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by Anthony Roberts - After resistance exercise,
IGF-1 is released within the muscle. Specifically,
at this time, immediately following the mechanical
use of a muscle, the IGF-I gene is spliced towards
MGF which initiates hypertrophy and repair of local
muscle damage. It does so both by activating muscle
stem cells and satellite cells, but also via various
other anabolic processes. (1) It differs from “regular”
IGF-1 mainly due to it’s C-Terminal sequence.
Background
At the time of this writing, bodybuilders and
athletes have been experimenting with MGF for a
couple of years already. It was first discovered
in the muscle by Goldspink, et al. In human muscle,
a 49-base insert changes the reading frame in mechano
growth factor (MGF) as compared to IGF-1.

Action
When mechanical overload is introduced to a muscle
(as by weight training), the IGF-1 gene released
and is differentially spliced during the bodies
response. Initially, it it is spliced to produce
predominantly IGF-1Ec (called the MGF splice variant
of IGF-1). This early splicing stimulates satellite
cells into activation. Which in turn allows the
activation of extra undamaged nuclei to grow new
muscle fiber and tissue. The appearance of MGF also
initiates the upregulation of new protein synthesis.
After this initial splicing of IGF-1 into MGF, production
then switches towards producing a systemic release
of IGF-1Ea from the liver, which also upregulates
protein synthesis as well. The expression of IGF-1
splice variants, over the course of the healing
and regrowth phase of muscle repair is thought to
be the primary anabolic mechanism by which the body
produces new muscle. MGF is available as an injectable
peptide, and it has been anecdotally shown that
injecting it will cause a response in the area resulting
in localized muscle growth.

Technical Data
In a rodent study, a single intramuscular injection
into muscle resulted in a 25% increase in mean muscle
fibre cross section area within three weeks.(2)
Using a similar protocol, liver-derived IGF-1 took
four months to produce a 15% increase.(3)
It would also appear that with regards to age,
the young have a better ability to respond to MGF
(4), and that the elderly experience a decreased
response to MGF which results in a decreased ability
to stimulate the growth of new muscle tissue.
In the words of the man known as the father of
MGF research:
“MGF is… a prime candidate for gene doping
for enhancement of athletic performance.”(1)
User Notes
I’ve personally used MGF several times and think
it’s a really great product. Admittedly, I have
only used it in conjunction with Lr3IGF-1, but many
(myself included) feel that there’s probably quite
a bit of synergy to be found between these two peptides.
I experienced muscle growth (localized) with
MGF, but not really much of a strength increase
over what I would have experienced with just the
IGF. Most users find MGF to be very good for muscle
growth and typically use a protocol of 100mcgs injected
into each lagging muscle just after working it.
A further discussion of how to incorporate this
compound can be found in my article “Peptides: The
next frontier in hypertrophy”
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| Trivial Name |
Mechano Growth Factor |
| Systematic Name |
†IGF-1Ec |
| Bioavailability |
99% |
| Metabolism |
Almost all tissues |
| Elimination Half Life |
Variable |
| Excretion |
N/A |
| Legal Status |
Varies |
| Route of Administration |
Subcutaneous injection,
Intramuscular Injection |
References
- British Journal of Sports Medicine 2005;39:787-788;
doi:10.1136/bjsm.2004.015826 © 2005 by BMJ Publishing
Group Ltd & British Association of Sport and
Exercise Medicine
- Goldspink G, Yang SY. Method of treating
muscular disorders. United States Patent. Patent
No US 6,221,842 B1, Apr 24 2001.
- Barton-Davis E, Shoturma DI, Musaro A, et
al. Viral mediated expression of insulin-like
growth factor-I blocks the aging-related loss
of skeletal muscle function. Proc Natl Acad
Sci USA 1998;95:15603–7
- J Physiol (2003), 547.1, pp. 247-254© Copyright
2003 The Physiological SocietyDOI: 10.1113/jphysiol.2002.032136
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