Thread: more MGF experiences
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05-23-2006, 02:25 PM #1
more MGF experiences
hey,
read the thread about Logan's mgf log...was interesting..
I allready seen some more sources carrying this stuff, so was wondering if anybody else allready tried this..
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05-23-2006, 02:53 PM #2
I will be trying it, but as of now, I haven't tried it, sorry.
JohnnyB
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05-23-2006, 03:28 PM #3
np...keep us updated when ur ready to go
all those strange (for me) peptides/hormones MGF, GHRP 2, GHRP 6, Sermorelin Acetate sounds very interesting
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05-23-2006, 03:34 PM #4
I haven't tried it yet either, not as yet anyway. I'm very keen to find out what the fuss is about though.
Bump!
-Gear
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05-24-2006, 02:04 PM #5Junior Member
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Just as an update I heard the MGF that is out now (like ***) has a problem, it turns out is has to be pegylated to be effective, the MGF now deteriorates to quckly before it can do its job. I am very interested in MGF but I am waiting until more info comes out.
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05-24-2006, 02:39 PM #6
PEGylated peptides have an extended half-life. I remember when I was getting ready to do a treatment for Hep-C, and PEGylated was still in the research faze. Since then they only (I believe) use the PEGylated version for the treatment of Hep-C, I have a friend that is on it right now.
By PEGylating it you only needed to do a shot once a week, instead of every day, that was the info at the time. I'll have to call my friend and see if that is still the case. That would be great, doing one injection a week to get the desired results.
JohnnyB
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05-24-2006, 08:11 PM #7Anabolic Member
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The MGF is effective without the PEGylation. The PEGylation is going to just increase it's effectiveness by delaying its breakdown. I am very much looking forward to trying the new one in a month or so when it comes in. Until then, the original will be available at a nice discount.
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05-25-2006, 10:42 PM #8
i tired it... pumps were crazy with AS. More like a bad pump cuz it was so crazy it would stop the workout
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05-26-2006, 06:02 AM #9Originally Posted by juicehoe
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05-26-2006, 10:05 AM #10Junior Member
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Originally Posted by Whitey
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05-26-2006, 11:20 AM #11
Hard to say since i got injured half way threw the mgf cycle, but while on it felt similar. I think the mgf pumps might be more extreme
Originally Posted by fred9
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05-30-2006, 11:55 PM #12Originally Posted by juicehoe
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05-31-2006, 01:51 AM #13
I've used 1mg... @ 100 mcg ED
Can't say i got these extreme pumps y'all speak of... nor that 'fullness' either.
Narkissos
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05-31-2006, 04:23 PM #14Anabolic Member
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Originally Posted by fred9
A good analogy for IGF-1 vs. MGF is GH vs. IGF-1:
GH (which alone has shown quite limited potential for gaining mass, apart from mega doses) converts to IGF-1, the muscle building component, which has proved it's potential for mass gain.
Similarly, IGF-1 breaks down into MGF which is the component directly responsible for adding new muscle cells. For the purpose of hyperplasia, IGF-1 is far more efficient than growth, and MGF is more efficient even than IGF-1. The raw form of MGF has already shown it's power - there are some excellent logs written by users that indicate its potential. The fact is, some of the ideas we had about dosing were probably wrong in regard to timing and stacking with IGF-1.
However, the recent discovery of PEGylating the peptide will dramatically extend the active life of MGF in the test subject, potentially making this product scary-effective. I B E is coming out with the first PEGylated version in roughly 4 weeks.
But even after the PEGylated version comes out, there may still be advantages to the base peptide, depending on certain variables that we don't know yet, like will the PEGylated version go systemic, or stay local like the original?
There are a lot of unanswered questions really, but MGF is important enough that you can be certain in time, we'll know how to run this powerful compound to its full potential.
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05-31-2006, 09:22 PM #15
MGF mechano growth factor
The growth hormone (GH)/IGF-I axis is regarded as an important regulator of muscle mass. However, it is now appreciated that other tissues in addition to the liver express IGF-I and that there are local as well as systemic forms of IGF-I which have different functions. At least two different kinds of IGF-I that are expressed by skeletal muscle are derived from the IGF-I gene by alternative splicing, one of which is expressed in response to physical activity which has now been called ‘mechano growth factor’ (MGF). The other is similar to the systemic or liver type (IGF-IEa) and is important as the provider of mature IGF-I required for upregulating protein synthesis. 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. The ability to produce MGF declines with age, and this is commensurate with the decline in circulating GH levels. GH treatment up regulates the level of IGF-I gene expression in older people and when combined with resistance exercise more is spliced towards MGF and hence should improve the ability of muscle to respond to physical activity.
By combining physiological studies with molecular biology techniques we are beginning to understand the signals, including those of mechanical origin, that are involved in not only switching on or switching off certain genes and also in directing the splicing to give one or more different gene products. One example of this gene splicing is MGF: a growth/repair factor cloned from exercised and/or damaged muscle and that differs from other splice variants of the IGF-I gene. MGF has been found to initiate muscle hypertrophy and local repair process of skeletal muscle by activating muscle stem cells as well as upregulating protein synthesis. It is also expressed in other post mitotic tissue and is neuroprotective as well as cardio-protective but its expression is much reduced in certain diseases and during ageing. Therefore, MGF may have considerable therapeutic potential, particularly as it appears to rapidly increase the strength of normal and diseased muscles as well as enhance their innervation.
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06-10-2006, 10:38 AM #16Originally Posted by Whitey
He could not have said it better!
MGF still works and its active life in cell tissue is up to 48 hours, this coming from a chemist that produced this peptide, all I can say for now about that.
I believe once per week injection may defeat its purpose when injecting after damaging muscle fiber is best, that is my own personal experience based on what I am experiencing with it for the last three weeks now.
In layman temrms, MGF ( IGF-IEc ) is produced by IGF-1 to repair damaged muscle of course is more complicated than that and I will post some info here soon for you guys to read.
Thanks,
Carlo
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06-10-2006, 10:39 AM #17
Hello,
Maybe I can help a little here...
Mechano growth factor increase in IGF-I expression.256
.................................................. .....................................
Research on mechano growth factor: its potential for optimising physical training as well as misuse in doping
G Goldspink
.................................................. .................................
Mechano growth factor can produce rapid increases in muscle and strength, giving it considerable therapeutic and doping
potential
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 for our team to identify and characterise a local muscle growth/repair factor (MGF). This we found is derived from the insulin -like growth factor I (IGF-I) gene by alternative splicing, but, owing to a reading frame shift, MGF has a unique C-terminal peptide. 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. In these conditions it seems that the muscle stem (satellite) cell pool is not adequately replenished.
CLONING OF MGF AND OTHER HUMAN MUSCLE IGF-I SPLICE VARIANTS
For some time it has been apparent that muscle mass and strength must be under the control of local growth factors because if one exercises a particular muscle, it is that muscle and not all the muscles of the body that undergo hypertrophy. A little over 10 years ago, our group set out to clone the factor(s) that are involved in autocrine regulation of muscle mass. For this purpose we needed to have an animal model in which we could make muscle grow rapidly. Previous work had shown that the tibialis anterior muscle in the mature rabbit, when held in the stretched position by plaster cast immobilisation combined with low voltage electrical stimulation, increased in mass by 35% in just over a week.1 It was known that muscles adapt to a new functional length by adding sarcomeres in series at the ends of the existing myofibrils. However, if muscles are also subjected to electrical stimulation, they increase in girth as well as length. Total RNA in these muscles was found to increase by about four times within couple of days. We also studied specific messenger RNAs using a technique known as differential display and detected an mRNA that was expressed in exercised but not in resting muscles.2 This was converted into cDNA and sequenced, and the genome database showed that it was derived from the IGF-I gene. This local type of IGF-I we called mechano growth factor (MGF) as it was expressed in response to mechanical stimuli and because it has different downstream (C-terminal) sequence from the liver or systemic types of IGF-I. From physiological experiments it became apparent that the muscle forms of IGF-I have different functions and that in the case MGF its unique C-terminal peptide has a special function of activating and replenishing the muscle stem (satellite) cell pool. As with the central nervous system, skeletal muscle is a post-mitotic tissue. Therefore there has to be an effective local cellular repair mechanism otherwise cell death will ensue. The extra nuclei required for growth and repair come from the muscle stem (satellite) cells fusing with the muscle fibres. This is also one of the early events in the hypertrophy process. MGF is responsible for replenishing the pool of muscle stem cells,34 and this provides the means by which strength adaptation occurs after exercise and/or local muscle damage.
