Source:http://linkedlifedata.com/resource/pubmed/id/10358066
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
24
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| pubmed:dateCreated |
1999-7-6
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| pubmed:databankReference | |
| pubmed:abstractText |
We isolated a cDNA encoding a novel glucuronyltransferase, designated GlcAT-D, involved in the biosynthesis of the HNK-1 carbohydrate epitope from rat embryo cDNA by the degenerate polymerase chain reaction method. The new cDNA sequence revealed an open reading frame coding for a protein of 324 amino acids with type II transmembrane protein topology. The amino acid sequence of GlcAT-D displayed 50.0% identity to rat GlcAT-P, which is involved in the biosynthesis of the HNK-1 epitope on glycoproteins. Expression of GlcAT-D in COS-7 cells resulted in the formation of the HNK-1 epitope on the cell surface. The enzyme expressed in COS-7 cells transferred a glucuronic acid (GlcA) not only to asialo-orosomucoid, a glycoprotein bearing terminal N-acetyllactosamine structure, but also to paragloboside (lacto-N-neotetraosylceramide), a precursor of the HNK-1 epitope on glycolipids. Furthermore, substrate specificity analysis using a soluble chimeric form of GlcAT-D revealed that GlcAT-D transfers a GlcA not only to Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine++ + but also to Galbeta1-3GlcNAcbeta1-3Galbeta1-4Glc-pyridylamine++ +. Enzymatic hydrolysis and Smith degradation of the reaction product indicated that GlcAT-D transfers a GlcA through a beta1,3-linkage to a terminal galactose. The GlcAT-D transcripts were detected in embryonic, postnatal, and adult rat brain. In situ hybridization analysis revealed that the expression pattern of GlcAT-D transcript in embryo is similar to that of GlcAT-P, but distinct expression of GlcAT-D was observed in the embryonic pallidum and retina. Regions that expressed GlcAT-D and/or GlcAT-P were always HNK-1-positive, indicating that both GlcATs are involved in the synthesis of the HNK-1 epitope in vivo.
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| pubmed:commentsCorrections | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD57,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Globosides,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronates,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronosyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/galactosylgalactoylxylosylprotein...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
11
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| pubmed:volume |
274
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
17115-22
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10358066-Amino Acid Sequence,
pubmed-meshheading:10358066-Animals,
pubmed-meshheading:10358066-Antigens, CD57,
pubmed-meshheading:10358066-Base Sequence,
pubmed-meshheading:10358066-Brain,
pubmed-meshheading:10358066-DNA, Complementary,
pubmed-meshheading:10358066-Epitopes,
pubmed-meshheading:10358066-Globosides,
pubmed-meshheading:10358066-Glucuronates,
pubmed-meshheading:10358066-Glucuronic Acid,
pubmed-meshheading:10358066-Glucuronosyltransferase,
pubmed-meshheading:10358066-Glycoproteins,
pubmed-meshheading:10358066-Membrane Proteins,
pubmed-meshheading:10358066-Molecular Sequence Data,
pubmed-meshheading:10358066-Multigene Family,
pubmed-meshheading:10358066-Oligosaccharides,
pubmed-meshheading:10358066-Protein Conformation,
pubmed-meshheading:10358066-Rats,
pubmed-meshheading:10358066-Recombinant Proteins,
pubmed-meshheading:10358066-Sequence Homology, Amino Acid,
pubmed-meshheading:10358066-Species Specificity,
pubmed-meshheading:10358066-Substrate Specificity,
pubmed-meshheading:10358066-Tissue Distribution
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| pubmed:year |
1999
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| pubmed:articleTitle |
Cloning and expression of a novel galactoside beta1, 3-glucuronyltransferase involved in the biosynthesis of HNK-1 epitope.
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| pubmed:affiliation |
Department of Biochemical Cell Research, Tokyo Metropolitan Institute of Medical Science (RINSHOKEN), Tokyo 113-8613, Japan.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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