Isolation of complexes formed between insulin-like growth factor-binding protein-3 and transferrin from the human serum

Insulin-like growth factors (IGFs) play an important role in the regulation of cell growth, differentiation and metabolism. The amount of free, biologically active IGFs is regulated by the IGF-binding proteins (IGFBPs). IGFBP-3 is the most abundant binding protein and it is known to interact wit...

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Bibliographic Details
Main Authors: Miljuš Goran, Petrović Miomir, Nedić Olgica
Format: Article
Language:English
Published: Serbian Chemical Society 2012-01-01
Series:Journal of the Serbian Chemical Society
Subjects:
Online Access:http://www.doiserbia.nb.rs/img/doi/0352-5139/2012/0352-51391100211M.pdf
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Summary:Insulin-like growth factors (IGFs) play an important role in the regulation of cell growth, differentiation and metabolism. The amount of free, biologically active IGFs is regulated by the IGF-binding proteins (IGFBPs). IGFBP-3 is the most abundant binding protein and it is known to interact with other circulating proteins, including transferrin (Tf). In order to elucidate the possible role of IGF/IGFBP-3 in the iron metabolism, it is necessary to isolate IGFBP-3/Tf complexes. Several affinity-based techniques were employed. Results have shown that only double immunoprecipitation method with anti-Tf and anti-IGFBP-3 antibodies selectively separated complexes from other molecular forms, such as monomers, oligomers or fragments of IGFBP-3 and Tf. Isolated complexes can now be used to investigate the relationship between IGF/IGFBP-3 and iron, both in structural and metabolic tеrms.
ISSN:0352-5139