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Originally published In Press as doi:10.1074/jbc.M201312200 on March 12, 2002
J. Biol. Chem., Vol. 277, Issue 20, 18182-18190, May 17, 2002
Biosynthesis of HNK-1 Glycans on O-Linked
Oligosaccharides Attached to the Neural Cell Adhesion Molecule
(NCAM)
THE REQUIREMENT FOR CORE 2 1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE AND THE
MUSCLE-SPECIFIC DOMAIN IN NCAM*
Edgar
Ong ,
Misa
Suzuki,
Frederic
Belot§,
Jiunn-Chern
Yeh¶,
Isabelle
Franceschini ,
Kiyohiko
Angata,
Ole
Hindsgaul, and
Minoru
Fukuda**
From the Glycobiology Program, Cancer Research Center, The Burnham
Institute, La Jolla, California 92037
The HNK-1 glycan,
sulfo 3GlcA 1 3Gal 1 4GlcNAc 1 R, is highly expressed
in neuronal cells and apparently plays critical roles in neuronal cell
migration and axonal extension. The HNK-1 glycan synthesis is initiated
by the addition of 1,3-linked GlcA to N-acetyllactosamine followed by sulfation of the C-3
position of GlcA. The cDNAs encoding 1,3-glucuronyltransferase
(GlcAT-P) and HNK-1 sulfotransferase (HNK-1ST) have been recently
cloned. Among various adhesion molecules, the neural cell adhesion
molecule (NCAM) was shown to contain HNK-1 glycan on
N-glycans. In the present study, we first demonstrated that
NCAM also bears HNK-1 glycan attached to O-glycans when
NCAM contains the O-glycan attachment scaffold,
muscle-specific domain, and is synthesized in the presence of core 2 1,6-N-acetylglucosaminyltransferase, GlcAT-P,
and HNK-1ST. Structural analysis of the HNK-1 glycan revealed that the
HNK-1 glycan is attached on core 2 branched O-glycans,
sulfo 3GlcA 1 3Gal 1 4GlcNAc 1 6(Gal 1 3)GalNAc. Using synthetic oligosaccharides as acceptors, we found that GlcAT-P and HNK-1ST almost equally act on oligosaccharides, mimicking N- and O-glycans. By contrast, HNK-1 glycan was
much more efficiently added to N-glycans than
O-glycans when NCAM was used as an acceptor. These results
are consistent with our results showing that HNK-1 glycan is minimally
attached to O-glycans of NCAM in fetal brain, heart, and
the myoblast cell line, C2C12. These results combined together
indicate that HNK-1 glycan can be synthesized on core 2 branched
O-glycans but that the HNK-1 glycan is preferentially added
on N-glycans over O-glycans of NCAM, probably
because N-glycans are extended further than
O-glycans attached to NCAM containing the muscle-specific domain.
*
This work was supported by NCI, National Institutes of
Health, Grants R37CA33000, RO1CA33895, and PO1CA71932.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.
Present address: Corvas International Inc., San Diego, CA 92121.
§
Present address: Unite de Chimie Organique, Institute Pasteur,
75724 Paris cedex 15, France.
¶
Present address: Genset Corp., San Diego, CA 92121.
Present address: Deptartment of Neuroscience, Institute
Pasteur, 75724 Paris cedex 15, France.
**
To whom correspondence should be addressed: The Burnham Institute,
10901 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-646-3144; Fax:
858-646-3193; E-mail: minoru@burnham.org.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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