Source:http://linkedlifedata.com/resource/pubmed/id/10816579
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
31
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pubmed:dateCreated |
2000-9-7
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pubmed:abstractText |
In the present study, experimental control of the formation of bisecting GlcNAc was investigated, and the competition between beta-1,4-GalT (UDP-galactose:N-acetylglucosamine beta-1, 4-galactosyltransferase) and GnT-III (UDP-N-acetylglucosamine:beta-d-mannoside beta-1, 4-N-acetylglucosaminyltransferase) was examined. We isolated a beta-1,4-GalT-I single knockout human B cell clone producing monoclonal IgM and several transfectant clones that overexpressed beta-1,4-GalT-I or GnT-III. In the beta-1,4-GalT-I-single knockout cells, the extent of bisecting GlcNAc addition to the sugar chains of IgM was increased, where beta-1,4-GalT activity was reduced to about half that in the parental cells, and GnT-III activity was unaltered. In the beta-1,4-GalT-I transfectants, the extent of bisecting GlcNAc addition was reduced although GnT-III activity was not altered significantly. In the GnT-III transfectants, the extent of bisecting GlcNAc addition increased along with the increase in levels of GnT-III activity. The extent of bisecting GlcNAc addition to the sugar chains of IgM was significantly correlated with the level of intracellular beta-1,4-GalT activity relative to that of GnT-III. These results were interpreted as indicating that beta-1, 4-GalT competes with GnT-III for substrate in the cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetyllactosamine Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/beta-1,4-mannosyl-glycoprotein...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23456-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10816579-Acetylglucosamine,
pubmed-meshheading:10816579-Antibodies, Monoclonal,
pubmed-meshheading:10816579-B-Lymphocytes,
pubmed-meshheading:10816579-Carbohydrate Sequence,
pubmed-meshheading:10816579-Clone Cells,
pubmed-meshheading:10816579-Glycosylation,
pubmed-meshheading:10816579-Humans,
pubmed-meshheading:10816579-Immunoglobulin M,
pubmed-meshheading:10816579-Molecular Sequence Data,
pubmed-meshheading:10816579-Mutation,
pubmed-meshheading:10816579-N-Acetylglucosaminyltransferases,
pubmed-meshheading:10816579-N-Acetyllactosamine Synthase,
pubmed-meshheading:10816579-Protein Processing, Post-Translational,
pubmed-meshheading:10816579-Transfection
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pubmed:year |
2000
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pubmed:articleTitle |
Control of bisecting GlcNAc addition to N-linked sugar chains.
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pubmed:affiliation |
Life Science Laboratory, Mitsui Chemicals, Inc., 1144 Togo, Mobara, Chiba 297-0017, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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