MGF Peptide UK: Mechano Growth Factor Research, Mechanism and Study Data

In the mid-1990s, a team at the Royal Free Hospital in London stretched a rabbit muscle and caught a gene changing its mind. The gene was IGF-1, one of the body’s best-known growth signals. Resting muscle made the usual version. Stretched muscle started making a second version that had barely been noticed before, with a different tail on the end. The researchers came to call it mechano growth factor, or MGF: a growth signal that muscle seems to make for itself when it is put under strain.

That discovery opened a line of research that has since reached the heart, the brain, tendon and bone. This guide explains what MGF actually is, how a single gene can produce more than one growth factor, what the cell and animal studies have found, why some laboratories could not reproduce the early results, and how MGF compares with IGF-1 LR3 and the tissue repair peptides it is often grouped with. MGF is sold by Crown Peptides strictly for laboratory research use only, and everything below is written for readers interested in the science. You can find it on our MGF Research Peptide page, part of our musculoskeletal research peptides category.

What Is MGF, and Why Does a Muscle Make Its Own Version of IGF-1?

MGF stands for mechano growth factor. It is the name given to one particular form of insulin-like growth factor 1 (IGF-1) that muscle produces in response to stretch, overload or damage. The “mechano” part is the clue: it was found because of a mechanical signal, not a hormonal one.

Most people know IGF-1 as a hormone made mainly by the liver in response to growth hormone, travelling round the body in the blood. But the IGF-1 gene is more flexible than that. Cells can cut and join its message in different ways, a process called alternative splicing, and each version produces a slightly different precursor protein. The main forms share the same core IGF-1 molecule but carry different tails, known as E-domains or E-peptides. MGF is the form with the unusual tail.

Is MGF the same as IGF-1Ec?

In humans, yes. The human splice variant is called IGF-1Ec, and in rodents the equivalent form is called IGF-1Eb. That naming difference causes a lot of confusion, because human IGF-1Eb is a different form again. Researchers often sidestep the problem by saying “MGF”, “IGF-1Ec/MGF” or “human Ec / rodent Eb”. If you see any of those terms in a paper, they are usually describing the same biology.

The splice variant and the peptide in the vial are not the same thing

This is the part most people miss. “MGF” is used for two different things. The first is the natural splice variant: a full-length precursor protein containing mature IGF-1 plus the MGF E-domain. The second is a short synthetic peptide made of the last 24 amino acids of that E-domain. This 24-residue peptide, sometimes written MGF-Ct24E or MGF E-peptide, is what is sold as MGF peptide and what most of the laboratory studies used. It does not contain the IGF-1 part at all. Keeping that difference in mind makes the rest of the research story much easier to follow.

The Stretched Muscle That Started It All

The MGF story belongs to Geoffrey Goldspink and his colleagues at the Royal Free Hospital School of Medicine, later the Royal Free and University College Medical School in London. Goldspink had spent years asking a deceptively simple question: how does a muscle know it is being worked, and how does it turn that physical signal into growth?

In a 1996 paper, Yang, Goldspink and colleagues analysed rabbit muscle that had been made to grow rapidly using active stretch. Resting muscle produced one main IGF-1 form. Stretched muscle produced an additional form whose E-domain carried a 52 base pair insert, enough to shift the genetic reading frame and give the precursor protein a completely different tail. Using primers designed for both rabbit and human sequences, the team detected appreciable levels of this variant in muscle after altered physical activity lasting from 2 hours to 6 days, while very little, if any, could be found in muscle that had not been stretched or worked (PMID: 8884603).

Three years later, the same group described the variant as mechano-growth factor, apparently designed for local, autocrine and paracrine action rather than travelling round the body. In rabbit muscle, stretch alone markedly increased both IGF-1 forms within 4 days. Stretch combined with electrical stimulation increased them even more, while electrical stimulation without stretch produced no significant rise (PMID: 10087355). Stretch, not simply activity, was the trigger.

A pulse, then a hand-over

Here is where it gets interesting. In 2003, Hill and Goldspink followed the timing of IGF-1 splicing in rat muscle after two kinds of local damage. MGF appeared quickly and then declined within a few days. The systemic form, IGF-1Ea, rose more slowly, and its increase matched the fall in MGF. Markers of satellite cell activation, including M-cadherin and MyoD, appeared in a sequence suggesting that the early pulse of MGF was what woke the muscle’s stem cells, while the later IGF-1Ea supplied the mature IGF-1 needed to finish the repair (PMID: 12692175). In other words, the gene seemed to switch products partway through the repair job.

The age connection

The next question was obvious: what happens in older muscle? In a rat overload study, older muscles that failed to grow in response to extra load showed considerably lower MGF expression and failed to raise IGF-1 receptor and MyoD levels (PMID: 11566187). Then came a small human study. Eight young adults aged 25 to 36 and seven older adults aged 70 to 82 performed a single heavy bout of knee extensor exercise, with muscle samples taken 2.5 hours later. At rest, MGF levels were about 100-fold lower than IGF-1Ea. After exercise, MGF rose significantly in the young group but not in the older group, while IGF-1Ea did not change in either (PMID: 12562960). It measured messenger RNA rather than the protein, and it was a small group, but it gave the field one of its most quoted ideas: that older muscle may be less able to switch on its own local repair signal.

How MGF Is Thought to Work

MGF research has produced a picture of a local, short-lived signal that helps start repair. Here is the plain-English version of the main ideas, along with where the evidence comes from.

A first-responder signal after strain

Unlike liver IGF-1, which circulates throughout the body, MGF is thought to act close to where it is made. The timing studies suggest it appears early after strain or damage, does its job and fades as the more familiar IGF-1Ea takes over (PMID: 12692175). That makes it a natural candidate for the “go” signal at the start of tissue repair.

Waking up satellite cells

Muscle fibres cannot divide. To repair or grow, they rely on satellite cells, a reserve of stem cells that sit quietly on the fibre surface until they are needed. Once activated, satellite cells multiply and then fuse into the fibre to donate new nuclei. In a cell study, Yang and Goldspink found that the MGF E-domain increased myoblast proliferation while holding back terminal differentiation, the opposite pattern from mature IGF-1, which pushes cells towards fusing (PMID: 12095637). The idea is that MGF expands the pool of repair cells first, and IGF-1 then helps turn them into muscle.

A signal that may work through a different route

In that same study, blocking the IGF-1 receptor with an antibody did not stop the MGF E-domain’s effect, which suggested it acts through a different receptor (PMID: 12095637). Later work in heart cells found that a synthetic MGF E-domain peptide entered cells rapidly, without IGF-1 receptor activation, and ended up in the nucleus (PMID: 23712705). Not every laboratory agrees, as we will see shortly, and no specific MGF receptor has yet been identified.

A survival signal for stressed cells

The fourth recurring theme is cell survival. Across heart and nerve studies, the MGF E-peptide has been reported to reduce programmed cell death, for example by protecting the mitochondrial membrane and preventing activation of caspase-3, one of the enzymes that carries out cell death (PMID: 23712705). That anti-apoptotic theme is what took MGF research well beyond skeletal muscle.

What the Research Has Actually Found

MGF research spans about three decades and several organ systems. Almost all of it comes from cell cultures and animal models, so the findings below describe what happened in those settings. Here they are, area by area.

Muscle stem cells and progenitors

Some of the most direct evidence comes from human muscle cells grown in the laboratory. In primary cultures from healthy people and from people with muscular dystrophy or ALS, the MGF E-peptide significantly increased the number of progenitor cells, while IGF-1 pushed cells towards differentiation instead (PMID: 17531227).

A 2011 study from the Institut de Myologie in Paris took the age question into the dish. The 24-residue MGF E-peptide significantly increased the proliferative life span and delayed senescence of satellite cells taken from newborn and young adult muscle, though not from older adult muscle. In all cultures, it was associated with larger myotubes and fewer reserve cells (PMID: 21354439).

