Glycoproteins expressed at the fetal-maternal interface have been shown to exert immunomodulating effects. Glycodelin, hCG and transferrin have been used in in vitro experiments as ligands to block E-selectin-mediated cell adhesion. We found that glycodelin is a strong inhibitor of the E-selectin-mediated cell adhesion with a 10(3)-fold increase in potency compared to the monovalent tetrasaccharide sialyl Lewis X. HCG with distinct carbohydrate expression is also an effective selectin antagonist, whereas the potency of transferrin is low. This could indicate a possible role of glycodelin, hCG and transferrin in preventing leukocyte adhesion to the fetal trophoblast. In decidual tissue of abortion patients, glycodelin expression was significantly reduced compared to normal gestation. These results were confirmed by in situ hybridization. Moreover, glycodelin expression in endometrial cells in vitro could be stimulated by addition of hCG. Because hCG is down-regulated in women with abortion, we speculate that hCG could be one of the factors regulating glycodelin expression. Galectins are structurally related proteins with the ability to bind beta-galactosides through a conserved carbohydrate recognition domain. Galectin-1 (gal-1) expression in the syncytiotrophoblast is down-regulated in early pregnancy loss. Gal-1 recognizes the Thomsen-Friedenreich disaccharide (Galbeta1-3GalNAc-) on the syncytiotrophoblast and extravillous trophoblast. Gal-1 also inhibited trophoblast cell proliferation but did not induce apoptosis in BeWo cells. Ligation of Gal-1 on trophoblast cells may have regulatory effects on trophoblast cell differentiation. Decreased expression of Gal-1 may partly explain disturbed trophoblast differentiation during early placentation leading to early pregnancy loss.
Copyright (c) 2010 Elsevier Ireland Ltd. All rights reserved.