Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 70, Issue 5, Pages 829-839Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-012-1082-6
Keywords
IgA nephropathy; O-glycosylation; IgA; MUC1; Anti-glycan antibodies
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Funding
- National Institutes of Health [DK082753, DK078244, DK083663, DK075868, DK077279, GM098539]
- IGA Nephropathy Foundation of America
- Ministry of School, Youth, and Sport [LH11046]
- Czech Science Foundation [GAP302/10/1055]
- Grant Agency of the Ministry of the Health, Czech Republic [NT11081]
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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.
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