PHOSPHORYLATION OF INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN-1 INCREASES IN HUMAN AMNIOTIC-FLUID AND DECIDUA FROM EARLY TO LATE PREGNANCY

Different fractions of insulin-like growth factor-binding protein-1 (IGFBP-1) from anion exchange chromatography represent differently phosphorylated forms as demonstrated by protein kinase and alkaline phosphatase treatments. The major fraction is non-phosphorylated. Three minor fractions are more phosphorylated and, in native polyacrylamide gel electrophoresis (PAGE), they migrate faster than the major fractions. We studied the changes in phosphorylation of decidual and amniotic fluid IGFBP-1 during pregnancy. Both in decidua and in amniotic fluid the degree of phosphorylation increased from early to late pregnancy, as indicated by faster mobility of IGFBP-1 in native PAGE and increased relative amount of the phosphorylated forms in anion exchange chromatography. The more phosphorylated forms had higher IGF-binding affinity than the less phosphorylated forms. As the degree of phosphorylation of IGFBP-1 is highest in full term decidua it is likely that the inhibitory role of IGFBP-1 is accentuated in the end of pregnancy.