SPLICING OF THE IGF-I GENE IN RESPONSE TO EXERCISE AND HORMONES
Previous research had shown that resistance exercise which results in muscle hypertrophy is associated with an IGF-I. As mentioned above, the way MGF was discovered was by studying the RNA transcript of exercised and non-exercised muscle.2 Shortly after this, the group of Ken Baldwin and Greg Adams in the United States7 showed that MGF is expressed earlier than IGF-IEa in response to exercise. Using specific primers (gene probes), we measured the mRNA concentrations of MGF and IGF-IEa using quantitative polymerase chain reaction mechanically in overloaded rodent muscle8 as well as in human volunteers in which muscle biopsy specimens were taken 2.5 hours after a single bout of high intensity exercise of knee extensor muscles.9 In young muscle, MGF mRNA concentrations were significantly increased as a result of resistance exercise, but no significant change was observed in older muscle when subjected to the same degree of mechanical overload. a However, elderly male volunteers when given growth hormone combined with exercise training produced increased concentrations of MGF,10 which could be correlated with increased muscle cross sectional area as determined from computed tomography scans.
Figure 1
shows the way the IGF-I gene is spliced after exercise and in response to hormones. It was noted that in exon 5 of MGF in the human there is a 49 base insert (52 a in the rat) which results in a reading frame shift. Amino acids are coded for by triplets of bases. As the exon 5 insert is not a multiple of 3, the downstream peptide sequence of MGF is different from that of the other kinds of IGF-I. This region has important functional consequences as the carboxy peptide of some IGF-I isoforms is involved in the recognition of the specific binding proteins that stabilise these growth factors. At least two forms of systemic IGF-I are expressed by muscle even at rest. However, it is apparent that in response to exercise and/or damage, MGF is expressed locally and that it has a dual action. This includes activating the muscle stem cell pool through its C-Terminal domain (encoded in exons 5 and 6) and increasing anabolic effects as the result of its IGF-I receptor binding domain (encoded in exons 3 and 4), which all the IGF-I genes possess.
Figure 1 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-I as the 49 base insert in the exon creates a reading frame shift so that the downstream or C-terminal peptide sequence is different. This unique peptide has been found to be involved in activating the muscle stem cells and to ‘‘kick start’’ the tissue repair and/or hypertrophy processes. In the elderly, who are growth hormone (GH) deficient, there is an improvement in MGF expression when administration of recombinant human GH is combined with exercise.
Reg Seqn, Regulatory sequence.
surprise a single intramuscular injection into a mouse muscle resulted in a 25% increase in mean muscle fibre cross section area within three weeks.11 Similar experiments have been carried out using the systemic or liver type of IGF-I 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-I, which is common to all the splice variants.12 The use of the DNA of IGF-I and particularly MGF is therefore a prime candidate for gene doping for enhancement of athletic performance. This presents the anti-doping agencies with a challenge, as the range of vectors available for use in engineering these genes enable them to be designed so that the gene product can be delivered locally or systemically and also so that they can be switched on and switched off after they have been introduced into the body. Our research unit is using the extremely sensitive and specific reverse transcriptase polymerase chain reaction
to amplify a vector and/or the enhancer cDNA as a means of detecting gene doping. We also know that MGF as well as IGF-I exist as class I and class 2 isoforms and that the ratios of these in serum change if they are introduced as the peptide or by gene transfer. Therefore there is the possibility of detecting the misuse of these strength generating substances even if delivered in the form of ‘‘gene doping’’.
ACKNOWLEDGEMENTS
The work described in this Review was supported by the Wellcome Trust, Action Research, the International Olympic Games WADA committee.
