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Pregnancy |
Endocrine Sciences3
School of Biological Sciences,4 University of Manchester, Manchester, M13 9PT, United Kingdom
Academic Unit of Obstetrics & Gynaecology,5 Human Development and Reproductive Health Academic Group, University of Manchester, St Mary's Hospital, Manchester, M13 OJH, United Kingdom
Growth in utero depends on adequate development and function of the fetal/maternal interface. During pregnancy, the insulin-like growth factors (IGFs), which are known to be critically involved in placental development, are controlled by a binding protein—IGFBP-1—produced by maternal decidualized endometrium. We have previously found that decidua also produces a protease that cleaves IGFBP-1; because proteolysis of IGFBP-1 may represent a mechanism for increasing IGF bioavailability, the present study aimed to identify the protease and its regulators to understand the control of IGF activity at the maternal/fetal interface. Immunochemical methods were used to show that decidualized endometrial cells from first-trimester pregnancy produced matrix metalloprotease (MMP)-3; incubation of IGFBP-1 with either this enzyme or MMP-9, which is produced by the trophoblast, produced a series of fragments that were unable to bind IGF-I. Western immunoblot analysis and immunocytochemistry demonstrated that decidual cells also produce tissue inhibitor of metalloproteinase (TIMP)-1, TIMP-2, and 
2-macroglobulin, and all three inhibitors attenuated the proteolysis of IGFBP-1 by MMPs. The N-terminal sequence analysis of the fragments revealed that the enzymes cleave IGFBP-1 at 145Lys/Lys146, resulting in a small (9-kDa) C-terminal peptide of IGFBP-1. These findings suggest cleavage of IGFBP-1 as a novel mechanism in the control of placental development by matrix metalloproteases.
2 Correspondence: Melissa Westwood, Endocrine Sciences, University of Manchester, Stopford Building, Oxford Road, Manchester, M13 9PT, U.K. FAX: 44 161 275 5958; melissa.westwood{at}man.ac.uk
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