UPA MGF PEG

UPA MGF PEG(PREGLYLATED MECHANO GROWTH FACTOR 5000MCG/AMP =1AMP)

PEG MGF is a splice variant of the IGF produced by a frame shift if the IGF gene and PEGylated to improve stability.  PEG-MGF, or PEGylated Mechano Growth Factor, is a new and innovative form of the IGF produced by a frame shift if the IGF gene, namely Mechano Growth Factor (MGF), which is PEGylated to improve stability that outperforms natural MGF many times over.  MGF is a splice variant of the IGF gene which increases stem cell count in the muscle and allows for muscle fibers to fuse and mature. This is a process required for growth of adult muscle. Natural MGF is made locally and does not travel into the bloodstream. Synthetic MGF is water based and when administered intramuscularly, travels into the bloodstream. MGF is only stable in the blood stream for only a few minutes. Research has shown that PEG-MGF helps increase the muscle stem cell count, so that more may fuse and become part of adult muscle cells. 

PEGylation is the act of attaching a Polyethylene glycol (PEG) structure to another larger molecule (in this case, MGF). The PEG acts as a protective coating and the theory here is that this will allow the MGF to be carried through the blood stream without being broken down. Neurological research has shown that utilizing PEGylated MGF resulted in a longer more stable acting version of the MGF peptide in serum/blood.

Mechano Growth Factor (MGF) exhibits local effects in skeletal muscle and without cannot travel through the body without modification. The problem with synthetic Mechano Growth Factor (MGF) is that it is introduced intramuscularly and is water based so it goes into the blood stream. When used this way, Mechano Growth Factor (MGF) only remains stable in the blood stream for a few minutes. Biologically produced MGF is made locally and does not enter the bloodstream. It is also short acting so stability is not an issue. By PEGylating the Mechano Growth Factor (MGF) it is almost as efficient as local produced Mechano Growth Factor (MGF) when used intramuscularly. This is accomplished by surrounding part of the peptide with a structure of polyethylene glycol, which can be attached to a protein molecule. The polyethylene glycol groups protect the peptide but do not surround it completely. The active sites of the peptide are still free to do their biological function. In this case the shell is a negative charged shield against positively charged compounds that would affect the protein.

Mechano Growth Factor (MGF): a local growth factor or a local tissue repair factor. MGF is derived from the insulin-like growth factor (IGF-1), but its sequence differs from the systemic IGF-1 produced by the liver. MGF is expressed as a form of IGF-1 by mechanically overloaded muscle when mechanical resistance is applied to muscles (such as weight training). At this point, the IGF-1 gene is spliced to produce IGF-1Ec (which is another name for MGF). It is expressed as a pulse following muscle damage and is apparently involved in the activation of muscle satellite cells[1]. This production of MGF can stimulate satellite cells into activation, to create new muscle fiber[2]. MGF also promotes nitrogen retention and new protein synthesis. It could actually be the case that this particular expression of MGF (IGF-1Ec) is an important part of the deciding factors in whether a muscle will grow or not. The introduction of this peptide, either by weight training or by an injection, will cause the affected area to respond by producing new muscle tissue. It would be safe to say that MGF presence in the muscle is one of the most major factors in the anabolic effect of resistance training (weight training). Currently, this compound is being used successfully by bodybuilders, for bringing up lagging body parts as well as overall growth.

Effects

MGF is being used successfully by bodybuilders, for bringing up lagging body parts as well as overall growth. The most relevant rodent data has been shown that MGF is a very potent inducer of muscle growth when it’s introduced into the muscle via an intramuscular injection of cDNA. In fact, in one study MGF caused a 20% increase in the weight of the injected muscle within 2 weeks[3]. Further investigation elucidated that this was actually due to an increase in the size of the muscle fibers.

Mechanism

MGF is extremely likely to cause myogenesis during skeletal muscle hypertrophy by contributing to at least by three important molecular processes: increased satellite cell activity, gene transcription and protein translation. Satellite cells in skeletal muscle provide the extra nuclei for postnatal growth[5] and that they are also involved in repair and regeneration following local injury of muscle fibers[6]. In normal adult undamaged tissue, the satellite cells are quiescent and usually detected just beneath the basal lamina. When activated, they commence to coexpress myogenic factors, including c-met, myoD, myf5, and, later, myogenin[7]. When introduced either by weight training or by an injection?MGF appears to stimulate satellite cells into activation. This in turn allows the activation of extra undamaged nuclei required for muscle fiber growth and repair to occur. In addition, the appearance of MGF initiates the upregulation of new protein synthesis. After this initial and short lived burst of splicing, IGF-1 production switches towards producing a systemic release of IGF-1Ea from the liver, which upregulates protein synthesis as well, but over a longer time line. During this process of regenerating muscle, myoblasts are formed to replace and hypercompensate for damaged/destroyed ones, and then they can either fuse with each other to form totally new myofibers or become incorporated into previously damaged (surviving) myofibers. Ultimately, if more myofibers are created than were destroyed (by training) new muscle growth is experienced.  

