Description
Theinsulin-like growth factor binding protein (IGFBP) family consists of six structurallyrelated proteins that bind IGF with high affinity. These proteins share conservedcysteine-rich N- and C-terminal regions that participate in IGF binding.IGFBPs regulate the bioavailability of IGFs and modulate their biologicalactivities, both positively and negatively. Some IGFBPs also have intrinsicbioactivity that is IGF-independent. Post-transitional modifications of theIGFBPs, including glycosylation, phosphorylation and proteolysis, influenceIGF binding affinities and tissue localization, affecting both theIGF-dependent and independent functions