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J Biol Chem, Vol. 275, Issue 15, 11106-11113, April 14, 2000
From the Core 2 O-glycan branching catalyzed
by UDP-N-acetyl- The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF132035.
Control of O-Glycan Branch Formation
MOLECULAR CLONING AND CHARACTERIZATION OF A NOVEL
THYMUS-ASSOCIATED CORE 2 
1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE*
§,
,,
School of Dentistry, University of
Copenhagen, Nørre Allé 20, 2200 Copenhagen N, Denmark,
the ¶ Glycobiology Program, Cancer Research Center, The Burnham
Institute, La Jolla, California 92037, the University of
Georgia, Complex Carbohydrate Research Center, Athens, Georgia 30602, and the ** Department of Human Genetics, University Hospital
Nijmegen, 6500 HB Nijmegen, The Netherlands
-D-glucosamine: acceptor
1,6-N-acetylglucosaminyltransferases
(6GlcNAc-Ts) is an important step in mucin-type biosynthesis. Core 2 complex-type O-glycans are involved in selectin-mediated
adhesion events, and O-glycan branching appears to be
highly regulated. Two homologous 6GlcNAc-Ts functioning in
O-glycan branching have previously been characterized, and
here we report a third homologous 6GlcNAc-T designated C2GnT3.
C2GnT3 was identified by BLAST analysis of human genome survey
sequences. The catalytic activity of C2GnT3 was evaluated by in
vitro analysis of a secreted form of the protein expressed in
insect cells. The results revealed exclusive core 2 6GlcNAc-T
activity. The product formed with core 1-para-nitrophenyl was confirmed by 1H NMR to be core
2-para-nitrophenyl. In vivo analysis of the
function of C2GnT3 by coexpression of leukosialin (CD43) and a full
coding construct of C2GnT3 in Chinese hamster ovary cells confirmed the core 2 activity and failed to reveal I activity. The C2GnT3
gene was located to 5q12, and the coding region was contained in a single exon. Northern analysis revealed selectively high levels of a
5.5-kilobase C2GnT3 transcript in thymus with only low levels in other
organs. The unique expression pattern of C2GnT3 suggests that this
enzyme serves a specific function different from other members of the
6GlcNAc-T gene family.
*
This work was supported by The Danish Cancer Society, the
Velux Foundation, the Danish Medical Research Council, funds from the
EU Biotech 4th Framework, and National Institutes of Health Resource
Center for Biomedical Complex Carbohydrates Grant 5 P41 RR05351.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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