Phosphorylated insulin-like growth factor (IGF)-binding protein-1 (IGFBP-1) inhibits while non-phosphorylated IGFBP-1 stimulates IGF-I-induced amino acid uptake by cultured trophoblast cells.

The effects of phosphorylated insulin-like growth factor-binding protein (pIGFBP-1) and non-phosphorylated (npIGFBP-1) IGFBP-1 on amino acid uptake induced by IGF-I were studied using cultured trophoblast cells. Trophoblast cells obtained from term pregnancy were incubated with indicated concentrations of pIGFBP-1 or npIGFBP-1 for 24 h and further incubated with 10 nM IGF-I for 3 h. Cells were then incubated with 3H-alpha-amino isobutyric acid (3H-AIB) for 30 min. Both pIGFBP-1 and npIGFBP-1 alone had no effect on 3H-AIB uptake; however, pIGFBP-1 inhibited IGF-I-stimulated 3H-AIB uptake with an ED50 of 0.26 nM while npIGFBP-1 potentiated 3H-AIB uptake with an ED50 of 0.27 nM. Maternal IGF-I promotes fetal growth by stimulating nutrient transport in the placenta. As shown in this study, pIGFBP-1 inhibits while npIGFBP-1 stimulates this IGF-I action in the placenta. Thus, it is suggested that IGFBP-1 phosphoisoforms are also involved in fetal growth by modulating IGF-I action in the placenta.