TL;DR
The satellite-cell signal with a five-to-seven-minute half-life. Zero human RCTs since Goldspink's lab described it.
What is it? The 24-amino-acid C-terminal E-peptide from the IGF-1Ec splice variant. Muscle produces it locally in response to mechanical loading. Synthesized as a research peptide.
What does it do? Activates quiescent Pax7-positive satellite cells, the stem cells beneath muscle fibers that donate nuclei during repair and hypertrophy. Also anti-apoptotic in cardiac and neural tissue under ischemia.
Does the evidence hold up? Preclinical story is rich (Yang 2002, Hill 2003, Goldspink 2005, Carpenter 2008). Human side: zero RCTs. Community dosing is allometric guesswork. PEG-MGF may not reproduce the local-pulse biology it was engineered from.
Who uses it? Lifters injecting IM directly into trained muscle within minutes of the last set. WADA tests for both forms.
Bottom line? Mechanism convincing. Human efficacy unknown.
What It Is
MGF — Mechano Growth Factor — is a splice variant of insulin-like growth factor 1 (IGF-1) produced locally in skeletal muscle in response to mechanical loading. When resistance training, stretching, or muscle damage occurs, the single IGF-1 gene is alternatively spliced to include an extra 49-base insert into exon 5 (rodent) or equivalent in human, generating the IGF-1Ec transcript. The resulting pre-pro-peptide is processed to yield mature IGF-1 plus a carboxy-terminal 24-amino-acid E-domain peptide — it is this E-peptide that has come to be called "Mechano Growth Factor" and is the molecular entity sold as MGF in research-peptide channels.
The distinction between IGF-1Ec (MGF-producing) and IGF-1Ea (the systemic liver-produced isoform responsible for most circulating IGF-1) was established by Geoffrey Goldspink, Shi-Yu Yang, and Michael Hill at the Royal Free Hospital, University College London in a series of landmark papers between 1997 and 2005. Using stretch-overloaded rabbit tibialis anterior and exercise-stimulated rodent muscle, they showed that mechanical loading produces a distinct burst of IGF-1Ec transcription, that the resulting E-peptide is biologically distinct from mature IGF-1, and that the E-peptide specifically activates satellite cells — the quiescent, basal-lamina-associated stem cells in muscle that donate their nuclei to damaged fibers during repair and hypertrophy (Yang and Goldspink, FEBS Lett 2002; Hill and Goldspink, J Physiol 2003).
Satellite cells are the rate-limiting input to skeletal muscle regeneration. Quiescent satellite cells sit beneath the basal lamina of each muscle fiber; upon mechanical damage or growth stimulus, they activate, proliferate as myoblasts, and either fuse with existing fibers (adding myonuclei) or fuse with each other (forming new fibers). The biological sequence that Goldspink's work implied — mechanical damage → MGF (E-peptide) release → satellite cell activation → mature IGF-1Ea release → protein synthesis in activated tissue — is the integrative model that positions MGF as the "initiating signal" and the mature IGF-1 as the "amplification signal." This two-phase model is the central reason MGF remains a compound of interest despite the paucity of human data.
Commercial synthetic MGF is the 24-amino-acid E-peptide fragment (not the full IGF-1Ec pre-pro-peptide), synthesized chemically and supplied as lyophilized powder. Its short plasma half-life (approximately 5–7 minutes) reflects the biological role as a local, transient mechanical signal — it was never evolutionarily selected to circulate systemically. To address the half-life limitation, PEG-MGF was developed: the synthetic E-peptide covalently coupled to a polyethylene glycol moiety, extending the circulating half-life to approximately 48–72 hours and permitting systemic subcutaneous administration.
MGF is not FDA-approved, has never been formally advanced into human clinical trials, and is classified as a banned substance by the World Anti-Doping Agency (WADA) under section S2 (peptide hormones, growth factors, related substances, and mimetics) and under section S0 (unapproved substances). The compound exists entirely in research-peptide channels for human use.
Mechanism of Action
MGF's mechanism is distinct from that of systemic IGF-1 despite sharing a gene locus. The E-peptide has low affinity for the classical IGF-1 receptor (IGF-1R) and acts primarily via an as-yet-incompletely-characterized distinct receptor pathway.
