tl;dr MGF IGF-1EC is an exciting peptide with proven use for traumatic injury repair, nerve regrowth, and muscle development. There are 2 forms available and is tested as an injectable peptide. MGF has a promising future for injury recovery and anti-aging.

Names: mechano-growth factor (MGF), MGF IGF-1EC, PEG-MGF, PMGF

IGF-1EC structure


Mechano Growth Factor (MGF) is also known as IGF-1EC. I will use both of these names in this article.

Regardless of what it’s called, MGF is actively being researched. It has a long history thanks to the work of Geoff Goldspink (More on him later). It is specifically researched as an intramuscular injectable peptide.1

A different version of IGF-1 that appears to be more potent

As it’s name implies it is a variant of the Insulin-like growth factor 1 (IGF-1), hormone. The changes to the structure make it a “splice variant.”2 Without getting into the biology too much, this means part of the protein structure can vary based on local gene expression.34

In scientific studies this peptide is often referenced as having a changed “E domain.”567 The book Advances in Genetics, Volume 52 and Insulin-like Growth Factors: Molecular and Cellular Aspects by Derek LeRoith has more information than you would ever care to learn about how changes in the IGF-1 E domain effects genes and protein. If you read it get comfy - these are massive books.

Muscle Growth and Repair



MGF is highly anabolic

The most well known property of MGF is the body’s natural anabolic uses in building and repairing muscle.

It is necessary for muscle growth to occur.8 It is found to activate the muscle stem cells that start local muscle repair. This also causes muscle hypertrophy.9

Your body creates MGF after a workout1011 or any muscle stress.12 The local IGF-1 genes create the MGF variant which helps the localized muscle repair and regrow. Exercise also increases local MGF which in turn reduces some catabolic gene expression.13

It also causes smooth muscle hypertrophy.14 This means it could be useful in many digestive disorders.

There are staggering implications of MGF for anti-aging and helping people suffering from muscle wasting caused by any number of diseases. MGF is used in preventing skeletal muscles decline, and keeping muscles strong as you age.15 Because MGF helps promote proliferation of myogenic stem cells it can be used to prevent and treat age-related muscle degenerative diseases.16

Other Benefits



MGF helps soft tissue repair

IGF-1EC does not help just muscles. Even soft tissue such as tendons are also strengthened by exercise induced MGF.17 It is also implicated in bone growth.18 One study in rabbits suggest it can help heal bone defects faster.19 When used along with TGF-β3 (another growth factor hormone), it helped cartilage regeneration.20 It might also be used to help endometriosis.21

When tested in sheep, MGF helped them survive and function after heart attacks.22 These effects should work on humans as well. Research finds it “may be used to prevent adverse remodeling of the heart and improve function following myocardial infarction”23 and that it can preserve heart functions.24

MGF also helps nerve damage

IGF-1 is found in recent studies to be effective in nerve regeneration.2526 This implies IGF-1EC would have similar effects. And in fact, IGF-1EC is found to be more effective than plain IGF-1 at protecting nerves from damage 27 and specifically plays a role in nerve regrowth after injury.28

Neuroprotectant for TBI



IGF-1EC appears to act as a potent neuroprotectant as well. It is found to be helpful in stroke victims.29 Similar to effects in motoneurons, there is also some evidence that MGF’s neuroprotectant features are more potent than that of plain IGF-1.30 It easily passes the blood brain barrier31 and offers “very significant protection” to neurons.32

There are no studies testing IGF-1EC specifically in TBI. In a rat model normal IGF-1 is shown to prevent TBI-induced brain damage33 and that the body use IGF-1 as a natural neuroprotectant in response to brain damage.34 Give the other similarities it is likely that MGF would offer the same or greater benefits for TBI recovery.

Alzheimer’s Disease


There are no studies with IGF-1EC specifically. But, the role of normal IGF-1 in Alzheimer’s is under research.35 There is no conclusive relationship with plain IGF-1, but the little of what is published appears promising.3637 The closest link is that patients with low IGF-1 levels show a faster cognitive decline. Given the neuroprotectant effects of IGF-1 this makes sense.



There are no studies with IGF-1EC specifically. The closest findings is that one study in PTSD veterans found that as their sleep improved, so did their levels of IGF-1.38

Cancer Link


Mixed Effect:

Conflicting research

IGF-1 use is controversial because of cancer links. Since MGF is a variant of regular IGF-1, it triggers many of the same responses in the body.39 This is because it activates the IGF-I receptor.40

There is debate about IGF-1EC’s link to cancer. One study finds that while MGF greatly enhances muscle stem cell activation and muscle maintenance, it does this without the cancer causing side effects of IGF-1.41

Unfortunately, there is data that says the opposite also.

MGF is found to be overexpressed in malignant bone cancer42 and prostate cancer.43 It’s presence also seems to be associated with more advanced stages of prostate cancer.44 Finding the links between IGF and cancer is a current area of active research. I think you will see studies supporting both sides until something revolutionary is found in IGF-1’s role in cancer.

PEG-MGF Variant

MGF version with a longer half-life

PEG-MGF is a form of MGF that has Polyethylene glycol added. The technical term for any chemical with this addition is that it has been PEGylated. The PEG-MGF form is more stable and will have a much longer half-life because PEG extends circulating life, increases molecular stability, and often makes it more soluble.45

Unfortunately, as usual, there is a big gap between what people are doing vs. what medicine is studying.

PEG-MGF is found in the bodybuilding world, whereas the straight form of MGF is found in scientific studies. I am unable to find medical research done with the PEGylated MGF version.

PEG-IGF1 has been found to be more effective at muscle repair46 compared to IGF-1 so it seems safe to assume PEG-MGF would too. The only clinical speculation I could find on PEG-MGF is that it is thought to have similar effects on IGF-1 and insulin receptors.47


Used postworkout to match the small window of bio-availability

Natural IGF-1EC is made by cells for local use.48 This means it has a very short half life because it normally never leaves the cell.49 The conditions that make a cell sensitive to IGF-1EC don’t last forever, so there’s no need for it to have evolved to last for hours.

This is why the majority of people reporting IGF-1EC use inject it postworkout into the muscles trained. Common doses are 50, 100, or 200mcgs after each training session.

Used in larger doses for injury recovery

Medical studies are starting to explore sports injury repairs using IFG-1EC50, but their research is lagging behind years of people already using it. For acute muscle recovery from injuries people report using IFG-1EC at higher doses usually once a day. For example, Jason Blaha talks about using 600mcg of MGF to quickly heal a pulled hamstring:

PEG-MGF vs. MGF doses

Lacking any side by side studies of human muscle repair comparing PEG-MGF vs MGF, the only people talking about the difference are bodybuilders. From what is reported PEG-MGF seems to be preferred for muscle growth. But for injury recovery either will do.

In theory PEG-MGF could be dosed outside of workout times (since it should stay available longer) with users injecting every other day. Unfortunately, I’m not finding any studies showing the exact half-life of PEG-MGF besides estimates.


As mentioned above, Geoff Goldspink at the University of London has been researching MGF for longer than I’ve been alive. He has done the bulk of the work on describing MGF and exploring it’s effects in humans.

Based on his history Dr. Goldspink is going to be involved with the most viable patents for MGF/IGF-1EC.

He holds many interesting patents for the use of MGF including: using MGF to prevent heart damage after a heart attack, helping neurological disorder with MGF’s nerve protection, and specifically repairing nerve damage. His team was able to regrow 3mm of nerves in 2 weeks with MGF therapy.


Pubchem doesn’t seem to have an entry for IGF-1EC. Sigma-Aldrich does not seem to sell it either so high-end pricing is unknown.

Peptide site pricing:

  • MGF: $14-38 for 2mg
  • PEG-MGF: $28-58 for 2mg


This is a good time to point out my standard disclaimer: I am not a doctor or a lawyer. I made this site to help in my own research of the human endocrine system, and to find any new treatments for PTSD and Traumatic Brain Injury. I’m not making any medical or legal claims about any drug here besides what medical studies are showing and what people are self-reporting they use.

Each country and state is free to make their own scheduling on substances so it’s up to you to check. At the time of writing MGF/IGF-1EC didn’t appear on the DEA list.

WADA specifically bans MGF by name since 2005, and the IGF-1 class as a whole. They prohibit at all times:

  • Insulin-like Growth Factor-1 (IGF-1), and its analogues
  • Mechano Growth Factors (MGFs)

The NCAA bans as a class “Peptide Hormones and Analogues” naming “Growth hormone (hGH); human chorionic gonadotropin (hCG); erythropoietin (EPO); IGF-1; etc.” MGF being a form of IGF-1 would fall under this ban.

Doping controls for MGF exist including detection of fragment and full-length.51


  1. Chen, Hailong, Ke Lv, Zhongquan Dai, Guohua Ji, Tingmei Wang, Yanli Wang, Yongliang Zhang, Guanghan Kan, Yinghui Li, and Lina Qu. 2016. “Intramuscular Injection of Mechano Growth Factor E Domain Peptide Regulated Expression of Memory-Related Sod, miR-134 and miR-125b-3p in Rat Hippocampus Under Simulated Weightlessness.” Biotechnology Letters 38 (12) (September 13): 2071–2080. doi:10.1007/s10529-016-2210-4.
  2. Schlegel, Werner, Adalbert Raimann, Daniel Halbauer, Daniela Scharmer, Susanne Sagmeister, Barbara Wessner, Magdalena Helmreich, Gabriele Haeusler, and Monika Egerbacher. 2013. “Insulin-Like Growth Factor I (IGF-1) Ec/Mechano Growth Factor €“ A Splice Variant of IGF-1 Within the Growth Plate.” Edited by Francisco J. Esteban. PLoS ONE 8 (10) (October 11): e76133. doi:10.1371/journal.pone.0076133.
  3. Hill, Maria, and Geoffrey Goldspink. 2003. “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.” The Journal of Physiology 549 (2) (June): 409–418. Portico. doi:10.1113/jphysiol.2002.035832.
  4. Goldspink, Geoffrey. 2003. Journal of Muscle Research and Cell Motility 24 (2/3): 121–126. doi:10.1023/a:1026041228041.
  5. Liu, Meili, Xufeng Niu, Gang Zhou, Zhengtai Jia, Ping Li, and Yubo Fan. 2016. “Potential Effect of Mechano Growth Factor E-Domain Peptide on Axonal Guidance Growth in Primary Cultured Cortical Neurons of Rats.” Journal of Tissue Engineering and Regenerative Medicine. Portico. doi:10.1002/term.2364.
  6. Peña, James R., James R. Pinney, Perla Ayala, Tejal A. Desai, and Paul H. Goldspink. 2015. “Localized Delivery of Mechano-Growth Factor E-Domain Peptide via Polymeric Microstructures Improves Cardiac Function Following Myocardial Infarction.” Biomaterials 46 (April): 26–34. doi:10.1016/j.biomaterials.2014.12.050.
  7. KM, Shioura. 2013. “Administration of a Synthetic Peptide Derived from the E-Domain Region of Mechano-Growth Factor Delays Decompensation Following Myocardial Infarction.” International Journal of Cardiovascular Research 03 (03). doi:10.4172/2324-8602.1000169.
  8. Yang, Shi Yu, and Geoffrey Goldspink. 2002. “Different Roles of the IGF-I Ec Peptide (MGF) and Mature IGF-I in Myoblast Proliferation and Differentiation.” FEBS Letters 522 (1-3) (June 9): 156–160. Portico. doi:10.1016/s0014-5793(02)02918-6.
  9. Goldspink, Geoffrey. 2012. “Age-Related Loss of Muscle Mass and Strength.” Journal of Aging Research 2012: 1–11. doi:10.1155/2012/158279.
