Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma

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Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma. / Stuchlová Horynová, Milada; Raška, Milan; Clausen, Henrik; Novak, Jan.

I: Cellular and Molecular Life Sciences, Bind 70, Nr. 5, 03.2013, s. 829-839.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Stuchlová Horynová, M, Raška, M, Clausen, H & Novak, J 2013, 'Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma', Cellular and Molecular Life Sciences, bind 70, nr. 5, s. 829-839. https://doi.org/10.1007/s00018-012-1082-6

APA

Stuchlová Horynová, M., Raška, M., Clausen, H., & Novak, J. (2013). Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma. Cellular and Molecular Life Sciences, 70(5), 829-839. https://doi.org/10.1007/s00018-012-1082-6

Vancouver

Stuchlová Horynová M, Raška M, Clausen H, Novak J. Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma. Cellular and Molecular Life Sciences. 2013 mar;70(5):829-839. https://doi.org/10.1007/s00018-012-1082-6

Author

Stuchlová Horynová, Milada ; Raška, Milan ; Clausen, Henrik ; Novak, Jan. / Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma. I: Cellular and Molecular Life Sciences. 2013 ; Bind 70, Nr. 5. s. 829-839.

Bibtex

@article{6501e50327ff488da78f76ddf5781a9c,
title = "Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma",
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.",
author = "{Stuchlov{\'a} Horynov{\'a}}, Milada and Milan Raška and Henrik Clausen and Jan Novak",
year = "2013",
month = "3",
doi = "10.1007/s00018-012-1082-6",
language = "English",
volume = "70",
pages = "829--839",
journal = "Cellular and Molecular Life Sciences",
issn = "1420-682X",
publisher = "Springer Basel AG",
number = "5",

}

RIS

TY - JOUR

T1 - Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma

AU - Stuchlová Horynová, Milada

AU - Raška, Milan

AU - Clausen, Henrik

AU - Novak, Jan

PY - 2013/3

Y1 - 2013/3

N2 - 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.

AB - 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.

U2 - 10.1007/s00018-012-1082-6

DO - 10.1007/s00018-012-1082-6

M3 - Journal article

VL - 70

SP - 829

EP - 839

JO - Cellular and Molecular Life Sciences

JF - Cellular and Molecular Life Sciences

SN - 1420-682X

IS - 5

ER -

ID: 40840642