Movement matters too. A team in Quebec found that the MGF-Ct24E peptide made human myogenic precursor cells more mobile, in the dish and in muscle, by raising u-PA, u-PAR and MMP-7 while lowering PAI-1 activity, a combination that helps cells move through tissue. Their results again suggested a mechanism that did not involve the IGF-1 receptor (PMID: 17156777).

The heart

The heart is one of the most striking chapters. In a sheep study from New Zealand, with Goldspink among the authors, heart attacks were induced experimentally and the animals were given vehicle, mature IGF-1, the MGF E-domain or full-length MGF at 200 nM. In a second experiment comparing the E-domain alone with vehicle, the E-domain preserved cardiac function and the animals had 35% less compromised heart muscle than controls. Staining for cleaved caspase-3 was absent in the E-domain group (PMID: 17581790).

Pamela Goldspink’s group in Chicago followed up in mice. A synthetic MGF E-domain peptide given at the time of heart attack lessened the decline in systolic and diastolic function at 2 weeks, preserved contractility, held back harmful enlargement of the heart and resulted in significantly fewer dying cells in the surviving heart muscle (PMID: 23712705). A later study delivered the peptide from tiny gel rods sized to match a heart muscle cell. In mice, it reduced mortality, lessened the decline in heart function and delayed decompensation over 10 weeks (PMID: 25678113). A related mouse study using a stabilised version of the peptide found that delivery within 12 hours of injury delayed decompensation, while delivery 8 weeks later improved systolic function (PMID: 25606570).

Neurons and the brain

MGF’s survival effects have also been studied in nerve tissue. In a gerbil model of temporary loss of blood flow to the brain, the synthetic MGF C-terminal peptide gave very significant protection to vulnerable neurons. In hippocampal tissue slices, it was as potent as full-length IGF-1, its effect lasted significantly longer, and the two acted additively. Its protective action did not depend on the IGF-1 receptor (PMID: 16144956).

Two further studies used genetic methods rather than the peptide, gene delivery in one and genetically engineered mice in the other, which is worth knowing when reading them. In SOD1 mice, a standard model of ALS, delivering either IGF-1 or MGF genes into hindlimb muscle at symptom onset improved muscle strength and motor neuron survival, with significantly more motor neurons surviving in the MGF group (PMID: 19038252). At the Mayo Clinic, researchers found that natural MGF levels in the brain’s neurogenic areas fell with age. Mice engineered to overproduce MGF had more newly dividing cells in the hippocampus, and when overproduction began at 1 or 3 months of age, the mice showed more new neurons in the olfactory bulbs and preserved sense of smell at 24 months. Starting at 12 months did not produce that effect (PMID: 28683812).

Tendon and bone

Musculoskeletal research has looked beyond muscle. In rats with injured Achilles tendons, a synthetic MGF E-peptide called MGF-C25E significantly improved a functional walking score compared with saline, and repaired tendons were significantly stiffer in the 1000 ng/ml group (PMID: 27334712). A bone study classified 52 MGF E-peptide variants from different species, synthesised the main types and found that one, T-MGF-19E, promoted proliferation, differentiation and mineralisation of bone-forming cells and supported bone defect healing in rabbits (PMID: 32339623).

The debate: does the synthetic peptide act like the natural variant?

Any honest look at MGF has to include this. In 2014, scientists at two pharmaceutical companies tried to reproduce the classic muscle cell findings. MGF peptide at concentrations up to 500 ng/ml did not increase proliferation of mouse C2C12 cells or primary human myoblasts, did not hold back differentiation, and had no significant effect on primary mouse muscle stem cells. Mature IGF-1 and full-length IGF-1Eb produced clear responses in the same experiments. Neither the native nor a stabilised MGF peptide reproduced a reported signalling effect in heart muscle cells. The authors concluded that their results called into question a physiological role for the MGF peptide (PMID: 24253050).

