Modulation of N-acetylglucosaminyltransferase III, IV and V activities and alteration of the surface oligosaccharide structure of a myeloma cell line by interleukin 6.

The activity of N-acetylglucosaminyltransferase (GnT) III, IV and V on a myeloma cell line, OPM-1, was examined after incubation with interleukin 6 (IL-6). While augmenting cell proliferation, IL-6 resulted in a decrease of GnT III activity and an increase of GnT IV and V activities. Consistent with this, OPM-1 cultured with IL-6 showed an increased affinity to Datura stramonium lectin, which recognizes asialo-tri- and asialo-tetraantenary N-linked oligosaccharides. These results indicate that IL-6 modulates glycosyltransferase activity and the oligosaccharide structure of target cells.