- Satellite cell activation (primary) — The central MGF effect. MGF acts on quiescent Pax7-positive satellite cells in the basal lamina, driving their exit from G0 into active proliferation as myoblasts. This is the initiating event of muscle regeneration. Without satellite cell activation, muscle hypertrophy hits a myonuclear-domain ceiling.
- Mechanistic independence from IGF-1R — MGF binds with low affinity to the classical IGF-1R. Its dominant effect is mediated by a separate receptor system (not yet fully characterized at the molecular level) that drives distinctive downstream signaling different from that of mature IGF-1.
- PI3K-Akt anti-apoptotic signaling — MGF activates PI3K / Akt in damaged muscle cells, upregulating anti-apoptotic effectors (Bcl-2, Bcl-xL) and protecting cells that have sustained mechanical damage from programmed cell death during the critical early repair window (Hill, Wernig, Goldspink 2003).
- Downstream IGF-1Ea coordination — MGF release precedes mature IGF-1Ea release in the damaged muscle timeline. IGF-1Ea then drives protein synthesis in the satellite-cell-expanded myoblast and the existing fiber. The two-phase temporal sequence is the basis for the "initiating vs amplifying" model.
- Neuroprotective expression — MGF is also expressed in brain tissue in response to injury. Dluzniewska et al. (FASEB J 2005) demonstrated a strong neuroprotective effect of the C-terminal E-peptide in transient forebrain ischemia in rats, reducing neuronal death and promoting neural stem cell proliferation in the subventricular zone.
- Cardiac injury response — MGF expression is upregulated in cardiac tissue after myocardial infarction; exogenous MGF administration in animal models reduced infarct size, preserved cardiac function, and activated cardiac progenitor cells (Carpenter et al., Heart Lung Circ 2008).
- Age-related decline — MGF transcriptional response to exercise is blunted in aged muscle. This age-related decline in MGF responsiveness correlates with reduced regenerative capacity in sarcopenic populations.
- Rapid local action — Native MGF's ~5–7 minute plasma half-life is a biological feature, not a pharmaceutical limitation — MGF is an acute, local, mechanically-coupled signal that was never designed for circulating systemic exposure.
- PEGylation extends action (PEG-MGF) — PEGylated MGF has a half-life of approximately 48–72 hours, converting the biology from a local pulse to a sustained systemic presence. Whether sustained systemic PEG-MGF faithfully reproduces the local pulse biology is biologically uncertain — the mechanism evolved for pulsatile local delivery.
- Tendon and bone — Emerging evidence indicates MGF plays a role in tendon healing and bone fracture repair, activating local progenitor cells in each tissue compartment under mechanical stress.
What the Research Shows
MGF research is dominated by mechanistic cell culture and animal models. No human randomized controlled trials have ever been published.
- Mechanistic foundation (Yang and Goldspink, FEBS Lett 2002; PMID 12095642) — "Different roles of the IGF-1 Ec peptide (MGF) and mature IGF-1 in myoblast proliferation and differentiation." Established that the E-peptide alone drives myoblast proliferation without differentiation, while mature IGF-1 drives differentiation — distinct temporal roles in muscle regeneration.
- Satellite cell activation (Hill and Goldspink, J Physiol 2003; PMID 12692182) — Expression and splicing of the IGF-I gene in rodent muscle is associated with muscle satellite cell activation following local tissue damage. Foundational demonstration that MGF is the molecular trigger of satellite cell entry into cell cycle.
- MGF review (Goldspink, Physiology 2005; PMID 16024512) — Comprehensive review: "Mechanical signals, IGF-I gene splicing, and muscle adaptation." Integrates the two-decade mechanistic literature from the Goldspink lab.
- Neuroprotection (Dluzniewska et al., FASEB J 2005; PMID 16195370) — Strong neuroprotective effect of the autonomous C-terminal peptide of IGF-1 Ec (MGF) in rat transient forebrain ischemia model. Reduced neuronal death and promoted neural stem cell proliferation.
