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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1992-12-22
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pubmed:abstractText |
The detailed substrate specificity of the UDP-GalNAc:sialylparagloboside N-acetylgalactosaminyltransferase to form the Sd(a+) blood group active carbohydrate determinant GalNAc beta 1-4(NeuAc alpha 2-3)Gal was studied using a membrane fraction prepared from human gastric fundic mucosa. Various sialosylated oligosaccharides and gangliosides were examined as acceptor substrates. Oligosaccharide substrates were fluorescence-labelled with 2-aminopyridine, and the transferase activity was quantified by h.p.l.c. using a reversed-phase column. The structures of the products were determined by glycosidase degradation and proton n.m.r. 3'-Sialyl-lactose (II3NeuAcLac), 3'-sialyl-lactotetraose (IV3NeuAcLc4), and 3'-sialyl-lactoneotetraose (IV3NeuAcnLc4) were good substrates for the beta 1-4GalNAc transferase in gastric fundic mucosa, but 6'-sialyl-lactoneotetraose (IV6NeuAcnLc4) or 6'-sialyl-lactose (II6NeuAcLac) were not. Gangliosides with a terminal NeuAc alpha 2-3Gal residue such as GM3, sialylparagloboside, GM1b and GD1a were also studied. The activity of beta 1-4GalNAc transfer to sialylparagloboside was much higher than that to GM2, GM1b or GD1a in spite of them having the same terminal residue. Measurement of the activity of the beta 1-4GalNAc transferase in biopsy specimens demonstrated that the activity was localized in gastric fundic mucosa and was absent in pyloric mucosa, intestinal metaplasia and gastric cancer tissue. Thus the beta 1-4GalNAc transferase present specifically in fundic mucosa required a NeuAc alpha 2-3Gal residue connected to either type-1-chain or type-2-chain oligosaccharides. In glycolipids, the acceptor specificity was restricted to NeuAc alpha 2-3Gal beta 1-4GlcNAc because the NeuAc alpha 2-3Gal beta 1-3GalNAc structure in ganglio-series glycolipids was not a good acceptor substrate.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-14066623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-1748676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-2139874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-2167157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-2425965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-2450092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-2479468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-2510926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-2513740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-2533651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-3044991,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-3106337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-3119392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-3140234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-3167001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-4684701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-5503169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-6706908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1445260-7451432
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
288 ( Pt 1)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
161-5
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1445260-Aminopyridines,
pubmed-meshheading:1445260-Carbohydrate Sequence,
pubmed-meshheading:1445260-Chromatography, High Pressure Liquid,
pubmed-meshheading:1445260-Fluorescent Dyes,
pubmed-meshheading:1445260-Gangliosides,
pubmed-meshheading:1445260-Gastric Fundus,
pubmed-meshheading:1445260-Gastric Mucosa,
pubmed-meshheading:1445260-Glycoside Hydrolases,
pubmed-meshheading:1445260-Humans,
pubmed-meshheading:1445260-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1445260-Molecular Sequence Data,
pubmed-meshheading:1445260-N-Acetylgalactosaminyltransferases,
pubmed-meshheading:1445260-Oligosaccharides,
pubmed-meshheading:1445260-Substrate Specificity,
pubmed-meshheading:1445260-Tissue Distribution
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pubmed:year |
1992
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pubmed:articleTitle |
Substrate specificity and distribution of UDP-GalNAc:sialylparagloboside N-acetylgalactosaminyltransferase in the human stomach.
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pubmed:affiliation |
Division of Clinical Biochemistry, National Medical Center, Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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