pubmed-article:20938724 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20938724 | lifeskim:mentions | umls-concept:C0229671 | lld:lifeskim |
pubmed-article:20938724 | lifeskim:mentions | umls-concept:C0007570 | lld:lifeskim |
pubmed-article:20938724 | lifeskim:mentions | umls-concept:C0020840 | lld:lifeskim |
pubmed-article:20938724 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:20938724 | pubmed:dateCreated | 2011-3-28 | lld:pubmed |
pubmed-article:20938724 | pubmed:abstractText | In celiac disease, gluten ingestion provokes small-bowel mucosal injury and production of IgA autoantibodies against transglutaminase 2 (TG2). It has been suggested that in celiac patients IgA could mediate the transepithelial passage of gluten peptides in a mechanism involving the transferrin receptor. As IgA1 with galactose-deficient O-linked glycans has elevated affinity for the transferrin receptor, we assessed whether total serum IgA1 and IgA1 anti-TG2 autoantibodies in celiac patients are aberrantly glycosylated. We report that males with celiac disease have higher total serum levels of galactose-deficient IgA1 than non-celiac males. Furthermore, O-glycans of the disease-specific TG2 IgA1 autoantibodies in celiac patients exhibited elevated galactose deficiency. A gluten-free diet had no effect on the total serum levels of galactose-deficient IgA1, whereas the amount of galactose-deficient anti-TG2 IgA1 decreased. Thus, the undergalactosylated IgA1 molecules are not pathognomonic for celiac disease, but galactose deficiency in IgA1 could be an aggravating factor. | lld:pubmed |
pubmed-article:20938724 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:language | eng | lld:pubmed |
pubmed-article:20938724 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20938724 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20938724 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20938724 | pubmed:month | Feb | lld:pubmed |
pubmed-article:20938724 | pubmed:issn | 1573-2592 | lld:pubmed |
pubmed-article:20938724 | pubmed:author | pubmed-author:MäkiMarkkuM | lld:pubmed |
pubmed-article:20938724 | pubmed:author | pubmed-author:NovakJanJ | lld:pubmed |
pubmed-article:20938724 | pubmed:author | pubmed-author:SuzukiHitoshi... | lld:pubmed |
pubmed-article:20938724 | pubmed:author | pubmed-author:KaukinenKatri... | lld:pubmed |
pubmed-article:20938724 | pubmed:author | pubmed-author:CollinPekkaP | lld:pubmed |
pubmed-article:20938724 | pubmed:author | pubmed-author:LindforsKatri... | lld:pubmed |
pubmed-article:20938724 | pubmed:author | pubmed-author:SaavalainenPä... | lld:pubmed |
pubmed-article:20938724 | pubmed:author | pubmed-author:KoskinenLotta... | lld:pubmed |
pubmed-article:20938724 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20938724 | pubmed:volume | 31 | lld:pubmed |
pubmed-article:20938724 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20938724 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20938724 | pubmed:pagination | 74-9 | lld:pubmed |
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pubmed-article:20938724 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:20938724 | pubmed:articleTitle | Galactosylation of serum IgA1 O-glycans in celiac disease. | lld:pubmed |
pubmed-article:20938724 | pubmed:affiliation | Pediatric Research Center, University of Tampere and Tampere University Hospital, Finn-Medi 3, FIN-33014 Tampere, Finland. katri.lindfors@uta.fi | lld:pubmed |
pubmed-article:20938724 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20938724 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:20938724 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |