IGF-binding proteins - the pieces are failing into place

Author(s): Bach, LA; Headey, SJ; Norton, RS;
Details: Publication Year 2005-07,Volume 16,Issue #5,Page 228-234
Journal Title: TRENDS IN ENDOCRINOLOGY AND METABOLISM
Publication Type: Journal Article
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.
Publisher: ELSEVIER SCIENCE LONDON
Keywords: C-TERMINAL DOMAIN; FACTOR (IGF)-BINDING PROTEIN-5; GROWTH-FACTOR-I; RECEPTOR INTERACTIONS; CANCER DEVELOPMENT; O-GLYCOSYLATION; LIGAND-BINDING; CELL-MIGRATION; HIGH-AFFINITY; AMINO-ACIDS
Publisher's Version: https://doi.org/10.1016/j.tem.2005.05.005
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2005-07-01 12:00:00