title: IGF-binding proteins--the pieces are falling into place.
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.
authors.affiliation: University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg 3084, Australia. l.bach@unimelb.edu.au
authors.forename: Leon A
authors.initials: LA
authors.lastname: Bach
authors.forename: Stephen J
authors.initials: SJ
authors.lastname: Headey
authors.forename: Raymond S
authors.initials: RS
authors.lastname: Norton
mesh_terms: D000818:Animals; D006801:Humans; D018969:Insulin-Like Growth Factor Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D008958:Models, Molecular
chemical_list: D018969:Insulin-Like Growth Factor Binding Proteins