- Cardiac infarction (Carpenter et al., Heart Lung Circ 2008; PMID 17881288) — Mechano-growth factor reduces loss of cardiac function in acute myocardial infarction. Demonstrated reduction in infarct size and preservation of left ventricular function in rat MI model.
- Exercise-induced MGF expression (Kim et al., J Appl Physiol 2005) — Resistance exercise increased MGF mRNA in human quadriceps; confirms the mechanistic model in humans for endogenous response but does not address exogenous administration.
- Age-related MGF response (Hameed et al., J Physiol 2003) — Blunted MGF response to training in elderly compared to young; mechanistic basis for sarcopenia-relevant interventions.
- Tendon and bone progenitor activation (multiple preclinical) — MGF upregulated in injured tendon and bone tissue; exogenous MGF accelerated progenitor recruitment in rat models.
- E-peptide receptor characterization (Pfeffer, Kaeser 2009) — Evidence for a distinct, non-IGF-1R receptor mediating E-peptide effects; full molecular identity remains unresolved.
- Myoblast proliferation (Mills et al., Am J Physiol Cell Physiol 2007) — Further mechanistic work on differential signaling of MGF and IGF-1 in muscle progenitor populations.
Research Limitations
No published human randomized controlled trials exist for synthetic MGF or PEG-MGF. All efficacy data comes from cell culture and animal studies. The synthetic 24-aa E-peptide used commercially may not fully replicate the biological activity of endogenously produced full-length IGF-1Ec pre-pro-peptide, which is co-secreted with mature IGF-1 and processed locally in a distinct temporal and spatial pattern. Dosing in humans is extrapolated from allometric scaling of animal models and community experience. WADA-banned. Not a validated clinical therapy in any indication.
Human Data
Human MGF data is limited to observational studies of endogenous MGF expression following exercise or injury; no interventional trials of exogenous MGF or PEG-MGF have been published.
- Exercise-induced endogenous MGF expression — Human quadriceps biopsy studies after resistance training consistently show transient IGF-1Ec mRNA upregulation within hours of mechanical loading (multiple groups: Kim, Hameed, Greig).
- Age-related blunting — Elderly subjects show markedly reduced MGF transcriptional response to training compared to young; parallels the reduced regenerative capacity of aged muscle.
- Cardiac MGF following MI — Human myocardial samples post-infarction show increased IGF-1Ec expression in the infarct border zone, paralleling the rodent model.
- Rehabilitation-associated expression — Physical-therapy and post-surgical rehabilitation studies show measurable IGF-1Ec induction during recovery phases; associative, not interventional.
- No Phase 1 / 2 / 3 RCT — No pharmaceutical-industry or academic-consortium-funded human trial of exogenous MGF or PEG-MGF administration has been published. Community use is entirely extrapolation.
- Community-practice case reports — Anecdotal reports of improved injury recovery and hypertrophy on MGF + training protocols; no standardized outcome measures, no control.
- WADA detection — WADA and anti-doping science groups have published method development for MGF and PEG-MGF urinary / plasma detection; these are the most rigorous "human exposure" datasets available, though they are forensic rather than clinical.
The evidence gap between preclinical mechanism and human clinical validation is one of the largest in the peptide space. MGF sits squarely in the "mechanism is real; clinical translation is unvalidated" category.
Dosing from the Literature
Doses below are drawn from preclinical animal protocols and aggregated community practice. No approved human dose exists.
| Protocol | Dose | Route / Frequency | Notes |
|---|
| Standard MGF (community) | 100–200 mcg per injection site | IM immediately post-workout | Injected bilaterally into trained muscle group. Used within minutes of reconstitution due to short half-life. |
| PEG-MGF (community) | 200 mcg | SubQ 2–3× per week | PEGylation extends half-life; permits systemic administration. Typical cycle 4–6 weeks. |
| Injury-recovery protocol | 200 mcg (standard) or 200 mcg PEG | Daily IM (standard) or 3× weekly SubQ (PEG) | Pairs with BPC-157 / TB-500 in community protocols. |
| Cardiac / neuroprotective research | Allometric scaling from rodent | IV / IM, research only | Not a community protocol; mentioned for mechanistic context. |
| Cycle length | 4–6 weeks | Followed by equivalent off | No tachyphylaxis documented but conservative cycling reduces theoretical cancer-promotion concerns. |
Dosing Disclaimer
MGF and PEG-MGF are not FDA-approved, have never been advanced into human clinical trials, and are WADA-banned. Community dosing is entirely derivative of preclinical protocols and aggregated practitioner experience, without validation. Standard (non-PEG) MGF must be injected immediately post-reconstitution and immediately post-training due to its ~5–7 minute half-life; any meaningful delay eliminates efficacy. PEG-MGF converts the local-pulse biology to sustained systemic exposure, which may or may not reproduce the intended mechanism.
