Insulin Like Growth Factor (IGF)-1 DES is a 67 amino acid residue analogy to native IGF-1, which has been documented as an agent for inducing hyperplasia and stimulating cellular proliferation1. By truncating the original IGF-1 polypeptide – a 70 amino acid residue sequence – to just 67 amino acids, retaining residue numbers 4-70 (hence the synonym ‘IGF-1 [4-70]’)2, IGF-1 DES introduces massive enhancements to IGF-1’s biological activity while making marginal improvements to its structural stability, and therefore, residence time, in vivo.
Animal studies have demonstrated the ability of IGF-1 DES to bind directly to natural IGF receptors and stimulate new tissue formation, while inhibiting apoptosis (programmed cell death) in existing tissues3. Especially at muscle cell sites, IGF-1 species are noted to enhance amino acid recruitment, augment the synthesis of new proteins while minimizing the digestion of intracellular protein as a fuel source. Instead, fat deposits are used as energy sources while IGF species are biochemically active4.
Product Comparison
IGF-1 is a key factor in mediating of growth-promoting effects of growth hormone (GH)5. This particular IGF-1 species was developed in order to avoid interaction with IGFBPs (Insulin Like Growth Factor Binding Proteins), which are known to hinder the activity of native IGF-1 over time6. By avoiding this interplay IGF-1 DES is capable of achieving highly active, unimpeded biological activity, which leads to its utility as a fast-acting facilitator of GH-stimulated biochemical activity.
IGF-1 DES and IGF-1 LR3 have both been shown to be more active relative to native IGF-1 when it comes to stimulating new cell growth in animal trials. Compared to IGF-1 LR3, IGF-1 DES is considered to be multi-fold more active as a stimulant of acute hypertrophy7.
Studies investigating the effects of concurrent IGF-1 species and GH (or GH secretagogue) administration have identified their synergy5 in promoting the development of lean body mass and reduction of fat stores in animal test subjects.
Synonyms:
Insulin Like Growth Factor-1 DES; IGF-1 DES; IGF-1 DES 1-3; IGF-1 DES (1-3); DES 1-3; DES 1-3, DES (1-3), IGF-1 (4-70); Somatomedin C analogue; Detropin
Peer-Reviewed Sources:
- Musarò, A., McCullagh, K., Paul, A., Houghton, L., Dobrowolny, G., Molinaro, M., & Rosenthal, N. (2001). Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle. Nature genetics, 27(2), 195-200. ↩︎
- Shavlakadze, T., Chai, J., Maley, K., Cozens, G., Grounds, G., Winn, N., & Grounds, M. D. (2010). A growth stimulus is needed for IGF-1 to induce skeletal muscle hypertrophy in vivo. Journal of cell science, 123(6), 960-971. ↩︎
- Tavakkol, A., Elder, J. T., Griffiths, C. E., Cooper, K. D., Talwar, H., Fisher, G. J., & Voorhees, J. J. (1992). Expression of growth hormone receptor, insulin-like growth factor 1 (IGF-1) and IGF-1 receptor mRNA and proteins in human skin. Journal of Investigative Dermatology, 99(3), 343-349. ↩︎
- LeRoith, D., & Yakar, S. (2007). Mechanisms of disease: metabolic effects of growth hormone and insulin-like growth factor 1. Nature Clinical Practice Endocrinology & Metabolism, 3(3), 302-310. ↩︎
- Berryman, D. E., Christiansen, J. S., Johannsson, G., Thorner, M. O., & Kopchick, J. J. (2008). Role of the GH/IGF-1 axis in lifespan and healthspan: lessons from animal models. Growth Hormone & IGF Research, 18(6), 455-471. ↩︎
- Francis, G. L., Ross, M., Ballard, F. J., Milner, S. J., Senn, C., McNeil, K. A., & Wells, J. R. E. (1992). 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. Journal of molecular endocrinology, 8(3), 213-223. ↩︎
- Ding, H. U., Gao, X. L., Hirschberg, R., Vadgama, J. V., & Kopple, J. D. (1996). Impaired actions of insulin-like growth factor 1 on protein Synthesis and degradation in skeletal muscle of rats with chronic renal failure. Evidence for a postreceptor defect. Journal of Clinical Investigation, 97(4), 1064. ↩︎
