No abstract

No abstract

Fetal growth in utero depends on the proper development and function of the placenta. Insulin-like growth factors (IGFs) are critically involved in placental development. During pregnancy, an IGF-binding protein, IGFBP-1, which is produced by maternal decidua, plays an important role in the control of the bioavailability of IGFs. It has recently been proposed that cleavage of decidual IGFBP-1 by matrix metalloproteases is a novel mechanism in the control of placental development. The presence of IGFBP-1 in solubilized placental cell membranes, i.e. its association with the membranes, was detected in an earlier work. Herein, it is shown that IGFBP-1 from the solubilized membranes forms dimers, as well as high molecular mass complexes. IGFBP-1 dimers preferably contain the non-phosphorylated form of IGFBP-1. The high molecular mass forms are polymers of IGFBP-1 or its complexes with other membrane proteins. Dimerization of IGFBP-1, together with its association with the placental cell membrane, could serve as an additional mechanism of the regulation of IGF availability to the type 1 IGF receptors.

No abstract