  10. Wackerhage, Henning, and Aivaras Ratkevicius. 2008. “Signal Transduction Pathways That Regulate Muscle Growth.” Essays In Biochemistry 44 (February): 99–108. doi:10.1042/bse0440099.
  11. Ahtiainen, Juha P, Maarit Lehti, Juha J Hulmi, William J Kraemer, Markku Alen, Kai Nyman, Harri Selänne, et al. 2011. “Recovery after Heavy Resistance Exercise and Skeletal Muscle Androgen Receptor and Insulin-Like Growth Factor-I Isoform Expression in Strength Trained Men.” Journal of Strength and Conditioning Research 25 (3) (March): 767–777. doi:10.1519/jsc.0b013e318202e449.
  12. McKoy, Godfrina, William Ashley, James Mander, Shi Yu Yang, Norman Williams, Brenda Russell, and Geoffrey Goldspink. 1999. “Expression of Insulin Growth Factor-1 Splice Variants and Structural Genes in Rabbit Skeletal Muscle Induced by Stretch and Stimulation.” The Journal of Physiology 516 (2) (April): 583–592. Portico. doi:10.1111/j.1469-7793.1999.0583v.x.
  13. Dieli-Conwright, Christina M., Jacqueline L. Kiwata, Creighton T. Tuzon, Tanya M. Spektor, Fred R. Sattler, Judd C. Rice, and Edward Todd Schroeder. 2016. “Acute Response of PGC-1α and IGF-1 Isoforms to Maximal Eccentric Exercise in Skeletal Muscle of Postmenopausal Women.” Journal of Strength and Conditioning Research 30 (4) (April): 1161–1170. doi:10.1519/jsc.0000000000001171.
  14. Li, Chao, Kent Vu, Krystina Hazelgrove, and John F. Kuemmerle. 2015. “Increased IGF-IEc Expression and Mechano-Growth Factor Production in Intestinal Muscle of Fibrostenotic Crohn’s Disease and Smooth Muscle Hypertrophy.” American Journal of Physiology - Gastrointestinal and Liver Physiology (October 1): ajpgi.00414.2014. doi:10.1152/ajpgi.00414.2014.
  15. Janssen, Joseph A.M.J.L. 2016. “Impact of Physical Exercise on Endocrine Aging.” Sports Endocrinology: 68–81. doi:10.1159/000445158.
  16. Qin, Li-Li, Xiao-Kui Li, Jian Xu, De-Lin Mo, Xiong Tong, Zhi-Cheng Pan, Jia-Qi Li, et al. 2012. “Mechano Growth Factor (MGF) Promotes Proliferation and Inhibits Differentiation of Porcine Satellite Cells (PSCs) by down-Regulation of Key Myogenic Transcriptional Factors.” Molecular and Cellular Biochemistry 370 (1-2) (August 9): 221–230. doi:10.1007/s11010-012-1413-9.
  17. Heinemeier, K. M., J. L. Olesen, P. Schjerling, F. Haddad, H. Langberg, K. M. Baldwin, and M. Kjaer. 2006. “Short-Term Strength Training and the Expression of Myostatin and IGF-I Isoforms in Rat Muscle and Tendon: Differential Effects of Specific Contraction Types.” Journal of Applied Physiology 102 (2) (October 26): 573–581. doi:10.1152/japplphysiol.00866.2006.
  18. Xin, Juan, Yuanliang Wang, Zhen Wang, and Fuchun Lin. 2013. “Functional and Transcriptomic Analysis of the Regulation of Osteoblasts by Mechano-Growth Factor E Peptide.” Biotechnology and Applied Biochemistry 61 (2) (December 20): 193–201. doi:10.1002/bab.1152.
  19. Deng, Moyuan, Bingbing Zhang, Ke Wang, Feng Liu, Hualiang Xiao, Jianhua Zhao, Peng Liu, Yuxiao Li, Fuchun Lin, and Yuanliang Wang. 2010. “Mechano Growth Factor E Peptide Promotes Osteoblasts Proliferation and Bone-Defect Healing in Rabbits.” International Orthopaedics 35 (7) (November 6): 1099–1106. doi:10.1007/s00264-010-1141-2.
