Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3

FEBS Lett. 2001 Dec 14;509(3):395-8. doi: 10.1016/s0014-5793(01)03204-5.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, Affinity
  • Chromatography, High Pressure Liquid
  • Humans
  • Insulin-Like Growth Factor Binding Protein 3 / metabolism*
  • Insulin-Like Growth Factor II / metabolism*
  • Kinetics
  • Mass Spectrometry
  • Precipitin Tests
  • Protein Binding
  • Surface Plasmon Resonance
  • Transferrin / metabolism*
  • Two-Hybrid System Techniques
  • Yeasts


  • Insulin-Like Growth Factor Binding Protein 3
  • Transferrin
  • Insulin-Like Growth Factor II