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Trends Endocrinol Metab. 2005 Jul;16(5):228-34.

IGF-binding proteins--the pieces are falling into place.

Author information

1
University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg 3084, Australia. l.bach@unimelb.edu.au

Abstract

The six insulin-like growth factor (IGF)-binding proteins (IGFBPs) are important regulators of IGF actions. IGF-independent actions of several IGFBPs have also been described. IGFBPs contain highly conserved N- and C-terminal domains, both of which are important for high-affinity IGF binding. The C-domain also binds a large number of other biomolecules, thereby modulating IGF binding and mediating IGF-independent effects. The 3D structures of the IGF-binding region of the N-domain of IGFBP-5 and the entire C-domain of IGFBP-6 have been solved recently, providing new insights into IGFBP modulation of IGF actions, and structural studies might be expected to do the same for IGF-independent actions. IGFBP-based therapies for diseases such as cancer are promising, and this recent progress will enhance their development.

PMID:
15935690
DOI:
10.1016/j.tem.2005.05.005
[Indexed for MEDLINE]

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