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IGF-1 LR3
The story
IGF-1 was first seen in 1957 as the sulfation factor, the substance growth hormone makes the liver release to build cartilage. In 1978 Ernst Rinderknecht and Rene Humbel in Zurich sequenced it and showed it looked like proinsulin. In Adelaide in the early 1990s, Geoffrey Francis, John Ballard and colleagues at CSIRO and GroPep built LR3: the Arg-3 swap and the front extension made it escape the binding proteins and act much more strongly. Frank Tomas in the same group showed it was strongly anabolic in rats under steroid stress. Russian endocrinologists, such as Gennadinik and Nelaeva, describe IGF-1 as the conductor of growth hormone's effects in metabolism, cell renewal and ageing.
Sources
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- The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin (Abstract · checked 2026-10-13)
- 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 (Abstract · checked 2026-10-13)
- Insulin-like growth factor-I (IGF-I) and especially IGF-I variants are anabolic in dexamethasone-treated rats (Abstract · checked 2026-10-13)
- Роль инсулиноподобного фактора роста-I в метаболизме, регуляции клеточного обновления и процессах старения (Gennadinik, Nelaeva, Obesity and Metabolism 2010) (Abstract · checked 2026-10-13)