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Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma
M. Stuchlová Horynová, M. Raška, H. Clausen, J. Novak,
Language English Country Switzerland
Document type Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't, Review
Grant support
NT11081
MZ0
CEP Register
Digital library NLK
Full text - Article
Source
NLK
PubMed Central
from 1997
ProQuest Central
from 1997-01-01 to 2017-12-31
Medline Complete (EBSCOhost)
from 2000-01-01
Health & Medicine (ProQuest)
from 1997-01-01 to 2017-12-31
- MeSH
- Adenocarcinoma immunology MeSH
- Glycosylation MeSH
- Glomerulonephritis, IGA immunology MeSH
- Immunoglobulin A chemistry immunology MeSH
- Humans MeSH
- Molecular Sequence Data MeSH
- Mucin-1 chemistry immunology MeSH
- Breast Neoplasms immunology MeSH
- Polysaccharides chemistry immunology MeSH
- Antibodies chemistry immunology MeSH
- Breast immunology MeSH
- Carbohydrate Sequence MeSH
- Amino Acid Sequence MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Female MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Research Support, N.I.H., Extramural MeSH
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.
References provided by Crossref.org
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