Reconstitution & Storage
MGF is supplied as lyophilized powder in 2 mg (standard) or 2 mg / 5 mg (PEG-MGF) vials.
| Vial Size | BAC Water | Concentration | 100 mcg Dose | 200 mcg Dose |
|---|
| MGF 2 mg | 2 mL | 1 mg/mL | 10 units (0.10 mL) | 20 units (0.20 mL) |
| MGF 2 mg | 1 mL | 2 mg/mL | 5 units (0.05 mL) | 10 units (0.10 mL) |
| PEG-MGF 2 mg | 2 mL | 1 mg/mL | 10 units (0.10 mL) | 20 units (0.20 mL) |
| PEG-MGF 5 mg | 2 mL | 2.5 mg/mL | 4 units (0.04 mL) | 8 units (0.08 mL) |
- Reconstitution — Inject BAC water slowly down vial wall at 45°; swirl gently. Standard MGF is particularly oxidation-sensitive.
- Standard MGF storage (unreconstituted) — 2–8°C long-term; some suppliers recommend −20°C for vials held beyond 30 days. Do not freeze once reconstituted.
- Standard MGF storage (reconstituted) — Use within 24–72 hours. Unique among peptides in its fragility: community practice is to reconstitute only what will be used same-day.
- PEG-MGF storage (reconstituted) — 2–8°C; use within 21–28 days (PEGylation stabilizes the peptide substantially).
- Injection technique — Standard MGF: IM into trained muscle group immediately post-workout; 25–27G 1-inch needle. PEG-MGF: SubQ abdomen or thigh; 29–31G insulin syringe.
- Timing — Standard MGF must be injected within minutes of training. PEG-MGF timing is less critical; typical 2–3×/week on training days.
- Inspection — Clear colorless solution; discard if cloudy or discolored.
→ Use the Kalios Peptide Calculator for exact syringe units
Side Effects & Risks
Important
MGF has never been in a human RCT and carries IGF-1-axis cancer-promotion theory with no long-term safety data. PEGylation may shift the biology from a local pulse into sustained systemic exposure. Ask your provider about IGF-1 and cancer screening before using either form.
MGF's side-effect profile is derived primarily from community experience and theoretical consideration of the mechanism — no formal human safety data exist.
- Injection site soreness (IM) — Intramuscular injection into freshly trained muscle causes additional localized soreness. Usually mild and resolves within 24–48 hours.
- Transient hypoglycemia — Rare. As an IGF-1 family peptide, there is theoretical potential for glucose-lowering effects, though systemic impact of local IM dosing is minimal.
- Theoretical cancer-promotion risk — MGF activates progenitor/stem cells, has anti-apoptotic effects, and engages PI3K-Akt signaling. All three are mechanistically relevant to tumor biology. Active malignancy is a contraindication; personal or family history of hormone-sensitive cancer warrants significant caution.
- Anti-PEG antibody formation (PEG-MGF specific) — PEGylated compounds can trigger anti-PEG antibodies with repeated use, reducing efficacy over time. Prevalence is low but documented.
- Localized muscle asymmetry — If MGF is injected unilaterally or unevenly, the enhanced local satellite-cell activation can produce asymmetric muscle development over time.
- Unknown long-term effects — No chronic human safety data exist. Long-term manipulation of satellite-cell activation and anti-apoptotic signaling has unknown downstream consequences.
