The BioGRID | PUBLICATION VIEW

	FEBS Lett. Dec (2001); 509(3):395-8
Transferrin binds insulin-like growth factors and affects binding properties of insulin-like growth factor binding protein-3.
Storch S, Kubler B, Honing S, Ackmann M, Zapf J, Blum W, Braulke T
Children's Hospital-Biochemistry, University of Hamburg, Germany.
Abstract: 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.
[PUBMED: 11749962]