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J. Biol. Chem., Vol. 269, Issue 6, 4473-4479, 02, 1994
MF Bierhuizen, K Maemura and M Fukuda
Chinese hamster ovary (CHO) cells do not contain detectable amounts of core
2 beta-1,6-N-acetylglucosaminyltransferase, C2GnT, and thus lack various
modifications in their branched O-linked oligosaccharides. In the present
study, the O-linked oligosaccharides and the occurrence of a
differentiation antigen were analyzed in CHO cells stably transfected with
cDNA encoding human leukosialin alone (CHO-leu) or with cDNAs encoding both
leukosialin and C2GnT (CHO-leu.C2GnT). The analysis of O- glycans, released
from [3H]glucosamine-labeled cells, revealed that CHO- leu cells synthesize
O-glycans with a Gal beta 1-->3GalNAc backbone, whereas CHO-leu.C2GnT
cells synthesize in addition O-glycans with a Gal beta 1-->3(Gal beta
1-->4GlcNAc beta 1-->6)GalNAc backbone. Moreover, CHO-leu.C2GnT cells
express poly-N-acetyllactosaminyl extensions from the GlcNAc beta 1-->6
branch in O-glycans, while CHO-leu cells express no detectable amount of
poly-N-acetyllactosaminyl O-glycans. It was also demonstrated that
leukosialin in CHO-leu.C2GnT cells is recognized by the T305 monoclonal
antibody, while the same antibody did not react at all with CHO-leu cells.
In addition, the transient expression cloning scheme using the T305
monoclonal antibody as a selectin marker and COS-1 cells, which
endogenously express C2GnT as recipient cells, resulted in the isolation of
cDNA encoding leukosialin. These results indicate that C2GnT determines the
expression of poly-N- acetyllactosamines in O-glycans and together with
leukosialin, an onco- differentiation antigen recognized by the T305
antibody.
Expression of a differentiation antigen and poly-N-acetyllactosaminyl O- glycans directed by a cloned core 2 beta-1,6-N- acetylglucosaminyltransferase
Glycobiology Program, La Jolla Cancer Research Foundation, California 92037.
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