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J. Biol. Chem., Vol. 275, Issue 31, 23456-23461, August 4, 2000

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Control of Bisecting GlcNAc Addition to N-Linked Sugar Chains^*

Kazuhiro Fukuta, Reiko Abe, Tomoko Yokomatsu, Fumio Omae, Mineko Asanagi, and Tadashi Makino

From the Life Science Laboratory, Mitsui Chemicals, Inc., 1144 Togo, Mobara, Chiba 297-0017, Japan

In the present study, experimental control of the formation of bisecting GlcNAc was investigated, and the competition between -1,4-GalT (UDP-galactose:N-acetylglucosamine -1,4-galactosyltransferase) and GnT-III (UDP-N-acetylglucosamine:-D-mannoside -1,4-N-acetylglucosaminyltransferase) was examined. We isolated a -1,4-GalT-I single knockout human B cell clone producing monoclonal IgM and several transfectant clones that overexpressed -1,4-GalT-I or GnT-III. In the -1,4-GalT-I-single knockout cells, the extent of bisecting GlcNAc addition to the sugar chains of IgM was increased, where -1,4-GalT activity was reduced to about half that in the parental cells, and GnT-III activity was unaltered. In the -1,4-GalT-I transfectants, the extent of bisecting GlcNAc addition was reduced although GnT-III activity was not altered significantly. In the GnT-III transfectants, the extent of bisecting GlcNAc addition increased along with the increase in levels of GnT-III activity. The extent of bisecting GlcNAc addition to the sugar chains of IgM was significantly correlated with the level of intracellular -1,4-GalT activity relative to that of GnT-III. These results were interpreted as indicating that -1,4-GalT competes with GnT-III for substrate in the cells.

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