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Adhesion of human uroepithelial cells to E-selectin: Possible involvement of sialosyl LewisA-ganglioside
Authors:Arkadiusz G. Klopocki  Anna Krop-Watorek  Danuta Dus  Maciej Ugorski
Abstract:
In a previous study we showed that tumorigenic and invasive human uroepithelial cell lines are characterized by the presence of sialosyl Lea (sLea) ganglioside. Our data suggested that expression of this glycolipid correlated with acquisition of the malignant phenotype by human urothelial cells. To evaluate the postulated adhesion function of sLea antigen, we studied the adherence of 6 human urothelial cell lines with different expressions of this carbohydrate structure to E-selectin-expressing CHO cells. The only cell line that bound specifically to E-selectin was Hu 1703He, which expressed the highest level of sLea antigen. The involvement of carbohydrate-E-selectin interaction in the adhesion of Hu 1703He cells was indicated by the following facts: (i) anti-E-selectin monoclonal antibody (MAb) completely abolished binding to E-selectin-expressing CHO cells; (ii) removal of sialic acid from Hu 1703He cells highly decreased the adhesion. Adhesion correlated with the presence of several sLea-carrying glycoproteins, which was shown by immunoblotting of Hu 1703He cell lysate with anti-sLea MAb 19-9. The binding of antibody was abolished when cell lysate was treated with O-sialoglycoprotein endopeptidase, suggesting that sLea is present on O-linked oligosaccharides. However, incubation of Hu 1703He cells with O-sialoglycoprotease had no effect on adhesion to E-selectin or on binding of 19-9 MAb to the cell surface. Our data suggest that (i) protein-bound sLea oligosaccharides represent only a minor portion of whole sLea antigen produced by uroepithelial cells; (ii) effective binding to E-selectin occurs when sLea oligosaccharide present on cell-surface glycosphingolipids is expressed in high density since the cell lines with moderate expression of sLea ganglioside did not bind to E-selectin-transfected CHO cells. © 1996 Wiley-Liss, Inc.
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