Source:http://linkedlifedata.com/resource/pubmed/id/11891229
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
|
pubmed:dateCreated |
2002-5-13
|
pubmed:abstractText |
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.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD57,
http://linkedlifedata.com/resource/pubmed/chemical/Mucins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Neural Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
17
|
pubmed:volume |
277
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
18182-90
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:11891229-Animals,
pubmed-meshheading:11891229-Antigens, CD57,
pubmed-meshheading:11891229-Binding Sites,
pubmed-meshheading:11891229-Blotting, Western,
pubmed-meshheading:11891229-Brain Chemistry,
pubmed-meshheading:11891229-Carbohydrate Sequence,
pubmed-meshheading:11891229-Chromatography, Ion Exchange,
pubmed-meshheading:11891229-Heart,
pubmed-meshheading:11891229-Mice,
pubmed-meshheading:11891229-Models, Chemical,
pubmed-meshheading:11891229-Molecular Sequence Data,
pubmed-meshheading:11891229-Mucins,
pubmed-meshheading:11891229-Muscles,
pubmed-meshheading:11891229-Myocardium,
pubmed-meshheading:11891229-N-Acetylglucosaminyltransferases,
pubmed-meshheading:11891229-Neural Cell Adhesion Molecules,
pubmed-meshheading:11891229-Oligosaccharides
|
pubmed:year |
2002
|
pubmed:articleTitle |
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.
|
pubmed:affiliation |
Glycobiology Program, Cancer Research Center, The Burnham Institute, La Jolla, California 92037, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|