  20. Luo, Ziwei, Li Jiang, Yan Xu, Haibin Li, Wei Xu, Shuangchi Wu, Yuanliang Wang, Zhenyu Tang, Yonggang Lv, and Li Yang. 2015. “Mechano Growth Factor (MGF) and Transforming Growth Factor (TGF)-Β3 Functionalized Silk Scaffolds Enhance Articular Hyaline Cartilage Regeneration in Rabbit Model.” Biomaterials 52 (June): 463–475. doi:10.1016/j.biomaterials.2015.01.001.
  21. MILINGOS, D., H. KATOPODIS, S. MILINGOS, A. PROTOPAPAS, G. CREATSAS, S. MICHALAS, A. ANTSAKLIS, and M. KOUTSILIERIS. 2006. “Insulin-Like Growth Factor-1 Isoform mRNA Expression in Women with Endometriosis: Eutopic Endometrium Versus Endometriotic Cyst.” Annals of the New York Academy of Sciences 1092 (1) (December 1): 434–439. doi:10.1196/annals.1365.042.
  22. Carpenter, Violaine, Kenneth Matthews, Gerard Devlin, Selwyn Stuart, Juliet Jensen, John Conaglen, Ferenc Jeanplong, et al. 2008. “Mechano-Growth Factor Reduces Loss of Cardiac Function in Acute Myocardial Infarction.” Heart, Lung and Circulation 17 (1) (February): 33–39. doi:10.1016/j.hlc.2007.04.013.
  23. Peña, James R., James R. Pinney, Perla Ayala, Tejal A. Desai, and Paul H. Goldspink. 2015. “Localized Delivery of Mechano-Growth Factor E-Domain Peptide via Polymeric Microstructures Improves Cardiac Function Following Myocardial Infarction.” Biomaterials 46 (April): 26–34. doi:10.1016/j.biomaterials.2014.12.050.
  24. Mavrommatis, Evangelos, Krystyna M. Shioura, Tamara Los, and Paul H. Goldspink. 2013. “The E-Domain Region of Mechano-Growth Factor Inhibits Cellular Apoptosis and Preserves Cardiac Function During Myocardial Infarction.” Molecular and Cellular Biochemistry 381 (1-2) (May 28): 69–83. doi:10.1007/s11010-013-1689-4.
  25. Bayrak, Asuman Feda, Yuksel Olgun, Ayla Ozbakan, Safiye Aktas, Can Ahmet Kulan, Gonca Kamaci, Emine Demir, Osman Yilmaz, and Levent Olgun. 2017. “The Effect of Insulin Like Growth Factor-1 on Recovery of Facial Nerve Crush Injury.” Clinical and Experimental Otorhinolaryngology (March 8). doi:10.21053/ceo.2016.00997.
  26. Tuffaha, Sami H., Prateush Singh, Joshua D. Budihardjo, Kenneth R. Means, James P. Higgins, Jaimie T. Shores, Roberto Salvatori, Ahmet Höke, W.P. Andrew Lee, and Gerald Brandacher. 2016. “Therapeutic Augmentation of the Growth Hormone Axis to Improve Outcomes Following Peripheral Nerve Injury.” Expert Opinion on Therapeutic Targets 20 (10) (May 24): 1259–1265. doi:10.1080/14728222.2016.1188079.
  27. Aperghis, Michael, Ian P. Johnson, John Cannon, Shi-Yu Yang, and Geoffrey Goldspink. 2004. “Different Levels of Neuroprotection by Two Insulin-Like Growth Factor-I Splice Variants.” Brain Research 1009 (1-2) (May): 213–218. doi:10.1016/j.brainres.2004.02.049.
  28. Quigley, A F, K J Bulluss, I L B Kyratzis, K Gilmore, T Mysore, K S U Schirmer, E L Kennedy, et al. 2013. “Engineering a Multimodal Nerve Conduit for Repair of Injured Peripheral Nerve.” Journal of Neural Engineering 10 (1) (January 3): 016008. doi:10.1088/1741-2560/10/1/016008.
