Who's running MGF & IGF-1 LR3, and how?

[R&D]

As the title says, who's running both, and how are (did) you use it? When do you inject what and how much are you injecting where?

Results? If gains are being seen, are they lasting?

I've only seen a couple people post about MGF and both seem to have a personal vested interest with a supplier (either they source or are getting some form of a kickback). I'd like to hear from as many users as possible before I start injecting this stuff.

FWIW, I'm running HGH and AAS as well if that matters...



Edit: I just realized this is my first post here after all this learking... HELLO FROM THE NEWBIE!

[Ufa]

Welcome! You are very perceptive. Don't be the first one to use anything.
Remember the first GH from cadaver's.

[vermin]

MGF? Muscle Growth Factor? (just a guess)

Please enlighten us....

[R&D]

MGF? Muscle Growth Factor? (just a guess)

Please enlighten me....

MGF = mechano growth factor

[vermin]

Have you done a medical literature search on this? Can you reference any papers?

[RedBaron]

Changes in muscle mass and phenotype and the expression of autocrine and systemic growth factors by muscle in response to stretch and overload. Goldspink G. J Anat. ;194 ( Pt 3):323-34 (1999).

The study of the underlying mechanisms by which cells respond to mechanical stimuli, i.e. the link between the mechanical stimulus and gene expression, represents a new and important area in the morphological sciences. Several cell types ('mechanocytes'), e.g. osteoblasts and fibroblasts as well as smooth, cardiac and skeletal muscle cells are activated by mechanical strain and there is now mounting evidence that this involves the cytoskeleton. Muscle offers one of the best opportunities for studying this type of mechanotransduction as the mechanical activity generated by and imposed upon muscle tissue can be accurately controlled and measured in both in vitro and in vivo systems. Muscle is highly responsive to changes in functional demands. Overload leads to hypertrophy, whilst decreased load force generation and immobilisation with the muscle in the shortened position leads to atrophy. For instance it has been shown that stretch is an important mechanical signal for the production of more actin and myosin filaments and the addition of new sarcomeres in series and in parallel. This is preceded by upregulation of transcription of the appropriate genes some of which such as the myosin isoforms markedly change the muscle phenotype. Indeed, the switch in the expression induced by mechanical activity of myosin heavy chain genes which encode different molecular motors is a means via which the tissue adapts to a given type of physical activity. As far as increase in mass is concerned, our group have cloned the cDNA of a splice variant of IGF-1 that is produced by active muscle that appears to be the factor that controls local tissue repair, maintenance and remodelling. From its sequence it can be seen that it is derived from the IGF-1 gene by alternative splicing but it has different exons to the liver isoforms. It has a 52 base insert in the E domain which alters the reading frame of the 3' end. Therefore, this splice variant of IGF-1 is likely to bind to a different binding protein which exists in the interstitial tissue spaces of muscle, neuronal tissue and bone. This would be expected to localise its action as it would be unstable in the unbound form which is important as its production would not disturb the glucose homeostasis unduly. This new growth factor has been called mechano growth factor (MGF) to distinguish it from the liver IGFs which have a systemic mode of action. Although the liver is usually thought of as the source of circulating IGF-1, it has recently been shown that during exercise skeletal muscle not only produces much of the circulating IGF-1 but active musculature also utilises most of the IGF-I produced. We have cloned both an autocrine and endocrine IGF-1, both of which are upregulated in cardiac as well as skeletal muscle when subjected to overload. It has been shown that, in contrast to normal muscle, MGF is not detectable in dystrophic mdx muscles even when subjected to stretch and stretch combined with electrical stimulation. This is true for muscular dystrophies that are due to the lack of dystrophin (X-linked) and due to a laminin deficiency (autosomal), thus indicating that the dystrophin cytoskeletal complex may be involved in the mechanotransduction mechanism. When this complex is defective the necessary systemic as well as autocrine IGF-1 growth factors required for local repair are not produced and the ensuing cell death results in progressive loss of muscle mass. The discovery of the locally produced IGF-1 appears to provide the link between the mechanical stimulus and the activation of gene expression.

[RedBaron]

Muscle satellite (stem) cell activation during local tissue injury and repair.Hill M, Wernig A, Goldspink G. J Anat. 2003 Jul;203(1):89-99

In post-mitotic tissues, damaged cells are not replaced by new cells and hence effective local tissue repair mechanisms are required. In skeletal muscle, which is a syncytium, additional nuclei are obtained from muscle satellite (stem) cells that multiply and then fuse with the damaged fibres. Although insulin-like growth factor-I (IGF-l) had been previously implicated, it is now clear that muscle expresses at least two splice variants of the IGF-I gene: a mechanosensitive, autocrine, growth factor (MGF) and one that is similar to the liver type (IGF-IEa). To investigate this activation mechanism, local damage was induced by stretch combined with electrical stimulation or injection of bupivacaine in the rat anterior tibialis muscle and the time course of regeneration followed morphologically. Satellite cell activation was studied by the distribution and levels of expression of M-cadherin (M-cad) and related to the expression of the two forms of IGF-I. It was found that the following local damage MGF expression preceded that of M-cad whereas IGF-IEa peaked later than M-cad. The evidence suggests therefore that an initial pulse of MGF expression following damage is what activates the satellite cells and that this is followed by the later expression of IGF-IEa to maintain protein synthesis to complete the repair.

[almostgone]

...Good reading material, RB...It hurt my head, but it's definitely great info...Have you tried any running MGF yet?..
...It looks like the combination of the the 2 would give a jump start to the the growth/repair repair process and also increase protein uptake....

AG

[Ejuicer]

I'm going to be picking up 4grams of mgf probably next week to experiment with, and i'll also be using it together with lr3.
I'll be shooting the long head of my triceps and my vastus medialis twice a week and use 500mcg between the 4 muscles. So twice a week i'll be going 125mcg per muscle group or 1 gram in total. The days i'm not using mgf i'll be shooting 100mcg lr3 post workout. I'll be running that for a month and see how things go.

[vermin]

Thanks RB - given the evident physiological discrimination between the factor types I wonder how relatively effective lr3 actually is. I know folks see benefits.

Also, has there been anything to correlate exogenous HGH with increased MGF release?

It seems as though two potential conclusions may arise. While I am aware of at least some of the literature that shows that HGH and lr3 stack well, either it is ultimately more effective to take HGH and allow your body to naturally release the appropriate factors, presumably timed better than we ever could; or at some level HGH's ability to stimulate release becomes sub-optimal and thus it would be recommended to take a more modest dose of HGH stacked with individual factors.

Good luck Ejuicer - we await your report!