Two other lines of work shape the debate. A 2010 review in Endocrinology pointed out that, at that time, no free MGF peptide had been isolated from cells, tissues or body fluids, so the synthetic peptide’s actions needed to be kept separate from those of the natural splice variant (PMID: 20130113). And a University of Pennsylvania study found that rodent E-peptides did need the IGF-1 receptor: they increased its activation by IGF-1 by improving its availability on the cell surface, rather than acting through a separate receptor (PMID: 23029120).

The story has moved on since. In 2017, a team in Athens reported, for the first time, that the human Ec peptide and its rodent Eb counterpart are produced in living tissue alongside their precursor, in muscle, liver and heart. They also showed that the enzyme furin can cut the precursor to release the free peptide, with early evidence that the Ec peptide is regulated differently during muscle regeneration after exercise-induced damage in humans (PMID: 27836414). So the natural peptide does appear to exist. What is still open is how closely a synthetic 24-residue fragment, delivered from outside, reproduces what that natural peptide does in context.

Why might laboratories disagree?

Several explanations have been suggested in the literature, including differences in cell types, peptide versions, concentrations and timing. The E-peptide’s effects may also depend on how much IGF-1 is present, as the Pennsylvania work suggests. A 2012 commentary by Zabłocka and both Goldspinks summed up the question in its title: is MGF an important cog or a loose screw in the repair machinery (PMID: 23125840)? It is one of the more interesting unresolved questions in growth factor biology.

MGF Research Peptide

HPLC and MS verified · certificate with every batch · pricing announced when stock arrives

statusComing soonView MGF Research Peptide

MGF vs IGF-1 LR3: Two Very Different Takes on the Same Gene

MGF is most often compared with IGF-1 LR3, and the comparison is useful because the two come from the same gene but take opposite approaches.

IGF-1 LR3 is built on the mature IGF-1 molecule itself. Australian researchers created it in the early 1990s by swapping the glutamic acid at position 3 for arginine and adding a 13-amino acid extension to the front. In cell lines that release IGF-binding proteins, the Long [Arg3] form was more potent than natural IGF-1 (PMID: 1378742). It is designed to avoid the IGF-binding proteins that normally hold IGF-1 back, so more of it stays free to act at the IGF-1 receptor, and it is studied as a systemic growth signal. Our IGF-1 LR3 guide covers it in depth.

MGF contains none of the IGF-1 part. It is built from the tail that is cut off, and it is studied as a local, early-stage repair signal. Its strongest reported effects are on cell numbers, migration and survival rather than the protein-building effects classically linked to IGF-1.

One study neatly shows the gap. Full-length MGF protein, which contains mature IGF-1, strongly activated the IGF-1 receptor, reaching an 89-fold maximal response against 77-fold for IGF-1 itself, though it needed higher concentrations to get there. The 24-residue human MGF peptide and a stabilised analogue known as Goldspink-MGF did not activate the receptor at all (PMID: 26991004). So researchers who want to study the IGF-1 receptor directly tend to reach for IGF-1 LR3, while researchers interested in the E-domain’s own biology use MGF.

How MGF relates to TB-500 and BPC-157

MGF is often grouped with TB-500 and BPC-157 because all three are studied in tissue repair, but they come from different biology. TB-500 is a synthetic peptide based on thymosin beta-4, a protein involved in actin handling and cell movement. BPC-157 is a 15-amino acid peptide derived from a protein found in gastric juice. MGF, by contrast, is a direct product of the IGF-1 gene and is most closely tied to muscle satellite cells. For a side-by-side look at the other two, see BPC-157 vs TB-500.

Where MGF Research Goes From Here

MGF sits in an exciting position: a well-defined natural signal, an intriguing set of cell and animal results, and some of the biggest open questions are now answerable with modern tools.

The natural peptide in action. Now that the free Ec peptide has been detected in tissue, researchers can ask how much is released after injury, where it goes and how long it lasts. That will help connect the synthetic peptide data to real physiology.