  29. Dai, Zhongquan, Feng Wu, Ella W. Yeung, and Yinghui Li. 2010. “IGF-IEc Expression, Regulation and Biological Function in Different Tissues.” Growth Hormone & IGF Research 20 (4) (August): 275–281. doi:10.1016/j.ghir.2010.03.005.
  30. Riddoch-Contreras, Joanna, Shi-Yu Yang, James R.T. Dick, Geoffrey Goldspink, Richard W. Orrell, and Linda Greensmith. 2009. “Mechano-Growth Factor, an IGF-I Splice Variant, Rescues Motoneurons and Improves Muscle Function in SOD1G93A Mice.” Experimental Neurology 215 (2) (February): 281–289. doi:10.1016/j.expneurol.2008.10.014.
  31. Górecki, Dariusz C., Małgorzata Beręsewicz, and Barbara Zabłocka. 2007. “Neuroprotective Effects of Short Peptides Derived from the Insulin-Like Growth Factor 1.” Neurochemistry International 51 (8) (December): 451–458. doi:10.1016/j.neuint.2007.04.030.
  32. Dluzniewska, J. 2005. “A Strong Neuroprotective Effect of the Autonomous C-Terminal Peptide of IGF-1 Ec (MGF) in Brain Ischemia.” The FASEB Journal (September 15). doi:10.1096/fj.05-3786fje.
  33. Rubovitch, Vardit, Adi Shachar, Haim Werner, and Chaim G. Pick. 2011. “Does IGF-1 Administration after a Mild Traumatic Brain Injury in Mice Activate the Adaptive Arm of ER Stress?” Neurochemistry International 58 (4) (March): 443–446. doi:10.1016/j.neuint.2011.01.009.
  34. Kizhakke Madathil, Sindhu, Heather N. Evans, and Kathryn E. Saatman. 2010. “Temporal and Regional Changes in IGF-1/IGF-1R Signaling in the Mouse Brain after Traumatic Brain Injury.” Journal of Neurotrauma 27 (1) (January): 95–107. doi:10.1089/neu.2009.1002.
  35. Procaccini, Claudio, Marianna Santopaolo, Deriggio Faicchia, Alessandra Colamatteo, Luigi Formisano, Paola de Candia, Mario Galgani, Veronica De Rosa, and Giuseppe Matarese. 2016. “Role of Metabolism in Neurodegenerative Disorders.” Metabolism 65 (9) (September): 1376–1390. doi:10.1016/j.metabol.2016.05.018.
  36. Lane, Elizabeth M., Timothy J. Hohman, and Angela L. Jefferson. 2016. “Insulin-Like Growth Factor Binding Protein-2 Interactions with Alzheimer’s Disease Biomarkers.” Brain Imaging and Behavior (November 5). doi:10.1007/s11682-016-9636-0.
  37. Ostrowski, Philip P., Andrew Barszczyk, Julia Forstenpointner, Wenhua Zheng, and Zhong-Ping Feng. 2016. “Meta-Analysis of Serum Insulin-Like Growth Factor 1 in Alzheimer’s Disease.” Edited by Madepalli K. Lakshmana. PLOS ONE 11 (5) (May 26): e0155733. doi:10.1371/journal.pone.0155733.
  38. Rusch, Heather L., Pedro Guardado, Tristin Baxter, Vincent Mysliwiec, and Jessica M. Gill. 2015. “Improved Sleep Quality Is Associated with Reductions in Depression and PTSD Arousal Symptoms and Increases in IGF-1 Concentrations.” Journal of Clinical Sleep Medicine (June 15). doi:10.5664/jcsm.4770.
  39. Zanou, Nadège, and Philippe Gailly. 2013. “Skeletal Muscle Hypertrophy and Regeneration: Interplay Between the Myogenic Regulatory Factors (MRFs) and Insulin-Like Growth Factors (IGFs) Pathways.” Cellular and Molecular Life Sciences 70 (21) (April 4): 4117–4130. doi:10.1007/s00018-013-1330-4.
  40. Janssen, Joseph A. M. J. L., Leo J. Hofland, Christian J. Strasburger, Elisabeth S. R. van den Dungen, and Mario Thevis. 2016. “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.” Edited by Andrea Morrione. PLOS ONE 11 (3) (March 18): e0150453. doi:10.1371/journal.pone.0150453.
