The Effect of Insulin-Like Growth Factor Analogs on Turkey Satellite Cell and Embryonic Myoblast Proliferation
| Autor: | G. L. Francis, J. A. Clapper, Kysa K. Gilkerson, Douglas C. McFarland, J. P. McMurtry, Jane E. Pesall |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Turkeys
Myoblast proliferation Cell type medicine.medical_treatment Cell Cell Culture Techniques Binding Competitive DNA-binding protein Iodine Radioisotopes Insulin-like growth factor Insulin-Like Growth Factor II medicine Animals Humans Insulin-Like Growth Factor I Muscle Skeletal Chemistry Cell growth Growth factor General Medicine Embryonic stem cell Cell biology medicine.anatomical_structure Animal Science and Zoology Chickens Cell Division |
| Zdroj: | Poultry Science. 80:944-948 |
| ISSN: | 0032-5791 |
| DOI: | 10.1093/ps/80.7.944 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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