Study summary · research use only
The effect of insulin-like growth factor analogs on turkey satellite cell and embryonic myoblast proliferation
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This in vitro study examined effects of several human and chicken insulin-like growth factor (IGF) analogs on turkey satellite cell and embryonic myoblast proliferation in serum-free medium. Human and chicken IGF-I and IGF-II at 13.1 nM produced similar proliferation rates. Human Des(1-6)IGF-II showed potency similar to native human and chicken IGF-II, while chicken LR3 IGF-I showed reduced activity compared with chicken IGF-I, and human [Leu27]IGF-II showed a reduced effect on proliferation. Receptor-binding assays showed chicken LR3 IGF-I had reduced ability to compete with labeled IGF-I for binding. The authors suggest IGF-binding proteins had little influence on Type I receptor action in these cells, and that altering IGF to avoid binding-protein interaction may also change receptor binding. Species: turkey (cells), with human and chicken IGF proteins tested.
Abstract
The effects of several human and chicken insulin-like growth factor (IGF) analogs on turkey satellite cell and embryonic myoblast proliferation were examined in serum-free medium. Similar rates of proliferation were observed when human or chicken IGF-I or IGF-II (13.1 nM) was administered to satellite cells. The biopotency of two analogs, which were modified to prevent interaction with IGF-binding proteins, was also examined. Human Des(1-6)IGF-II was equipotent to native human and chicken IGF-II. However, the chicken LR3 IGF-I analog was significantly less active toward satellite cells and embryonic myoblasts compared with chicken IGF-I. Human [Leu27] IGF-II, an analog designed to have reduced affinity to the IGF Type I receptor but unaltered binding to IGF-binding proteins, had a diminished effect on cell proliferation. Examination of IGF receptor binding characteristics revealed that chicken LR3 IGF-I had reduced ability to compete with [125I]hIGF-I for binding to satellite cells or embryonic myoblasts compared with chicken IGF-I. The observed biological responses to IGF suggest that IGF-binding proteins have little effect on Type I IGF receptor action in these cell types in serum-free medium. The results also suggest that alterations of the IGF molecule to prevent interaction with binding proteins may also alter receptor binding affinity.
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