Cloning, characterization, and expression of a human insulin-like growth factor binding protein

Insulin-like growth factors (IGFs) bind to specific proteins present in extracellular fluids. One of these binding proteins (IGF-BP) was purified from human amniotic fluid and was shown to potentiate the effects of IGF-I in vitro (10). In these studies, a polyclonal antibody to this protein was used to isolate a cDNA clone from a human decidua library. This clone encodes a polypeptide of 25,832 daltons that includes the sequences of 9 tryptic peptides that had been prepared from the purified IGF-BP. The protein has 15 cysteines that are clustered at the amino and carboxy ends of the molecule. The protein has an RGD sequence near its C-terminus, which may account for its ability to attach to cells and to potentiate the biological actions of IGF-I.