Binding of oxidized Jurkat cells to THP-1 macrophages and antiband 3 IgG through sialylated poly-N-acetyllactosaminyl sugar chains

Human T-lymphoid cell line Jurkat cells were mildly oxidized with diamide, hydrogen peroxide, or t-butyl-hydroperoxide. The recognition of Jurkat cells in the absence of serum by human monocytic leukemia cell line THP-1 differentiated into macrophages was enhanced by the oxidation with these reagents. The recognition was maximal when Jurkat cells were treated with each of the reagents at the relatively low concentrations, and the recognition was decreased on treatment with the reagents at the higher concentrations. The enhanced recognition of THP-1 macrophages to diamide-oxidized Jurkat cells was lowered when the binding was conducted in the presence of the oligosaccharides from band 3 glycoprotein and lactoferrin. The inhibitory effect of band 3 oligosaccharides was abolished by removal of the non-reducing-terminal sialyl residues or by cleavage of poly-N-acetyllactosaminyl sugar chains in the saccharides. Moreover, on enzymatic removal of the non-reducing-terminal sialyl residues or enzymatic cleavage of the poly-N-acetyllactosaminyl sugar chains on the surface of Jurkat cells prior to oxidation, the cells were recognized poorly by THP-1 macrophages. Human naturally occuring antiband 3 IgG bound effectively to the hydrogen peroxide-oxidized Jurkat cells. This binding was abolished by the enzymatic cleavage of the poly-N-acetyllactosaminyl sugar chains on the surface of the cells prior to oxidation with hydrogen peroxide. The results indicate that binding of THP-1 macrophages and antiband 3 IgG to Jurkat cells was increased by mild oxidation of Jurkat cells, and the bindings were through sialylated poly-N-acetyllactosaminyl sugar chains on Jurkat cell surface.