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.
Nakao
H
H
Second Department of Internal Medicine, Osaka University Medical School, Japan.
Nishikawa
A
A
Karasuno
T
T
Nishiura
T
T
Iida
M
M
Kanayama
Y
Y
Yonezawa
T
T
Tarui
S
S
Taniguchi
N
N
D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002471:Cell Transformation, Neoplastic; D005453:Fluorescence; D005964:Glucosyltransferases / Q000378:metabolism*; D006801:Humans; D015850:Interleukin-6 / Q000494:pharmacology*; D009101:Multiple Myeloma / Q000201:enzymology*; D017351:N-Acetylglucosaminyltransferases; D009844:Oligosaccharides / Q000737:chemistry*; D014407:Tumor Cells, Cultured
D015850:Interleukin-6; D009844:Oligosaccharides; D005964:Glucosyltransferases; D017351:N-Acetylglucosaminyltransferases; C054599:beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase; C052254:alpha-1,6-mannosylglycoprotein beta 1,6-N-acetylglucosaminyltransferase