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

      Trends in Endocrinology and Metabolism

      Animals, Humans, Insulin-Like Growth Factor Binding Proteins, chemistry, genetics, physiology, Models, Molecular

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          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.

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          Journal
          15935690
          10.1016/j.tem.2005.05.005

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