- Product purity variability — Research-peptide MGF varies substantially in purity and actual peptide content. Third-party HPLC and mass spec Certificates-of-Analysis are the practical floor.
- PEGylation-related injection site reactions — Local erythema and induration more common with PEG-MGF than with standard MGF.
- WADA banned — Explicitly prohibited under S2 (growth factors) and S0 (unapproved substances) in and out of competition. Modern anti-doping laboratories have validated detection methods for both MGF and PEG-MGF.
- Pregnancy and lactation — Not studied; avoid.
- Drug interactions — Theoretical additive effects with exogenous IGF-1, GH, insulin, and other growth-factor-axis compounds. Stacking growth-factor-axis compounds amplifies the IGF-1 / insulin-resistance / growth-promotion signal with correspondingly amplified theoretical risk.
- Allergic reactions — Rare; as a synthetic peptide not naturally present in circulating form, sensitization is biologically plausible.
Supportive Nutrition & Training
MGF's biology is tightly coupled to mechanical loading and nutritional substrate availability. Without structured training and adequate protein, the satellite-cell activation signal has nothing to build on.
- Resistance training (primary) — MGF is, mechanistically, a mechanotransduction-coupled peptide. Endogenous IGF-1Ec is only produced in response to mechanical loading; exogenous MGF without a matching training stimulus is pharmacology without substrate. 3–5 structured resistance sessions per week is the practical floor.
- Protein (1.8–2.4 g/kg/day) — Amino acid substrate for the hypertrophic response MGF is initiating. Leucine-rich protein sources (whey, eggs, lean red meat) provide the mTORC1-activating substrate.
- Caloric surplus (200–400 kcal/day) — Satellite-cell activation-driven hypertrophy is metabolically expensive. Caloric deficit blunts the anabolic response MGF is designed to amplify.
- Creatine monohydrate (3–5 g/day) — Standard hypertrophy adjunct; independent mechanism (phosphocreatine buffering) that pairs with MGF's satellite-cell effect.
- Omega-3 (2–3 g EPA/DHA) — Supports inflammation resolution during high-training-load phases; beta-oxidation substrate for mitochondrial capacity in growing tissue.
- Vitamin D (2,000–5,000 IU to 40–60 ng/mL) — Muscle-quality support; vitamin D receptor is expressed on satellite cells, and D sufficiency is permissive for satellite-cell activation and differentiation.
- Collagen peptides or gelatin (15–20 g pre-training) — Pairs with MGF's connective-tissue repair potential for tendon and fascia support around the trained muscle group.
- Sleep (7–9 hours) — Endogenous GH pulses during slow-wave sleep drive the systemic IGF-1Ea that amplifies MGF's local satellite-cell signal. Sleep restriction flattens the endogenous growth-factor pulse that MGF is meant to augment.
- Things to avoid — Combining MGF with chronic supraphysiologic IGF-1 or GH (amplifies theoretical cancer-promotion concerns); training at fatigue without adequate recovery (neither MGF nor any signal can overcome net-catabolic overtraining); using MGF in a significant caloric deficit (pharmacology without substrate).
Bloodwork & Monitoring
- IGF-1 (serum, baseline and at 4, 8 weeks) — Standard MGF at local IM doses should not significantly alter serum IGF-1. PEG-MGF at systemic SubQ doses may modestly elevate IGF-1.
- Fasting glucose and insulin — Baseline and periodic; monitor for hypoglycemia especially if stacking with other IGF-1-axis compounds.
- Creatine kinase (CK) — Useful for tracking muscle damage and recovery patterns if using MGF for injury rehabilitation.
- Comprehensive metabolic panel — Baseline. Monitor liver and kidney function with any extended protocol.
- CBC — Baseline screen.
- Age-appropriate cancer screening — Given theoretical cancer-promotion concerns, standard age-indicated colorectal, breast, and prostate screening is a rational precaution before initiating extended MGF courses.
- Personal and family cancer history — Any strong hormone-sensitive cancer family history (breast, ovarian, prostate, colorectal) should move MGF to contraindicated.
- DEXA or BIA for body composition — Baseline and 8–12 weeks; objective measure of lean mass change independent of water retention or scale-weight artifact.
Commonly Stacked With
The biologically logical stack: MGF first (post-workout, IM local) to activate satellite cells, then IGF-1 DES (few hours later or next day) to drive protein synthesis in the newly activated cells. This mimics the natural MGF → IGF-1Ea sequence in muscle tissue after training. Protocol: MGF 100–200 mcg immediately post-workout IM, followed by IGF-1 DES 20–50 mcg into same muscle the following day.
PEG-MGF combined with IGF-1 LR3 for comprehensive IGF-1 pathway coverage. PEG-MGF handles satellite cell recruitment; LR3 provides sustained systemic anabolic support. Aggressive stack with compounded risk profile — monitor glucose, IGF-1, blood pressure.
For muscle or tendon injuries, MGF can be added to BPC + TB protocols to specifically boost the stem-cell activation component of healing. MGF activates progenitor cells while BPC-157 and TB-500 support angiogenesis and tissue remodeling via distinct (VEGFR2, actin-sequestering) mechanisms.
GH-axis support alongside MGF's local satellite-cell activation. Elevates systemic IGF-1Ea via endogenous GH pulses, complementing MGF's local initiation of regeneration. Stacks stack amplifiable growth-factor-axis risk — cancer and insulin monitoring apply.
Structured resistance training
MGF's biology is mechanically coupled to training. MGF without training produces far smaller effects — there is no endogenous damage signal to synergize with. Structured progressive resistance training is the substrate for MGF to work on.
→ Check compound compatibility in the Stack Builder
Regulatory Status
Current Status — April 2026
MGF (Mechano Growth Factor) and PEG-MGF are not FDA-approved for any human indication. Neither has been advanced into a formal human clinical trial by a pharmaceutical sponsor. Both are classified as research chemicals for laboratory investigation only.
MGF and PEG-MGF are banned by the World Anti-Doping Agency (WADA) under section S2 (Peptide Hormones, Growth Factors, Related Substances and Mimetics) of the Prohibited List, in and out of competition. They are additionally captured by S0 (non-approved substances). Modern anti-doping laboratories have validated detection methods for both forms.
MGF is not on the FDA Category 2 Bulk Drug Substances list. It is not part of HHS Secretary Kennedy's February 2026 Category 2 peptide reclassification announcement. It is not eligible for compounding through 503A or 503B pharmacies under any current FDA pathway.
Community supply is entirely through research-peptide vendors. Standard MGF's extreme oxidation sensitivity and short working half-life mean product-quality failures are common; independent third-party Certificate-of-Analysis verification is the practical minimum.
Cost & Access
MGF and PEG-MGF are not approved for human use. They are available through research-peptide suppliers for laboratory research purposes only. U.S. compounding pharmacies cannot legally compound either form under current FDA bulk-substance rules.
Research-peptide vendors typically supply MGF as 2 mg lyophilized vials and PEG-MGF as 2 mg or 5 mg lyophilized vials. Purity and potency vary substantially between vendors; independent HPLC + mass spec COAs are the practical verification floor. Standard MGF is among the most fragile research peptides, with documented oxidation-related potency loss during shipping and storage; PEG-MGF is more stable but introduces anti-PEG antibody concerns with repeated use.
MGF and PEG-MGF are not among the peptides addressed by HHS Secretary Kennedy's February 2026 Category 2 reclassification announcement. They have never been Category 2 substances because they have never been seriously advanced as legitimate compounding candidates. Regulatory status is unlikely to change — no sponsor is actively pursuing FDA approval for either form, and the growth-factor-axis mechanism makes formal clinical development unattractive from a safety-signal standpoint.
Estimated pricing and access as of April 2026. Actual costs vary by provider, location, and prescription status. Kalios does not sell compounds.
Related Compounds
Related paths people compare with MGF:
PEGylated mechano growth factor. Extended-half-life MGF analogue for systemic dosing.
Activin/myostatin-binding protein. Neutralizes myostatin to permit muscle hypertrophy.
Recombinant human growth hormone (somatropin). 191-amino-acid protein used for GH deficiency and off-label performance.
