Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3.
In the circulation, most of the insulin-like growth factors (IGFs) are bound to a ternary 150 kDa complex with IGF-binding protein (IGFBP)-3 and the acid labile subunit. In the current study, we identify transferrin (Tf) by mass spectrometry, and immunoprecipitation as a component of a major IGF-binding fraction separated from ... human plasma. IGF ligand blotting, cross-linkage experiments and surface plasmon resonance spectrometry have been used to demonstrate the capability of Tf to bind IGFs specifically. In combination with Tf, IGFBP-3 showed a 5-fold higher affinity for IGF-II than IGFBP-3 alone. The data suggest that Tf may play an important role in regulating IGF/IGFBP-3 functions.
Mesh Terms:
Chromatography, Affinity, Chromatography, High Pressure Liquid, Humans, Insulin-Like Growth Factor Binding Protein 3, Insulin-Like Growth Factor II, Kinetics, Mass Spectrometry, Precipitin Tests, Protein Binding, Surface Plasmon Resonance, Transferrin, Two-Hybrid System Techniques, Yeasts
Chromatography, Affinity, Chromatography, High Pressure Liquid, Humans, Insulin-Like Growth Factor Binding Protein 3, Insulin-Like Growth Factor II, Kinetics, Mass Spectrometry, Precipitin Tests, Protein Binding, Surface Plasmon Resonance, Transferrin, Two-Hybrid System Techniques, Yeasts
FEBS Lett.
Date: Dec. 14, 2001
PubMed ID: 11749962
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