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

FEBS Letters

Kübler, Bernd⁴  Zapf, Jürgen⁵  Braulke, Thomas⁴  Höning, Stefan²  Storch, Stephan⁴  Ackmann, Michael³  Blum, Werner¹ 

[1] Eli Lilly and Company, Bad Homburg, and University Children's Hospital, Leipzig, Germany;Institute for Biochemistry II, University of Göttingen, D-37073 Göttingen, Germany;Megamedics GmbH, Hafenstr. 32, D-22880 Wedel, Germany;Children's Hospital-Biochemistry, University of Hamburg, Martinistr. 52, D-20246 Hamburg, Germany;Internal Medicine, University Hospital, CH-8091 Zurich, Switzerland

关键词: Insulin-like growth factor;    Insulin-like growth factor-binding protein-3;    Transferrin;    Surface plasmon resonance spectroscopy;    IGF;    insulin-like growth factor;    IGFBP;    insulin-like growth factor-binding protein;    Tf;    transferrin;    ALS;    acid-labile subunit;    HPLC;    high performance liquid chromatography;    AD;    activation domain;   

DOI  :  10.1016/S0014-5793(01)03204-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown