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rdf:type |
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lifeskim:mentions |
umls-concept:C0017982,
umls-concept:C0020792,
umls-concept:C0021311,
umls-concept:C0021832,
umls-concept:C0026682,
umls-concept:C0028959,
umls-concept:C0034693,
umls-concept:C0034721,
umls-concept:C0205374,
umls-concept:C0321331,
umls-concept:C1515926
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pubmed:dateCreated |
2001-1-2
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pubmed:abstractText |
The sialylation of the oligosaccharides from small-intestinal mucins during a 13-day infectious cycle was studied in Sprague-Dawley rats with the parasite Nippostrongylus brasiliensis. Sialic acid analysis and release, permethylation and analysis by GC-MS of the sialylated oligosaccharides isolated from the 'insoluble' mucin complex revealed a relative decrease (4-7-fold) of N-glycolylneuraminic acid compared with N-acetylneuraminic acid just before parasite expulsion. Northern blots showed that this effect was due to the decreased expression of a hydroxylase converting CMP-N-acetylneuraminic acid into CMP-N-glycolylneuraminic acid. Analysis of other rat strains showed that this parasite infection also caused the same effect in these animals. Detailed analysis of infected Sprague-Dawley rats revealed four sialylated oligosaccharides not found in the uninfected animals. These new oligosaccharides were characterized in detail and all shown to contain the trisaccharide epitope NeuAc/NeuGcalpha2-3(GalNAcbeta1-4)Galbeta1 (where NeuGc is N-glycolyl neuraminic acid). This epitope is similar to the Sd(a)- and Cad-type blood-group antigens and suggests that the infection causes the induction of a GalNAcbeta1-4 glycosyltransferase. This model for an intestinal infection suggests that the glycosylation of intestinal mucins is a dynamic process being modulated by the expression of specific enzymes during an infection process.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-10336486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-10406840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-1527047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-1576207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-1601877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-1697589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-1718981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-2459930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-2604041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-2673013,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-3106337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-3142362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-4735853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-6190803,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-6341324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-7502939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-7515051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-7608218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-7733455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-7778880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-7795415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-7980468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8206520,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8300571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8360170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8473019,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8645144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8703071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8748154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8785483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8909996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-8910009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-9341141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-9363937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-9603957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10970796-9668062
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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 |
Sep
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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 |
350 Pt 3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
805-14
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:10970796-Animals,
pubmed-meshheading:10970796-Carbohydrate Sequence,
pubmed-meshheading:10970796-Gas Chromatography-Mass Spectrometry,
pubmed-meshheading:10970796-Glycosylation,
pubmed-meshheading:10970796-Mixed Function Oxygenases,
pubmed-meshheading:10970796-Molecular Sequence Data,
pubmed-meshheading:10970796-Mucin-2,
pubmed-meshheading:10970796-Mucins,
pubmed-meshheading:10970796-N-Acetylneuraminic Acid,
pubmed-meshheading:10970796-Nippostrongylus,
pubmed-meshheading:10970796-Oligosaccharides,
pubmed-meshheading:10970796-Rats,
pubmed-meshheading:10970796-Rats, Sprague-Dawley,
pubmed-meshheading:10970796-Strongylida Infections
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pubmed:year |
2000
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pubmed:articleTitle |
Identification of transient glycosylation alterations of sialylated mucin oligosaccharides during infection by the rat intestinal parasite Nippostrongylus brasiliensis.
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pubmed:affiliation |
Department of Medical Biochemistry, Göteborg University, P.O. Box 440, SE 405 30 Gothenburg, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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