The receptor question. Some studies point to a route independent of the IGF-1 receptor, others to a helper role at that receptor. Heart research has started to map MGF E-domain partners inside cells: a 2022 mouse study linked one phosphorylation site in the E-domain to 14-3-3 proteins and to changes in heart muscle contraction (PMID: 36467694). Partners like these may help explain the nuclear localisation seen in earlier work.

Better delivery. The gel rod and microsphere studies show a growing interest in keeping MGF where it is needed and releasing it slowly. That local approach fits the biology of a signal that seems designed to act close to its source.

Ageing tissue. The human exercise study, the rat overload data and the brain studies all point the same way: the MGF response appears to weaken with age. Whether restoring it changes anything in older tissue is one of the most interesting questions in the field.

Independent replication. After the 2014 replication study, the most valuable work will be carefully controlled experiments that compare native and modified peptides side by side, in the same cells, at the same concentrations.

The Technical Breakdown: Exons, E-Domains and the 24-Residue Peptide

This section is for readers who want the molecular detail. Everything above makes sense without it.

How the IGF1 gene makes three precursors

The human IGF1 gene has six exons. Different combinations of transcription start sites and splicing produce three main precursor proteins in humans: IGF-1Ea, IGF-1Eb and IGF-1Ec. All three share the same mature IGF-1 sequence, which is the part that binds the IGF-1 receptor. They differ in their C-terminal E-peptides, which are normally removed by enzymes during processing (PMID: 24637928). IGF-1Ec, the human MGF, includes a 49 base pair insert from exon 5 (52 base pairs in rodents), which shifts the reading frame and gives the Ec peptide its unique C-terminal sequence (PMID: 21354439).

The 24-residue peptide and its variants

The native human MGF peptide corresponds to the last 24 amino acids of the Ec E-domain: YQPPSTNKNTKSQRRKGSTFEERK, with a molecular weight of about 2,868 Da. Several modified versions have been described in the scientific literature. Doping control laboratories have characterised a version with a C-terminal amide (PMID: 22328223) and a version in which the arginine at position 23 is replaced by histidine, known as MGF R23H, which showed good stability in plasma (PMID: 28035768). Stabilised analogues such as Goldspink-MGF have also been used in research (PMID: 26991004). Each version has a different exact mass, which is why identity testing matters so much for this compound.

Concentrations used in the studies

Published studies have used a wide range of concentrations: 200 nM in the sheep heart study, up to 500 ng/ml in the 2014 replication study and 1000 ng/ml in the rat tendon study. Those figures are useful for understanding the pharmacology. They are not guidance for laboratory work, where concentrations depend entirely on the experiment. Our understanding quantities guide explains how milligram figures relate to research solutions.

Why Identity Testing Matters So Much for MGF

With most peptides, the main question is purity. With MGF, there is a second question that matters just as much: which MGF is in the vial? As the technical section shows, the native 24-residue peptide, the amidated version, the R23H variant and stabilised analogues are all described in the literature, and they are not interchangeable. Doping control laboratories have found unlabelled MGF analogues in products bought on the black market (PMID: 22328223). For a research field where laboratories already disagree about results, starting with the wrong version of the peptide is the last thing anyone needs.

That is why mass spectrometry is so important here. Each MGF version has its own exact mass, so a mass spectrum confirms not just that a vial contains “an MGF peptide” but which one. MGF is also a short, highly charged peptide with several lysine and arginine residues, so a clean purity profile is the best evidence that no truncated or modified chains are present.

What every Crown Peptides batch comes with

Every batch we sell is tested before it reaches the shop. HPLC (high-performance liquid chromatography) separates the target peptide from anything else in the vial and measures its purity. Mass spectrometry measures the molecule’s mass to confirm its identity. The results are published as a certificate of analysis for that exact batch on our Lab Reports page, and the batch number on your vial matches the certificate. Our guide on how to read a peptide certificate of analysis explains every section, and how to tell if peptides are real covers the warning signs to look out for.