  41. Kandalla, Prashanth Kumar, Geoffrey Goldspink, Gillian Butler-Browne, and Vincent Mouly. 2011. “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.” Mechanisms of Ageing and Development 132 (4) (April): 154–162. doi:10.1016/j.mad.2011.02.007.
  42. Shang, Jin, Xin Fan, and Huan Liu. 2015. “The Role of Mechano-Growth factor-E Peptide in the Regulation of Osteosarcoma.” Oncology Letters (June 9). doi:10.3892/ol.2015.3339.
  43. Armakolas, Athanasios, Anastassios Philippou, Zacharoula Panteleakou, Adrianos Nezos, Antigone Sourla, Constantina Petraki, and Michael Koutsilieris. 2010. “Preferential Expression of IGF-1Ec (MGF) Transcript in Cancerous Tissues of Human Prostate: Evidence for a Novel and Autonomous Growth Factor Activity of MGF E Peptide in Human Prostate Cancer Cells.” The Prostate 70 (11) (April 6): 1233–1242. doi:10.1002/pros.21158.
  44. IGF-IEc expression is associated with advanced clinical and pathological stage of prostate cancer. Savvani A, Petraki C, Msaouel P, Diamanti E, Xoxakos I, Koutsilieris M. Anticancer Res. 2013 Jun; 33(6):2441-5. [PMID:23749893]
  45. Veronese, Francesco M, and Anna Mero. 2008. “The Impact of PEGylation on Biological Therapies.” BioDrugs 22 (5): 315–329. doi:10.2165/00063030-200822050-00004.
  46. Martins, Karen J.B., Stefan M. Gehrig, Timur Naim, Stefanie Saenger, Dale Baum, Friedrich Metzger, and Gordon S. Lynch. 2013. “Intramuscular Administration of PEGylated IGF-I Improves Skeletal Muscle Regeneration after Myotoxic Injury.” Growth Hormone & IGF Research 23 (4) (August): 128–133. doi:10.1016/j.ghir.2013.03.002.
  47. George Vassilakos, Anastassios Philippou, Panagiotis Tsakiroglou, Michael Koutsiliers, “Biological activity of the e domain of the IGF-1Ec as addressed by synthetic peptides” HORMONES 2014, 13(2):182-196
  48. McKoy G, Ashley W, Mander J, Yang SY, Williams N, et al. (1999) Expression of insulin growth factor-1 splice variants and structural genes in rabbit skeletal muscle induced by stretch and stimulation. J Physiol 516 (Pt 2): 583–592
  49. Schlegel, Werner, Adalbert Raimann, Daniel Halbauer, Daniela Scharmer, Susanne Sagmeister, Barbara Wessner, Magdalena Helmreich, Gabriele Haeusler, and Monika Egerbacher. 2013. “Insulin-Like Growth Factor I (IGF-1) Ec/Mechano Growth Factor – A Splice Variant of IGF-1 Within the Growth Plate.” Edited by Francisco J. Esteban. PLoS ONE 8 (10) (October 11): e76133. doi:10.1371/journal.pone.0076133.
  50. Therapeutic use of growth factors in the musculoskeletal system in sports-related injuries. Bachl N, Derman W, Engebretsen L, Goldspink G, Kinzlbauer M, Tschan H, Volpi P, Venter D, Wessner B. J Sports Med Phys Fitness. 2009 Dec; 49(4):346-57. [PMID:20087293]
  51. Thevis, Mario, Andreas Thomas, Hans Geyer, and Wilhelm Schänzer. 2014. “Mass Spectrometric Characterization of a Biotechnologically Produced Full-Length Mechano Growth Factor (MGF) Relevant for Doping Controls.” Growth Hormone & IGF Research 24 (6) (December): 276–280. doi:10.1016/j.ghir.2014.10.004.

Last updated: