Has anyone Used MGF yet

I am really keen to give MGF a try,

Has anyone used it yet? If so what dosage regimen did you use?

Doc and myself will give it a try soon.

I will probably use 200mcg MFG with 50mcg IGF.

Are you going to use the plain one or the pegulated one? PEG-MGF?

The only one I can get my hands on is the standard non-pegylated version,,

Will probably give it a try as soon as my neck injury is resolved and I'm back to proper training

MGF will NEVER behave as MGF if injected. Doesn't matter whether you pegylate it or not.

MGF is expressed from within and mediates its actions in the nulceus of the cell. Unlike IGF-1 it has no receptor. So writing on and on about timing it with IGF-1 is of zero value because MGF will behave like IGF-1 when injected and will NEVER behave as MGF.

To quickly summarize the difference in function, MGF stimulates muscle stem cells (satellite cells) to reenter the cell cycle and proliferate, whereas IGF-1 is necessary for the differentiation of newly generated muscle precursor cells into myoblasts and myofibers.

The Scientist wrote:

MGF will NEVER behave as MGF if injected. Doesn't matter whether you pegylate it or not.

MGF is expressed from within and mediates its actions in the nulceus of the cell. Unlike IGF-1 it has no receptor. So writing on and on about timing it with IGF-1 is of zero value because MGF will behave like IGF-1 when injected and will NEVER behave as MGF.

To quickly summarize the difference in function, MGF stimulates muscle stem cells (satellite cells) to reenter the cell cycle and proliferate, whereas IGF-1 is necessary for the differentiation of newly generated muscle precursor cells into myoblasts and myofibers.

Please explain in laymans terms if you can... why would it behave as IGF-1 ? I understand there has been no real research on the Pegylated version,, the pegylation is supposed to increase the half life,, as MGF only has a half life of a few minutes in the bloodstream,, but no one really knows what the pegylated version will really do in your body,,

if there are no receptors for it,, how does it work in our bodies,, and why would it have increased muscle mass i rats by 20%?

""""Research on mechano growth factor: its potential for optimising physical training as well as misuse in doping
[LEADER]

Goldspink, G

Correspondence to: Professor Goldspink Department of Surgery, Royal Free and University College Medical School, Hampstead Campus, Rowland Hill Street, London NW3 2PF, UK; EMAIL ADDRESS REMOVED

The work described in this Review was supported by the Wellcome Trust, Action Research, the International Olympic Games WADA committee.

Competing interests: none declared
Abstract

Mechano growth factor can produce rapid increases in muscle and strength, giving it considerable therapeutic and doping potential"""

I don't have much time at the moment but I'll try and fill in some info on this tomorrow.

But in a nutshell... MGF is simply a type of IGF-1.

The type of IGF-1 that everyone thinks of when talking about IGF is actually IGF-1Ea... MGF is IGF-1Ec.

The basic difference between the 2 types is Ea is expressed through the liver and goes systemic. Ec is expressed locally as a result of mechanical overload of the muscle cells. That's just a fancy way of saying the muscle has been worked hard... ie: weight training.

And of course when I talk about IGF-1 that we BB's use, of course I'm referring to LR3IGF-1. Which is no different than our natural IGF-1 except it has an additional 13 amino acids added to it which drastically increase its half life. Similar to an Enanthate ester added to a testosterone molecule.

Not to flame you .... but I know exactly wha LR3 IGF-1 is,, but you still don't explain why exogenous MGF would not act as MGF .


"MGF was inserted into rat leg muscles by intramuscular injection. This resulted in a 35 percent increase in the weight of the injected muscle within three weeks, and the analyses showed that this was due to an increase in the size of the muscle fibers.12 Additionally, there was a increase in muscle strength of 25 percent.
Similar experiments by other groups have also been carried out using a viral construct containing the liver-muscle type of IGF-1, which resulted in a 15 percent increase in muscle mass, but this took over four months to develop.11 Hence, the dual role MGF plays in inducing satellite cell activation as well as protein synthesis suggests it’s much more potent than the muscle-liver type or IGF-IEa for inducing rapid hypertrophy."

How does the behavior of IGF-1 and MGF differ?

"MGF is a non-secreted form of IGF-1 that can be found in the nucleus of cells in culture or in a perinuclear location in hippocampal cells after ischemia (restriction in blood supply)". 4

In other words MGF never leaves the cell it was created in. For emphasis I quote from another source:

"...MGF... is not normally secreted." 5

Geoffrey Goldspink has written "that MGF increases myoblast proliferation via a different signalling pathway" then IGF-1.

To reiterate & expand upon this concept I quote from another source:

"IGF-1 isoforms differ in the signaling pathways they activate. By over-expressing IGF-1Ea and MGF in muscle, it has been shown that both isoforms can activate IGF-1R and AKT phosphorylation. In addition, MGF was shown to induce phosphorylation of ERK, a property not shared with IGF-1Ea." 6

So IGF-1 and MGF work through different pathways not receptors. There is only one receptor, IGF-1-receptor (also insulin, IGF-II & hybrid receptors which are not relevant to this discussion). There is no MGF receptor. The reason why it would be nonsensical to have an MGF receptor is that MGF does not leave the cell.

This contrasts with IGF-1 which is released from the liver into circulation and which is created in muscle and translocates to the cell surface. Both events result in IGF-1 binding to the IGF-1 receptor.