Br J Sports Med 2005;39:787–788.REFERENCES
doi: 10.1136/bjsm.2004.015826
Correspondence to: Professor Goldspink,
Department of Surgery, Royal Free and
University College Medical School, Hampstead
Campus, Rowland Hill Street, London NW3
2PF, UK; [email protected]
Competing interests: none declared
1 Goldspink G, Scutt A, Loughna P, et al. Geneexpression in skeletal muscle in response tomechanical signs. Am J Physiol1992;262:R326–63.
2 Yang SY, Alnaqeeb M, Simpson H, et al. Cloning and characterisation of an IGF-I isoform expressed in skeletal muscle subjected to stretch. J Muscle Res Cell Motil 1996;17:487–95.
3 Yang SY, Goldspink G. Different roles of the IGF-
IEc peptide (MGF) and mature IGF-I in myoblast proliferation and differentiation. FEBS Lett 2002;522:156–60.
4 Hill M, Goldspink G. Expression and splicing of the insulin-like growth factor gene in rodent muscle is associated with muscle satellite (stem) cell activation following local tissue damage. J Physiol 2003;549:409–18.
5 Yan Z, Biggs RB, Booth FW. Insulin-like growth factor immunoreactivity increases in muscle after acute eccentric contractions. J Appl Physiol 1993;74:410–14.
6 Czerwinski SM, Martin JM, Bechtel PJ. Modulation of IGF mRNA abundance during stretch-induced skeletal muscle hypertrophy and regression. J Appl Physiol, 1994;76:2026–30.
7 Haddad F, Adams GR. Selected contribution:acute cellular and molecular responses toresistance exercise. J Appl Physiol2002;93:394–403.
8 Owino V, Yang SY, Goldspink G. Age-related loss of skeletal muscle function and the inability to express the autocrine form of insulin-like growth factor-1 (MGF) in response to mechanical overload. FEBS Lett 2001;505:259–63.
9 Hameed M, Orrell RW, Cobbold M, et al. Expression of IGF-I splice variants in young and old human skeletal muscle after high resistance exercise. J Physiol 2003;547:247–54.
10 Hameed M, Lange KH, Andersen JL, et al. The effect of recombinant human growth hormone and resistance training on IGF-I mRNA expression in the muscles of elderly men. J Physiol 2004;555:231–40.
11 Goldspink G, Yang SY. Method of treating muscular disorders. United States Patent. Patent No US 6,221,842 B1, Apr 24, 2001.
12 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.
COMMENTARY
The control of muscle growth is an important area of research in clinical and sports medicine. The team lead by Geoff Goldspink in London have made a significant contribution to the characterisation and function of growth factors in skeletal muscle. This leader is a summary of their work to date. It details the regulatory control and biological functions of spliced variants of the IGF-I gene and the potency and mechanism of action of the protein products. Genuine therapeutic potential is much in evidence from this work, but with athletes ever more informed of the potential of gene doping the article also serves to remind us of the challenges that lie ahead if we are to tackle ‘‘gene doping’’ for performance gain.
P Jakeman
Department of Physical Education and Sport
Sciences, University of Limerick, Limerick,
Ireland; [email protected]
www.bjsportmed.com
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06-10-2006, 01:59 PM #18
mgf
Originally Posted by inevitable
Locally around the muscle injected it becomes very full and it feels as though you have already finished a workout before you have even picked up a weight. So what has MGF done for me.......I have injected my chest, bi's, tri's, and most of all my delts. I look alot thicker and fuller. I have been cutting down from 195lbs. since Feb. for summer, I am now around 184lbs with 8.1% bodyfat. I have added 1/4" to my right (dominate arm) and almost 1/2" to my left arm-all while I have lost 11 lbs.
Many people have commented on how much bigger I look, and I am here to tell you that I do look bigger and I have the above measurements to prove it. IGF gave me good pumps and adequate fat loss, MGF has definately added muscle mass to my frame. My only complaint during the last 2 months, and it may have nothing to do with the MGF: My fingers go numb from time-to-time and my forearms are always tight.
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07-02-2006, 12:55 PM #19RETIRED VET
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Wow nice read guys, thanks for joinin us Logan...so which do you prefer then overall? IGF or MGF?
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12-30-2024, 06:57 AM in ANABOLIC STEROIDS - QUESTIONS & ANSWERS