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Transferrin binds insulin‐like growth factors and affects binding properties of insulin‐like growth factor binding protein‐3
Author(s) -
Storch Stephan,
Kübler Bernd,
Höning Stefan,
Ackmann Michael,
Zapf Jürgen,
Blum Werner,
Braulke Thomas
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03204-5
Subject(s) - transferrin , immunoprecipitation , surface plasmon resonance , chemistry , binding protein , plasma protein binding , protein subunit , insulin like growth factor binding protein , blot , ternary complex , biochemistry , growth factor , insulin , glycoprotein , insulin like growth factor , biology , receptor , endocrinology , enzyme , gene , materials science , nanoparticle , nanotechnology
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.