MGF is a peptide known as mechano growth factor. This is an IGF-1Ec repair and growth factor that is developed in muscle tissues that has been damaged after exercise. This chemical is referred to as MGF, simply as a means of differentiating the peptide from other IGF variants which are commonly used for research purposes.
MGF can be applied to animals to generate regrowth in wasted tissue. This chemical can stimulate stem cells in the muscles, causing upregulation of the protein synthesis that can improve recovery and encourage quick muscle growth.
MGF can also initiate stem cell activation in IGF-ireceptor domains that will increase the turnover of protein synthesis over time. Naturally, the liver creates two igf splice variants of MGF which include IGF-1Ec and IGF-IEa. The latter is significantly less anabolic than the former, which is designed to activate stem cells. IGF-1Ec is the closest variant to the synthetic MGF.
Effects on Growth Factor Expression
Muscle mass can be regulated systematically or locally, and isoforms of IGF-1 have been cloned as a means of stimulating this reaction during research.
Expressions of these clones were only detectable in the tissues after mechanical stimulation, which gave rise to the name MGF. This reaction is not glycosylated and has been found to be smaller and contain a shorter half-life than IGF-1 that is produced in the liver.
MGF also has a different C terminal sequent as IGF-1 which means it will bind with different receptor or protein affinities.
Another cloned variant, LIGF-1, has been found in muscle tissues after exercise with a similar systemic type as IGF-1.
Evidence suggests MGF is very potent and can induce local protein synthesis capable of preventing apoptosis that can encourage remodeling and repair of affected tissues. Combining applications of MGF with electrical stimulation can be used to encourage the production of IGF-1, which is commonly slowed during the aging process.
Different Roles in Myoblast Proliferation and Differentiation
IGF-1 has been involved in tissue differentiation and repair, but when this peptide is spliced it can respond to different signals.
Splicing IGF-1 using different transcripts can encode a variety of proteins. Two of these can be produced in rodents throughout active muscle tissue, acting as positive regulators of muscle hypertrophy.
MGF is particularly common in muscle IGF in rodents while IGF-1 Eb acts similarly to the IGF-1 Ec that would be found naturally in humans throughout damaged or exercised muscles.
Mammalian skeletal muscle differentiation can be used to switch cellular programs– from proliferation states to differentiation. These peptides are helpful in regulating this process because they will only affect the tissues where they are applied rather than spreading throughout the body.
Ischemic stroke is becoming increasingly common amongst aging populations, and splices of IGF-1 have been found to be effective in maintaining structures, to prevent this neuronal damage.
Isoforms of IGF-1 are in high conservation states in mammals, which notes their importance. Gerbils in particular have been noted for the high amount of liver type IGF-1E and MGF transcripts.
Analysis shows that administering MGF mRNA to a post-ischemic brain in gerbils can increase the expression of the endogenous MGF.
Western blot analysis has been used to extract proteins from the hippocampal regions of the ischemia, to increase the MGF levels in these animals.
MGF has a different peptide sequent than IGF-IEa that is responsible for replenishing any skeletal muscle satellite cells. This means that the peptide can remain anabolic for a longer period of time when compared to the systematic release of MGF liver variants.
Applying MGF can also encourage hypertrophy and repair localized damage to muscle tissues by activating anabolic processes– including nitrogen retention and protein synthesis.