Development of distinct clonal patterns of carbohydrate-binding activity in human promyelocytic HL 60 cells and histiocytic U 937 cells during DMSO-or PMA-induced differentiation

Increased ability to recognize carbohydrate structures on particles was observed in promyelocytic HL 60 cells and histiocytic U 937 cells during differentiation inducedin vitro with dimethylsulfoxide (DMSO) or phorbol myristate acetate (PMA). The size of the cells and increased capacity to bind and ingest IgG-or complement-coated yeast particles were used as indicators of phagocytic maturation. Carbohydrate affinities were assessed by the binding of glycolipid-containing liposomes displaying mannose, galactose, lactose,N-acetylgalactosamine, fucose, inositol, or ganglioside residues. With DMSO, HL 60 cells showed greater affinity for mannose and ganglioside residues, and with PMA also for fucosyl ligands. U 937 cells displayed a slightly different pattern; mannose binding was present before induction and by DMSO affinity was clearly augmented for galactose, fucose, ganglioside and inositol residues. With PMA these effects were smaller except for increased binding of lactosyl liposomes.Subclones of cells derived from U 937 (Cl 1, Cl 2 and Cl 3) appeared more mature already in the absence of inducing agent, and the lectin activity was barely affected by DMSO or PMA. Incidentally, Cl 1 lacked mannose affinity, which was fully expressed in Cl 2. With respect to inositol and ganglioside residues the reverse pattern was observed.In conclusion, DMSO- or PMA-mediated maturation in HL 60 and U 937 cells is accompanied by increased carbohydrate binding similar to what has been found in mature macrophages and granulocytes, indicating that these cellular systems can be used for further assessment of the molecular origin of lectin-like membrane components in phagocytic cells.