Stored, packed and dispatched properly

Our peptides are supplied as lyophilised (freeze-dried) powder, the most stable form for storage and transport. Short peptides like MGF are prone to enzyme breakdown once dissolved, so careful handling matters. Vials are kept cold, sealed and away from light and moisture, as set out on our storage information page, and our guide to how long peptides last covers stability once a vial is opened. Weekday orders placed before 2pm are dispatched the same day from the UK, and UK delivery is free on orders over £100.

A UK company you can actually talk to

Crown Peptides is a UK company. Our team replies to enquiries within 24 hours on business days, and WhatsApp is the quickest way to reach us. If you have a question about a certificate, a batch or a compound in our range, you can get in touch.

Related Compounds Worth Knowing About

MGF sits in a family of compounds studied for muscle, growth and tissue repair. Some work on the same IGF-1 system from a different angle, and others take a completely different route to repair. Most can be found in our musculoskeletal research peptides category.

PEG-MGF

PEG-MGF is MGF with polyethylene glycol chains attached, a modification designed to make a short-lived peptide last longer. It raises a different set of research questions from the native peptide, which we cover in our PEG-MGF guide.

IGF-1 LR3

IGF-1 LR3 is the long-acting analogue of mature IGF-1, the part of the molecule MGF leaves out. It is the tool of choice for studying the IGF-1 receptor directly, which makes it a natural point of comparison for MGF.

BPC-157 + TB-500 (Wolverine Stack)

The BPC-157 + TB-500 Blend (Wolverine Stack) combines two of the most widely studied tissue repair peptides in one vial. Where MGF is tied to muscle satellite cells, these two are studied for blood vessel growth, cell migration and tendon and ligament repair. Our article on the Wolverine Stack explains the pairing.

Ipamorelin

Ipamorelin works much further upstream. It prompts the pituitary to release growth hormone, which in turn drives IGF-1 production in the liver and other tissues. It is studied as a selective way to raise growth hormone without large effects on other pituitary hormones.

CJC-1295 (No DAC) + Ipamorelin

The CJC-1295 (No DAC) + Ipamorelin (Blend) pairs a growth hormone-releasing hormone analogue with Ipamorelin, so the pituitary receives two signals through two different receptors. It sits at the top of the same growth hormone and IGF-1 chain that MGF branches off at the very end.

MOTS-c

MOTS-c is a peptide encoded in mitochondrial DNA and studied for how muscle cells handle glucose and energy. It brings a metabolic angle to muscle research that complements MGF’s focus on repair and stem cells.

For a wider overview, see our guide to the best peptides for muscle research, or browse our musculoskeletal research peptides.

Common Questions About MGF

What does MGF stand for?

MGF stands for mechano growth factor. The name reflects how it was found: a form of IGF-1 that muscle produces when it is stretched or put under load.

Is MGF the same as IGF-1?

No. MGF is made from the same gene as IGF-1 but is a different splice variant, IGF-1Ec in humans. The research peptide sold as MGF is a 24-amino acid fragment of that variant’s tail and contains none of the IGF-1 molecule itself.

What is the difference between MGF and PEG-MGF?

PEG-MGF is the same peptide with polyethylene glycol attached to slow its breakdown and extend how long it lasts. Native MGF is short-lived and studied as a local signal. Our PEG-MGF guide explains what that change means for research.

What has MGF been studied for?

MGF has been studied in muscle satellite cells and progenitor cells, heart muscle after experimental heart attack, nerve cell survival, tendon healing and bone formation. Almost all of that work has been done in cell cultures and animal models, so the findings describe what happened in those settings.

Has MGF been studied in people?

There are no registered clinical trials of MGF peptide. Human research so far has measured natural MGF levels in muscle, for example the small exercise study comparing young and older adults, and human muscle cells grown in the laboratory.

Why do some studies disagree about MGF?

A 2014 study from two pharmaceutical companies could not reproduce several of the classic cell findings with the synthetic peptide. Researchers have suggested differences in peptide versions, cell types, concentrations and timing. The discovery that the natural Ec peptide is produced in tissue has given the field new ways to test the question.

