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|Title:||IGF-binding proteins--the pieces are falling into place.|
|Authors:||Bach, Leon A;Headey, Stephen J;Norton, Raymond S|
University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg 3084, Australia
|Citation:||Trends in Endocrinology and Metabolism: Tem; 16(5): 228-34|
|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.|
|Internal ID Number:||15935690|
Insulin-Like Growth Factor Binding Proteins.chemistry.genetics.physiology
|Appears in Collections:||Journal articles|
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