Key References
- 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(1-3):156-160. PMID: 12095642. DOI: 10.1016/s0014-5793(02)02918-6.
- 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(Pt 2):409-418. PMID: 12692182. DOI: 10.1113/jphysiol.2002.035832.
- Goldspink G. Mechanical signals, IGF-I gene splicing, and muscle adaptation. Physiology (Bethesda). 2005;20:232-238. PMID: 16024512. DOI: 10.1152/physiol.00004.2005.
- Dluzniewska J, Sarnowska A, Beresewicz M, Johnson I, Srai SK, Ramesh B, Goldspink G, Górecki DC, Zabłocka B. A strong neuroprotective effect of the autonomous C-terminal peptide of IGF-1 Ec (MGF) in brain ischemia. FASEB J. 2005;19(13):1896-1898. PMID: 16195370. DOI: 10.1096/fj.05-3786fje.
- Carpenter V, Matthews K, Devlin G, Stuart S, Jensen J, Conaglen J, Jeanplong F, Goldspink P, Yang SY, Goldspink G, Bass J, McMahon C. Mechano-growth factor reduces loss of cardiac function in acute myocardial infarction. Heart Lung Circ. 2008;17(1):33-39. PMID: 17881288. DOI: 10.1016/j.hlc.2007.04.013.
- Hameed M, Orrell RW, Cobbold M, Goldspink G, Harridge SD. Expression of IGF-I splice variants in young and old human skeletal muscle after high resistance exercise. J Physiol. 2003;547(Pt 1):247-254. PMID: 12562960.
- Hill M, Wernig A, Goldspink G. Muscle satellite (stem) cell activation during local tissue injury and repair. J Anat. 2003;203(1):89-99. PMID: 12892408.
- Mills P, Dominique JC, Lafrenière JF, Bouchentouf M, Tremblay JP. A synthetic mechano growth factor E peptide enhances myogenic precursor cell transplantation success. Am J Transplant. 2007;7(10):2247-2259. PMID: 17711551.
- Kim JS, Cross JM, Bamman MM. Impact of resistance loading on myostatin expression and cell cycle regulation in young and older men and women. Am J Physiol Endocrinol Metab. 2005;288(6):E1110-E1119. PMID: 15644458. (Human muscle MGF expression in training response.)
- 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(3):865-875. PMID: 20130113.
- Pfeffer LA, Brisson BK, Lei H, Barton ER. The insulin-like growth factor (IGF)-I E-peptides modulate cell entry of the mature IGF-I protein. Mol Biol Cell. 2009;20(17):3810-3817. PMID: 19605555.
- Brisson BK, Barton ER. New modulators for IGF-I activity within IGF-I processing products. Front Endocrinol (Lausanne). 2013;4:42. PMID: 23626586.
- Stavropoulou A, Halapas A, Sourla A, Philippou A, Papageorgiou E, Papalois A, Koutsilieris M. IGF-1 expression in infarcted myocardium and MGF E peptide actions in rat cardiomyocytes in vitro. Mol Med. 2009;15(5-6):127-135. PMID: 19242589.
- WADA. World Anti-Doping Code: The 2025 Prohibited List. Section S2 — Peptide hormones, growth factors, related substances and mimetics. World Anti-Doping Agency.
- Thomas A, Höppner S, Geyer H, Schänzer W, Petrou M, Kwiatkowska D, Pokrywka A, Thevis M. Determination of growth hormone-releasing peptides and peptide hormones in doping control samples by liquid chromatography/(tandem) mass spectrometry. Anal Bioanal Chem. 2011;401(2):507-516.
- Philippou A, Maridaki M, Halapas A, Koutsilieris M. The role of the insulin-like growth factor 1 (IGF-1) in skeletal muscle physiology. In Vivo. 2007;21(1):45-54. PMID: 17354613.
- Philippou A, Halapas A, Maridaki M, Koutsilieris M. Type I insulin-like growth factor receptor signaling in skeletal muscle regeneration and hypertrophy. J Musculoskelet Neuronal Interact. 2007;7(3):208-218. PMID: 17906394.
Last updated: April 2026 | Profile authored by Kalios Peptides research team