Is MGF legal in the UK?

MGF is not listed under the Misuse of Drugs Act and can be bought in the UK for laboratory research. It does appear on the World Anti-Doping Agency’s prohibited list, which applies to competitive sport. Our article are peptides legal in the UK explains how UK law handles research peptides.

Can I buy MGF in the UK?

Yes. Crown Peptides supplies MGF in 2mg vials, within our musculoskeletal research peptides category. Because several MGF versions exist, look for a batch-specific certificate that confirms by mass spectrometry exactly which peptide is in the vial.

How should MGF be stored?

As a lyophilised powder, MGF is best kept cold, sealed and away from light. Once reconstituted, short peptides like MGF are more vulnerable to breakdown, so they are usually kept refrigerated and used promptly. Our storage information page has the details.

The Signal a Muscle Makes for Itself

MGF began with a simple observation in a London laboratory: stretch a muscle and its IGF-1 gene starts writing a different message. From there, the research has followed that signal into stem cells, the heart, the brain, tendon and bone. It has also been tested by one of the most useful things in science, a laboratory that could not reproduce the result.

That combination is exactly what makes MGF interesting right now. The natural peptide has been found in living tissue. The delivery methods are getting smarter. And the biggest questions, from the receptor it uses to what happens to its signal as tissue ages, can finally be answered with careful, well-controlled experiments. The next round of studies will decide whether MGF is the cog or the loose screw.

For researchers who want to be part of that work, the MGF Research Peptide is ready to order, and every compound in our musculoskeletal research peptides range comes HPLC and MS verified, with its certificate published in full and dispatched from the UK.