Dosage and Administration

It’s a good way for bodybuilders and other athletes to increase muscle weight by shooting MGF immediately post workout. At this point natural levels of MGF are already elevated. The addition of extra MGF should push more satellite cells towards the formation of new muscle tissue. Administration dosage of MGF should be at about 400mcgs/day, which is injected into the primary muscle trained post workout – half going into that muscle on one side of the body, the other half going into the mirror image of that muscle on the other side. We suggest that a administration of IGF-1, such as IGF-1 Long R3, an hour after shooting of MGF will produce the additional activation of satellite cells, protein translation, and gene transcription. It will force the body to produce much more new tissue than if MGF or IGF are used at any other point during the day, or in a different sequence. It seems that MGF and IGF-1 appear to act synergistically and promote rapid new muscle growth.  
Differences between MGF, IGF-1 and HGH (human growth hormone)
HGH is actually closely related to IGF-1, in a lot of ways. HGH, or GH in short, is certainly an effective fat burner and anabolic agent, and is a protein secreted by the pituitary. Once secreted, it has the ability to influence various cells in the body to increase in number and size, as well as having the ability to enhance the movement of amino acids through cell membranes- thereby increasing the rate at which the cells can convert those molecules to usable proteins. It also causes cells to preferentially burn fat in lieu of carbohydrates. The important thing to realize is that there is a mounting body of evidence that strongly suggests that these effects occur as a result of the IGF-1 released as a result of the pituitaries GH secretion. Scientists have discovered that many of HGH’s anabolic and regenerative effects are actually mediated by IGF-1. HGH indirectly causes muscle growth by stimulating the release of IGF-1 when it (the HGH) is destroyed in the human body. So one way you could look at it as HGH being a precursor to IGF-1. The later is more effective at directly causing muscle growth and density increases than HGH. Over the past few decades, HGH has developed quite a reputation for taking awhile (often several weeks) for the user to start seeing results. In contrast, IGF-1 often begins to product noticeable results within the first couple of weeks. With growth hormone you need to use high amounts of anabolics and often insulin to see any gains at all, this is not the case with IGF-1. IGF-1’s superiority to HGH is not only intuitive at some level, but has also been clearly elucidated clinically as well. In the following graphs taken from a rodent study comparing IGF-1 and HGH, a low dose as well as a high dose of IGF-1 was shown to be more anabolic than HGH. In comparison to HGH, IGF-1 produced an overall greater total protein content within the injected muscle as well as a greater final weight of the that muscle (called the “Tibialis Anterior” or TA)
It seems to be the case that IGF-1 would be superior to HGH as an anabolic agent. In some clinical studies, that is not always the case, but in most of bodybuilders and athletes, greater results are often seen with IGF-1 over HGH – and it should be noted that they are often seen more quickly as well.
The mature systemic type of IGF-1 is a simple 70 amino acid peptide, but its gene is unexpectedly large spanning a region of over 90 kb of genomic DNA. Alternative splicing of IGF-I gene results in different transcripts encoding several IGF-I precursor proteins. MGF is expressed by mechanically overloaded muscle and it is derived from the IGF-1, but its sequence differs from the systemic IGF-1 produced by the liver[9]. In addition to MGF expression being mechanosensitive, it has a unique carboxy peptide sequence . It was noted that in exon 5 there is an insert that changes the reading frame. In the rat it is 52 bases, but the human the insert is 49 bases. Amino acids are encoded by triplets of bases, and because the exon 5 sequence that is spliced into the MGF mRNA is not a multiple of 3, the downstream peptide sequence is different from that of the other IGF-1 isoforms. This has important functional consequences, because the carboxy peptide of some IGF-1 isoforms is involved in the recognition of the specific binding proteins that stabilize these growth factors. However, it appears that in the case of MGF the carboxy-terminal peptide (encoded by parts of exons 5 and 6) is unique and has now been shown to act as a separate growth/repair factor from the IGF-1 receptor domain
Splicing of the insulin-like growth factor (IGF) gene to produce different forms of IGF-I in human muscle. Mechano growth factor (MGF) is produced locally in response to exercise and it differs from the two systemic types of IGF-1 as the 49 base insert in the exon creates a reading frame shift so that the downstream or C-terminal peptide sequence is different. Reg Seqn, Regulatory sequence.
Although MGF is a fairly new peptide, recent studies drawing the comparison between IGF-1 and MGF have concluded that MGF is even quicker to produce results. Actually, it’s been found in rodent studies to produce both faster and better results with regards to muscle growth, compared to IGF-1. It has been found by Goldspink G.’group that a single intramuscular injection of MGF cDNA into a mouse muscle resulted in a 25% increase in mean muscle fibre cross section area within three weeks. Similar experiments have been carried out using the systemic or liver type of IGF-1 in an adenoviral vector under the control of a muscle regulatory sequence. However, this took four months to produce a 15% increase and is probably due to the anabolic effect of IGF-1, which is common to all the splice variants. So far as we know, MGF is superior to IGF-1 and HGH for bodybuilders as an anabolic agent and this compound is being used successfully by bodybuilders, for bringing up lagging body parts as well as overall growth.