Source:http://linkedlifedata.com/resource/pubmed/id/12438318
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
|
| pubmed:dateCreated |
2003-2-17
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| pubmed:abstractText |
The hinge region of human immunoglobulin A1 (*IgA1) possesses multiple O-glycans, of which synthesis is initiated by the addition of GalNAc to serine or threonine through the activity of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases (pp-GalNAc-Ts). We found that six pp-GalNAc-Ts, pp-GalNAc-T1, -T2, -T3, -T4, -T6, and -T9, were expressed in B cells, IgA-bearing B cells, and NCI-H929 IgA myeloma cells. pp-GalNAc-T activities of these six enzymes for a synthetic IgA hinge peptide, which has nine possible O-glycosylation sites, were examined using a reversed phase-high performance liquid chromatography, a matrix-assisted laser desorption ionization time of flight mass spectrometry, and peptide sequencing analysis. pp-GalNAc-T2 showed the strongest activity transferring GalNAc to a maximum of eight positions. Other pp-GalNAc-Ts exhibited different substrate specificities from pp-GalNAc-T2; however, their activities were extremely weak. It was reported that the IgA1 hinge region possesses a maximum of five O-glycans, and their amino acid positions have been determined. We found that pp-GalNAc-T2 selectively transferred GalNAc residues to the same five positions. These results strongly suggested that pp-GalNAc-T2 is an essential enzyme for initiation of O-linked glycosylation of the IgA1 hinge region.
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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/Immunoglobulin A,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylgalactosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine Diphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/polypeptide...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
|
| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
21
|
| pubmed:volume |
278
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
5613-21
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12438318-Amino Acid Sequence,
pubmed-meshheading:12438318-B-Lymphocytes,
pubmed-meshheading:12438318-Base Sequence,
pubmed-meshheading:12438318-Cell Line,
pubmed-meshheading:12438318-Humans,
pubmed-meshheading:12438318-Immunoglobulin A,
pubmed-meshheading:12438318-Kinetics,
pubmed-meshheading:12438318-Lymphocytes,
pubmed-meshheading:12438318-Molecular Sequence Data,
pubmed-meshheading:12438318-Multiple Myeloma,
pubmed-meshheading:12438318-N-Acetylgalactosaminyltransferases,
pubmed-meshheading:12438318-Polysaccharides,
pubmed-meshheading:12438318-Reference Values,
pubmed-meshheading:12438318-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12438318-Substrate Specificity,
pubmed-meshheading:12438318-Transcription, Genetic,
pubmed-meshheading:12438318-Tumor Cells, Cultured,
pubmed-meshheading:12438318-Uridine Diphosphate N-Acetylgalactosamine
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| pubmed:year |
2003
|
| pubmed:articleTitle |
Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2.
|
| pubmed:affiliation |
Glycogene Function Team, Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Open Space Laboratory C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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