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- W1965279497 endingPage "839" @default.
- W1965279497 startingPage "829" @default.
- W1965279497 abstract "Glycosylation abnormalities have been observed in autoimmune diseases and cancer. Here, we compare mechanisms of aberrant O-glycosylation, i.e., formation of Tn and sialyl-Tn structures, on MUC1 in breast cancer, and on IgA1 in an autoimmune disease, IgA nephropathy. The pathways of aberrant O-glycosylation, although different for MUC1 and IgA1, include dysregulation in glycosyltransferase expression, stability, and/or intracellular localization. Moreover, these aberrant glycoproteins are recognized by antibodies, although with different consequences. In breast cancer, elevated levels of antibodies recognizing aberrant MUC1 are associated with better outcome, whereas in IgA nephropathy, the antibodies recognizing aberrant IgA1 are part of the pathogenetic process." @default.
- W1965279497 created "2016-06-24" @default.
- W1965279497 creator A5031087263 @default.
- W1965279497 creator A5058714848 @default.
- W1965279497 creator A5070363000 @default.
- W1965279497 creator A5077607534 @default.
- W1965279497 date "2012-08-03" @default.
- W1965279497 modified "2023-10-18" @default.
- W1965279497 title "Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma" @default.
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