Document Detail


Biosynthesis of HNK-1 glycans on O-linked oligosaccharides attached to the neural cell adhesion molecule (NCAM): the requirement for core 2 beta 1,6-N-acetylglucosaminyltransferase and the muscle-specific domain in NCAM.
MedLine Citation:
PMID:  11891229     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The HNK-1 glycan, sulfo-->3GlcAbeta1-->3Galbeta1-->4GlcNAcbeta1-->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 beta1,3-linked GlcA to N-acetyllactosamine followed by sulfation of the C-3 position of GlcA. The cDNAs encoding beta1,3-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 beta1,6-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-->3GlcAbeta1-->3Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->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.
Authors:
Edgar Ong; Misa Suzuki; Frederic Belot; Jiunn-Chern Yeh; Isabelle Franceschini; Kiyohiko Angata; Ole Hindsgaul; Minoru Fukuda
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.     Date:  2002-03-12
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  277     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2002 May 
Date Detail:
Created Date:  2002-05-13     Completed Date:  2002-07-16     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  18182-90     Citation Subset:  IM    
Affiliation:
Glycobiology Program, Cancer Research Center, The Burnham Institute, La Jolla, California 92037, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Antigens, CD57 / biosynthesis*
Binding Sites
Blotting, Western
Brain Chemistry
Carbohydrate Sequence
Chromatography, Ion Exchange
Heart / embryology
Mice
Models, Chemical
Molecular Sequence Data
Mucins / metabolism
Muscles / metabolism*
Myocardium / metabolism
N-Acetylglucosaminyltransferases / metabolism*
Neural Cell Adhesion Molecules / metabolism*
Oligosaccharides / metabolism*
Grant Support
ID/Acronym/Agency:
P01CA71932/CA/NCI NIH HHS; R01CA33895/CA/NCI NIH HHS; R37CA33000/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Antigens, CD57; 0/Mucins; 0/Neural Cell Adhesion Molecules; 0/Oligosaccharides; EC 2.4.1.-/N-Acetylglucosaminyltransferases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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