Galactosylation of Serum IgA1 O-Glycans in Celiac Disease |
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| Authors: | Katri Lindfors Hitoshi Suzuki Jan Novak Pekka Collin Päivi Saavalainen Lotta L. E. Koskinen Markku Mäki Katri Kaukinen |
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| Affiliation: | (1) Pediatric Research Center, University of Tampere and Tampere University Hospital, Finn-Medi 3, FIN-33014 Tampere, Finland;(2) Department of Microbiology, University of Alabama at Birmingham, Alabama, USA;(3) Department of Nephrology, Juntendo University Faculty of Medicine, Tokyo, Japan;(4) Department of Gastroenterology and Alimentary Tract Surgery, Tampere University Hospital, Tampere, Finland;(5) Department of Medical Genetics and Research Program for Molecular Medicine, Biomedicum Helsinki, University of Helsinki, Helsinki, Finland;(6) Medical School, University of Tampere, Finn-Medi 3, 33014 Tampere, Finland |
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| Abstract: | ![]()
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. |
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