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Molecular Human Reproduction, Vol. 7, No. 1, 79-87, January 2001
© 2001 European Society of Human Reproduction and Embryology

Implantation and pregnancy

Regulation of IGF bioavailability in pregnancy

J.M. Gibson1,3, J.D. Aplin2,4, A. White3,4 and M. Westwood2,4,5

1 Department of Diabetes & Endocrinology, Hope Hospital, Salford, M6 8HD, 2 Academic Unit of Obstetrics & Gynaecology, St Mary's Hospital, Manchester, M13 0JH, 3 Endocrine Sciences Research Group, University of Manchester, Manchester, M13 9PT and 4 School of Biological Sciences, University of Manchester, Manchester, M13 9PT, UK

Abstract

During pregnancy, insulin-like growth factors (IGFs) are important for growth of fetal and maternal tissues. One of the IGF binding proteins, IGFBP-1, is thought to regulate their activity within the local environment of the placenta. IGFBP-1 usually exists as a phosphorylated, high affinity species, which sequesters IGFs, thereby inhibiting their actions. This study has investigated the mechanisms that release IGF from IGFBP-1 at the maternal–fetal interface. Under basal conditions, human decidualized endometrium produces both non-phosphorylated (np) and phosphorylated (p) isoforms of IGFBP-1; however, in the presence of IGF-II, which is a trophoblast secretory product, npIGFBP-1 was preferentially produced. Furthermore, we found that trophoblast, presumably via placental alkaline phosphatase, can de-phosphorylate pIGFBP-1. Since npIGFBP-1 has decreased affinity for IGF-I, these effects should enhance IGF-I bioavailability. In addition, we found that decidual cells produce a protease, which cleaves IGFBP-1, but only when it is non-phosphorylated; [125I]-npIGFBP-1 is proteolysed into 14 and 17 kDa fragments which have markedly reduced affinity for IGF. We therefore propose paracrine modulation of IGFBP-1 at the maternal–fetal interface involving a multi-step process of de-phosphorylation and proteolysis; this will result in enhanced IGF bioavailability and is likely to represent an important mechanism for controlling fetal and maternal tissue growth.

decidua/IGFBP-1/phosphorylation/proteolysis/trophoblast

Notes

5 To whom correspondence should be addressed at: Endocrine Sciences Research Group, University of Manchester, Oxford Road, Manchester, M13 9PT, UK. E-mail: melissa.westwood{at}man.ac.uk


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