Osteopontin increases the expression of β1, 4-galactosyltransferase-I and promotes adhesion in human RL95-2 cells.

Beta1, 4-Galactosyltransferase-I (β1, 4-GalT-I), which transfers galactose from UDP-Gal to N-acetylglucosamine and N-acetylglucosamine-terminated oligosaccharides of N- and O-linked glycans in a β(1-4) linkage, plays a critical role in cell adhesion, sperm-egg recognition, neurite growth, and tumor cell migration and invasion. Our previously experiments also show that β1, 4-GalT-I was up-regulated by estrogens and some important cytokines of embryo implantation especially Interleukin-1 (IL-1), TGF-α and Leukemia Inhibitory Factor (LIF) in endometrial cells. In the receptive phase human uterus, osteopontin (OPN) is the most highly up-regulated extracellular matrix/adhesion molecule/cytokine. In this study, we demonstrated the correlated expression of OPN and β1, 4-GalT-I in endometrium during early pregnancy, and recombinant human OPN (rhOPN) protein induced the β1, 4-GalT-I up-regulation in RL95-2 cells. Inhibition of MEK/ERK, PI3K/AKT and NF-κB suppressed rhOPN-induced β1, 4-GalT-I expression. In addition, rhOPN promoted the adhesion of blastocysts cells in vitro in β1, 4-GalT-I-dependent manner. Moreover, the adhesion is greatly inhibited when β1, 4-GalT-I was blocked with the specific antibody. Taken together, our data suggest that β1, 4-GalT-I provides a mechanism to bridge embryo to endometrium during implantation.