Source:http://linkedlifedata.com/resource/pubmed/id/14623122
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2003-11-18
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| pubmed:abstractText |
UDP-N-acetylglucosamine:alpha(1,6)-D-mannoside beta(1,6)-N-acetylglucosaminyltransferase (GnT-V, Mgat5) functions in the biosynthesis of N-linked glycans and is transcriptionally upregulated by oncogene signaling. We report here the cloning and characterization of a human cDNA encoding a distinct enzyme with related substrate specificity, termed GnT-VB, which is predicted to have 53% similarity to the original amino acid sequence of GnT-V(A). Transient expression of GnT-VB cDNA in COS7 cells yielded significant increases of activity toward GnT-VA acceptors, including synthetic saccharides and N-linked glycopeptides, with some differences in specificity. Unlike GnT-VA, GnT-VB required divalent cation for full activity. EST databases showed expression of a 6 bp (+) splice isoform of GnT-VB; when expressed, this enzyme showed significantly reduced activity. CHO Lec4 cells, which do not express GnT-VA or B activity, lack synthesis of the N-linked beta(1,6) branch, and do not bind L-phytohemagglutinin (L-PHA), were transfected with GnT-VB or GnT-VA; both then bound significant amounts of L-PHA, demonstrating that both enzymes synthesized N-linked beta(1,6) branched glycans in vivo. Real-time polymerase chain reaction results showed that GnT-VB mRNA was highly expressed in brain and testis, with lesser levels in other tissues, while human GnT-VA showed a more general expression, but with low levels in brain and no expression in skeletal muscle.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-1,6-mannosylglycoprotein...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0014-5793
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
20
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| pubmed:volume |
554
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
515-9
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:14623122-Alternative Splicing,
pubmed-meshheading:14623122-Amino Acid Sequence,
pubmed-meshheading:14623122-Animals,
pubmed-meshheading:14623122-CHO Cells,
pubmed-meshheading:14623122-COS Cells,
pubmed-meshheading:14623122-Cloning, Molecular,
pubmed-meshheading:14623122-Cricetinae,
pubmed-meshheading:14623122-DNA, Complementary,
pubmed-meshheading:14623122-Humans,
pubmed-meshheading:14623122-Isoenzymes,
pubmed-meshheading:14623122-Molecular Sequence Data,
pubmed-meshheading:14623122-N-Acetylglucosaminyltransferases,
pubmed-meshheading:14623122-Oligosaccharides,
pubmed-meshheading:14623122-Organ Specificity,
pubmed-meshheading:14623122-Recombinant Proteins,
pubmed-meshheading:14623122-Sequence Alignment,
pubmed-meshheading:14623122-Sequence Homology, Amino Acid,
pubmed-meshheading:14623122-Substrate Specificity,
pubmed-meshheading:14623122-Transfection
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| pubmed:year |
2003
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| pubmed:articleTitle |
A novel beta(1,6)-N-acetylglucosaminyltransferase V (GnT-VB)(1).
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| pubmed:affiliation |
Complex Carbohydrate Research Center and Department of Biochemistry and Molecular Biology, University of Georgia, 30605, Athens, GA, USA
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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