References

• Yang S, Alnaqeeb M, Simpson H, et al. Cloning and characterization of an IGF-1 isoform expressed in skeletal muscle subjected to stretch. J Muscle Res Cell Motil. 1996;17:487-95. PMID: 8884603
• McKoy G, Ashley W, Mander J, et al. Expression of insulin growth factor-1 splice variants and structural genes in rabbit skeletal muscle induced by stretch and stimulation. J Physiol. 1999;516 ( Pt 2):583-92. PMID: 10087355
• 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. PMID: 12692175
• 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. PMID: 11566187
• 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. PMID: 12562960
• Yang SY, Goldspink G. Different roles of the IGF-I Ec peptide (MGF) and mature IGF-I in myoblast proliferation and differentiation. FEBS Lett. 2002;522:156-60. PMID: 12095637
• Ates K, Yang SY, Orrell RW, et al. The IGF-I splice variant MGF increases progenitor cells in ALS, dystrophic, and normal muscle. FEBS Lett. 2007;581:2727-32. PMID: 17531227
• Kandalla PK, Goldspink G, Butler-Browne G, et al. Mechano Growth Factor E peptide (MGF-E), derived from an isoform of IGF-1, activates human muscle progenitor cells and induces an increase in their fusion potential at different ages. Mech Ageing Dev. 2011;132:154-62. PMID: 21354439
• Mills P, Lafrenière JF, Benabdallah BF, et al. A new pro-migratory activity on human myogenic precursor cells for a synthetic peptide within the E domain of the mechano growth factor. Exp Cell Res. 2007;313:527-37. PMID: 17156777
• Carpenter V, Matthews K, Devlin G, et al. Mechano-growth factor reduces loss of cardiac function in acute myocardial infarction. Heart Lung Circ. 2008;17:33-9. PMID: 17581790
• Mavrommatis E, Shioura KM, Los T, et al. The E-domain region of mechano-growth factor inhibits cellular apoptosis and preserves cardiac function during myocardial infarction. Mol Cell Biochem. 2013;381:69-83. PMID: 23712705
• Shioura K, Pena J, Goldspink P. Administration of a Synthetic Peptide Derived from the E-domain Region of Mechano-Growth Factor Delays Decompensation Following Myocardial Infarction. Int J Cardiovasc Res. 2014;3:1000169. PMID: 25606570
• Peña JR, Pinney JR, Ayala P, et al. Localized delivery of mechano-growth factor E-domain peptide via polymeric microstructures improves cardiac function following myocardial infarction. Biomaterials. 2015;46:26-34. PMID: 25678113
• Solís C, Thompson WC, Peña JR, et al. Mechano-growth factor E-domain modulates cardiac contractile function through 14-3-3 protein interactomes. Front Physiol. 2022;13:1028345. PMID: 36467694
• Dluzniewska J, Sarnowska A, Beresewicz M, et al. A strong neuroprotective effect of the autonomous C-terminal peptide of IGF-1 Ec (MGF) in brain ischemia. FASEB J. 2005;19:1896-8. PMID: 16144956
• Riddoch-Contreras J, Yang SY, Dick JR, et al. Mechano-growth factor, an IGF-I splice variant, rescues motoneurons and improves muscle function in SOD1(G93A) mice. Exp Neurol. 2009;215:281-9. PMID: 19038252
• Tang JJ, Podratz JL, Lange M, et al. Mechano growth factor, a splice variant of IGF-1, promotes neurogenesis in the aging mouse brain. Mol Brain. 2017;10:23. PMID: 28683812
• Zhang B, Luo Q, Kuang D, et al. Mechano-growth factor E peptide promotes healing of rat injured tendon. Biotechnol Lett. 2016;38:1817-25. PMID: 27334712
• Wei W, Liu S, Song J, et al. MGF-19E peptide promoted proliferation, differentiation and mineralization of MC3T3-E1 cell and promoted bone defect healing. Gene. 2020;749:144703. PMID: 32339623
• Fornaro M, Hinken AC, Needle S, et al. Mechano-growth factor peptide, the COOH terminus of unprocessed insulin-like growth factor 1, has no apparent effect on myoblasts or primary muscle stem cells. Am J Physiol Endocrinol Metab. 2014;306:E150-6. PMID: 24253050
• Matheny RW Jr, Nindl BC, Adamo ML. Minireview: Mechano-growth factor: a putative product of IGF-I gene expression involved in tissue repair and regeneration. Endocrinology. 2010;151:865-75. PMID: 20130113
• Brisson BK, Barton ER. Insulin-like growth factor-I E-peptide activity is dependent on the IGF-I receptor. PLoS One. 2012;7:e45588. PMID: 23029120
• Vassilakos G, Philippou A, Koutsilieris M. Identification of the IGF-1 processing product human Ec/rodent Eb peptide in various tissues: Evidence for its differential regulation after exercise-induced muscle damage in humans. Growth Horm IGF Res. 2017;32:22-28. PMID: 27836414
• Janssen JA, Hofland LJ, Strasburger CJ, et al. Potency of Full-Length MGF to Induce Maximal Activation of the IGF-I R Is Similar to Recombinant Human IGF-I at High Equimolar Concentrations. PLoS One. 2016;11:e0150453. PMID: 26991004
• Zabłocka B, Goldspink PH, Goldspink G, et al. Mechano-Growth Factor: an important cog or a loose screw in the repair machinery?. Front Endocrinol (Lausanne). 2012;3:131. PMID: 23125840
• Francis GL, Ross M, Ballard FJ, et al. Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological potency. J Mol Endocrinol. 1992;8:213-23. PMID: 1378742
• Philippou A, Maridaki M, Pneumaticos S, et al. The complexity of the IGF1 gene splicing, posttranslational modification and bioactivity. Mol Med. 2014;20:202-14. PMID: 24637928
• Esposito S, Deventer K, Van Eenoo P. Characterization and identification of a C-terminal amidated mechano growth factor (MGF) analogue in black market products. Rapid Commun Mass Spectrom. 2012;26:686-92. PMID: 22328223
• Cox HD, Miller GD, Eichner D. Detection and in vitro metabolism of the confiscated peptides BPC 157 and MGF R23H. Drug Test Anal. 2017;9:1490-1498. PMID: 28035768