So what happens in plain language please?

During the process of gene transcription pieces of DNA are transcribed and then spliced together by RNA and this code is taken to the ribosomes where the peptide is manufactured. In splicing MGF there is a subtle frame shift such that the right side of the code is a little different then IGF-1. Everything else is identical.

This subtle difference means that when MGF & IGF-1 are manufactured by the riboomes MGF MUST because of the signal pull that is part of its make up, translocate to the Nucleus of the cell and more specifically the Nucleolus.

IGF-1 because of its makeup MUST move to the cytoplasm where it forms a pool of IGF-1 which will transloacte to the cell membrane where it will bind w/ an IGF-1 receptor.

MGF has NO receptor. It does not need it to mediate events. Too many times people think that a lock/key ligand/receptor is needed to intiate signals. That is not always true especially when proteins move to the nucleus.

MGF is NEVER found in circulation. It is produced in a muscle cell as described and it [img] .

IGF-1 however does circulate. It is produced in the liver and secreted into the blood stream. If it is made in muscle tissue or in local tissue it makes its way to the surface and can bind to a receptor on that cell or nearby cells. The latter is how muscle made IGF-1 can effect nearby bone growth.

In lab experiments with MGF they usually do one of two things. One they use a viral vector of MGF cDNA to increase the cDNA of MGF in the cell so that more MGF is made internally. When they do this they get a 25% increase in muscle in a three week period. If they use the same approach to get IGF-1 to express itself from within they get less muscle growth (15%) and it takes 4 months.

The second approach is to actually inject MGF into a cell (i.e. penetrate the cell membrane). Unfortunately for scientists this also invokes a damage repair function in cells so it is difficult to actually attribute all of the benefits that ensue to MGF.

You follow neither of these approaches when you inject MGF or Peg MGF.

MGF is identical to IGF-1 in chemical makeup on the leftside of the peptide. This allows it to bind with IGF-1 receptors should it ever be injected or find itself outside of the cell. However because of the difference in right-side structure MGF is incapable of binding to IGF-1 binding proteins (which would prolong its life).

MGF has a very short half-life in blood plasma. If it is pegylated it has a longer half-life. I do not know the extent to which pegylation reduces binding affinity but it probably does to some extent depending on where it is pegylated.

Injecting Peg MGF will, if it survives, probably bind to an IGF-1 receptor. If it does so it activates the IGF-1 signaling pathways just as IGF-1 would.

I do not have any data on how strongly MGF will bind to IGF-1 receptors. A pegylated MGF is small enough to penetrate the vascular wall and travel systemically. It will not be confined to the area injected as IGF-1 bound to IGF-BindingProtein3 bound to Acid laibile subunit (i.e. the ternary complex) will. Thats why injecting large amounts of MGF brings vacularization, pumps, glucose uptake, in essence insulin-like activity....because it is behaving as IGF-1...and doing so in systemic fashion.


Hey Batman, hope this explains it a little better but please feel free to ask any oyher questions on this subject...

The Scientist

That's all very nice, but I still don't know, if it works? Which one is best, PEG-MGF or MGF? How and when do you inject? How do you and with what do you reconstitute it?

HaHa Yep,, that does explain it better,

Hi, well best results I got with my clients was on regular MGF mixed in bacterial water (the same as GH). 1 vail is 200 mcg's, so I will only use 80 mcg's per shot per day no more than 4 times a week. Becuase it's regular MGF you only got a active life of 4 to 6 hours, so you can either take it pre workout or post workout.

Works awesome on the upper chest, outer calf, side tricep and rear delts.

Did you use it in conjunction with a cycle of anabolics or was it on it's own? Please give an example of the results you achieved? Where can i find info on the side effects, because google isn't helping at the moment.

Hi dbol,

Thanks for your interest in my work,

Okay first I've used it on myself with great results in conjunction with a 10 day Blitz Cycle that consist of Suspension, Anapolin, Insulin,t3 and gh...my results was better by layering it in with the course as I'v used the gh to play the role of igf 1 to mature the newly satelite cells.

My next step will be to layer it in after a 20 day deca and sust cycle, where I will utilize some dnp with short acting insulin to mimick the effect of igf 1 (let me explain quick...The insulin molecule is experiencing N-terminal truncation when coming into
contact with circulatory DNP. When the N-terminal is removed from IGF-1 the
resulting growth factor is called Des (1-3) IGF-1. The result is an anabolic far
more powerful than even IGF-1 itself. This is true of IGF-2 and other growth
factors including insulin. The possibility strongly suggests that the truncated
insulin molecule would more readily fit into and activate the muscle cell IGF-1
receptors as well.) So now we got igf 2 in our cells and mgf splicing new cells...booom new bigger muscle...and this is what we all about.

Thank you

Can you please drop me a mail @ EMAIL ADDRESS REMOVED. I would like to discuss this matter further.

Hard core science-isnt this just better than- "Hi this oke at the gym told me to take Dbol if I want to get huge!" Nice post guys.

Very informative indeed.

are there any pharmacuetical companies making human grade mgf? of is it just UG labs.. also i have only found one source for the stuff, NO ONE knows about it or has heard of it, even the juice and bodybuilding veterans at my gyms..it seems to be VERY RARE, which is strange to cause from research i have found is that it was founded YEARS AGO!!!