF expression has been reported to increase significantly following eccentric exercise, mechanical load, or injury-induced stress. In experimental conditions, MGF appears to act through PI3K/Akt and MAPK pathways, which are implicated in cellular survival, growth, and anti-apoptotic signaling. Studies have also proposed that MGF may exhibit neuroprotective effects in neuronal cell models, potentially reducing apoptosis and promoting axonal regeneration.

Synthetic MGF peptides are used in laboratory research to investigate the mechanisms underlying muscle hypertrophy, tissue repair, and neuroregeneration. Their stability and bioavailability are determined largely by sequence optimization and the prevention of rapid enzymatic degradation in vitro.

Chemical Makeup

• Form: Lyophilized Powder
• Contents: Mechano Growth Factor (IGF-1Ec fragment)
• Molecular Formula: C121H200N42O39
• Molecular Weight: 2888.16 g/mol
• Batch Purity: 99.3% (COA verified)
• Formulation Size: 2 mg per vial

Research and Experimental Findings

MGF and Skeletal Muscle Regeneration
Experimental models demonstrate that MGF expression increases following muscle overload and mechanical stimulation. The peptide has been reported to stimulate satellite cell proliferation while delaying premature differentiation, potentially enhancing the regenerative capacity of skeletal muscle tissue.

MGF and Neuroprotection
In neuronal models, MGF has been observed to activate cell survival pathways associated with Akt phosphorylation, reducing apoptosis induced by oxidative or ischemic stress. These findings have led to further studies on the peptide’s possible role in neuronal recovery and axon outgrowth.

MGF and Cellular Repair Mechanisms
MGF may upregulate genes involved in cell-cycle progression, DNA synthesis, and anti-apoptotic regulation. In vitro research suggests that MGF-treated cells exhibit enhanced proliferation and repair efficiency compared to controls, indicating potential signaling distinct from systemic IGF-1 activity.

MGF and Cardiac Studies
Preclinical studies on cardiac tissue have shown transient MGF expression after myocardial injury. Researchers propose that the peptide may play a supportive role in cardiac tissue repair and cytoprotection through modulation of survival signaling pathways and fibroblast activity.

MGF and Age-Related Decline
MGF expression has been found to diminish with age in various models, potentially correlating with reduced muscle mass and regenerative ability. Experimental administration of synthetic MGF in aging models has been investigated for its ability to stimulate local IGF signaling and muscle stem cell activation.

Mechano Growth Factor peptide is available for research and laboratory purposes only. It is not intended for human or animal therapeutic use.

References

1. Yang SY, Goldspink G. Different roles of the IGF-I Ec peptide (MGF) and mature IGF-I in myoblast proliferation and differentiation. FEBS Lett. 2002;522(1-3):156–160. https://pubmed.ncbi.nlm.nih.gov/12095628/
   
2. McKoy G, Ashley W, Mander J, Yang SY, Williams N, Russell B, Goldspink G. Expression of IGF-1 splice variants and structural genes in rabbit skeletal muscle induced by stretch and stimulation. J Physiol. 1999;516(Pt 2):583–592. https://pubmed.ncbi.nlm.nih.gov/10087355/
   
3. Goldspink G. Mechanical signals, IGF-I gene splicing, and muscle adaptation. Physiology (Bethesda). 2005;20:232–238. https://pubmed.ncbi.nlm.nih.gov/16024513/
   
4. Owino V, Yang SY, Goldspink G. Age-related loss of skeletal muscle function and the role of MGF splice variant of IGF-1. J Musculoskelet Neuronal Interact. 2001;2(3):195–198. https://pubmed.ncbi.nlm.nih.gov/15758434/
   
5. Mills P, Nader GA. Regulation of muscle stem cell fate by IGF-1 and MGF signaling. Exp Gerontol. 2006;41(12):1114–1121. https://pubmed.ncbi.nlm.nih.gov/16996213/
   
6. Ramer MS, Priestley JV, McMahon SB. Functional regeneration of sensory axons into the adult spinal cord. Nature. 2000;403(6767):312–316. https://pubmed.ncbi.nlm.nih.gov/10659854/
   
7. Kandalla PK, Goldspink G, Butler-Browne G, Mouly V. Mechano Growth Factor activates human muscle progenitor cells and modulates their differentiation. J Cell Physiol. 2011;226(7):1743–1750. https://pubmed.ncbi.nlm.nih.gov/20945333/
   
8. Quesada A, Etayo-Labiano I, Villalba M, et al. Mechano-growth factor and IGF-I receptor signaling in neuroprotection. J Neurosci Res. 2007;85(10):2139–2148. https://pubmed.ncbi.nlm.nih.gov/17549746/
   
9. Mills P, Goldspink DF, et al. MGF and the adaptive response to mechanical loading in skeletal muscle. Biochem Soc Trans. 2003;31(Pt 6):1191–1196. https://pubmed.ncbi.nlm.nih.gov/14641011/
   
10. Zhao J, Li X, et al. Expression of mechano-growth factor after myocardial infarction and its effect on cardiomyocyte apoptosis. Biochem Biophys Res Commun. 2009;382(3):580–584. https://pubmed.ncbi.nlm.nih.gov/19280612/
    
11. Hameed M, Lange KH, Andersen JL, Schjerling P, Kjaer M, Harridge SD. The effect of recombinant human growth hormone and resistance training on IGF-I splice variant expression in older men. J Physiol. 2004;555(Pt 1):231–240. https://pubmed.ncbi.nlm.nih.gov/14678489/
    
12. McMahon CD, Popovic L, Oldham JM, Jeanplong F, Osepchook CC, Hodgkinson SC, Sheard PW, Dixon MW, Knowles SE, Bass JJ. GH dependence of skeletal muscle IGF-I and MGF mRNA expression. Am J Physiol Endocrinol Metab. 2003;284(4):E671–E678. https://pubmed.ncbi.nlm.nih.gov/12475752/
    
13. Yang SY, Alnaqeeb M, Simpson H, Goldspink G. Cloning and characterization of an IGF-I isoform expressed in skeletal muscle subjected to stretch. J Muscle Res Cell Motil. 1996;17(4):487–495. https://pubmed.ncbi.nlm.nih.gov/8884600/
    
14. Philippou A, Halapas A, Maridaki M, Koutsilieris M. Type I IGF-1 Ec (MGF) expression in exercising skeletal muscle. Histol Histopathol. 2007;22(6):603–618. https://pubmed.ncbi.nlm.nih.gov/17357089/
    
15. Quesada A, Romeo HE, Micevych P. IGF-1 and MGF expression in hippocampal neurons: neuroprotective role in aging. Neuroscience. 2009;162(1):64–73. https://pubmed.ncbi.nlm.nih.gov/19374946/

For research use only. Not for human or veterinary use.