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The sequencing of the human genome showed that there are only about 40,000 genes. However, there are many more proteins. This is because some genes are spliced to produce different protein/peptides which usually have different biological functions. Combining physiological and molecular biology methods made it possible to identify and characterize a local muscle growth/repair factor (MGF). After resistance exercise, the IGF-I gene is spliced towards MGF which kick starts hypertrophy and repair of local muscle damage by activating the muscle stem cells as well as anabolic processes. Interestingly, loss of muscle mass in old age and in certain diseases is associated with an impaired ability to express MGF.
DIFFERENCE FROM - IGF (Insulin-like growth factor)
MGF differs from systemic IGF-IEa in that it has a different peptide sequence which is responsible for replenishing the satellite (stem) cells in skeletal muscle, in other words it is more anabolic. In vivo experiments in which muscles of the rat were subjected to mechanical damage or injection of a myotoxic agent also demonstrated (Hill &Goldspink, 2003) that MGF precedes muscle satellite (stem) cell activation. This is in accord with the finding that when skeletal muscle cells in culture, were either transected with the MGF cDNA or were treated with the MGF carboxy peptide they increased in number but stayed as monocleated myoblasts (Yang & Goldspink, 2002).
It appears that MGF plays a dual role in inducing satellite cell activation as well as protein synthesis and this is probably why it is much more potent than the liver type or IGF-IEa for inducing rapid muscle hypertrophy.
The characterization of a local tissue repair factor (mechano growth factor, MGF) that is produced by exercised and/or damaged muscle by differential splicing of the IGF-I gene provides understanding of how muscle is maintained in the young normal individual. MGF is different to the systemic IGF-I as it have an insert of 49 base pairs in exon 5 that introduces a reading frame shift leading to C terminal peptide with unique properties.
DOSAGE
100-200 mcg every day.
Peptide is best administered at least twice daily, bi-lateral doses (so divide the research dose into two administrations on your research subject) this will assist to keep blood levels steady in your research subject, in cellular culture, or in vitro.
BENEFITS
Loss of muscle mass in old age and in certain diseases is associated with an impaired ability to express MGF.
- The ability to produce MGF declines with age, and this is commensurate with the decline in circulating GH levels.
- MGF has been shown to boost muscle mass by improving the ability of wasted tissue to grow.
- MGF has been shown to improve the ability of wasted tissue to grow.
- MGF has been shown to activate muscle stem cells.
- MGF has been shown to increase the upregulation of protein synthesis.
- MGF induces rapid muscle hypertrophy.
- MGF has considerable potential as a generic means of treating muscle cachexia.
SIDE EFFECTS
The drug administrated in grander dose nearby the 100 mcg range will cause:
- headaches;
- rare nausea also can contribute to less blood sugar of hypoglycemia in some persons.
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