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Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity. / Lavrsen, Kirstine; Madsen, Caroline B; Rasch, Morten G; Andersen, Anders Woetmann; Ødum, Niels; Mandel, Ulla; Clausen, Henrik; Pedersen, Anders E; Wandall, Hans H.

I: Glycoconjugate Journal, Bind 30, Nr. 3, 04.2013, s. 227-36.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Lavrsen, K, Madsen, CB, Rasch, MG, Andersen, AW, Ødum, N, Mandel, U, Clausen, H, Pedersen, AE & Wandall, HH 2013, 'Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity', Glycoconjugate Journal, bind 30, nr. 3, s. 227-36. https://doi.org/10.1007/s10719-012-9437-7

APA

Lavrsen, K., Madsen, C. B., Rasch, M. G., Andersen, A. W., Ødum, N., Mandel, U., ... Wandall, H. H. (2013). Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity. Glycoconjugate Journal, 30(3), 227-36. https://doi.org/10.1007/s10719-012-9437-7

Vancouver

Lavrsen K, Madsen CB, Rasch MG, Andersen AW, Ødum N, Mandel U o.a. Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity. Glycoconjugate Journal. 2013 apr;30(3):227-36. https://doi.org/10.1007/s10719-012-9437-7

Author

Lavrsen, Kirstine ; Madsen, Caroline B ; Rasch, Morten G ; Andersen, Anders Woetmann ; Ødum, Niels ; Mandel, Ulla ; Clausen, Henrik ; Pedersen, Anders E ; Wandall, Hans H. / Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity. I: Glycoconjugate Journal. 2013 ; Bind 30, Nr. 3. s. 227-36.

Bibtex

@article{29457ed4feb743dab345b3e2b24d0c23,
title = "Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity",
abstract = "Protein glycosylation often changes during cancer development, resulting in the expression of cancer-associated carbohydrate antigens. In particular mucins such as MUC1 are subject to these changes. We previously identified an immunodominant Tn-MUC1 (GalNAc-α-MUC1) cancer-specific epitope not covered by immunological tolerance in MUC1 humanized mice and man. The objective of this study was to determine if mouse antibodies to this Tn-MUC1 epitope induce antibody-dependent cellular cytotoxicity (ADCC) pivotal for their potential use in cancer immunotherapy. Binding affinity of mAb 5E5 directed to Tn-MUC1 was investigated using BiaCore. The availability of Tn-MUC1 on the surface of breast cancer cells was evaluated by immunohistochemistry, confocal microscopy, and flow cytometry, followed by in vitro assessment of antibody-dependent cellular cytotoxicity by mAb 5E5. Biacore analysis demonstrated high affinity binding (KD = 1.7 nM) of mAb 5E5 to its target, Tn-MUC1. Immunolabelling with mAb 5E5 revealed surface expression of the Tn-MUC1 epitope in breast cancer tissue and cell lines, and mAb 5E5 induced ADCC in two human breast cancer cell lines, MCF7 and T47D. Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity suggesting that antibodies targeting glycopeptide epitopes on mucins are strong candidates for cancer-specific immunotherapies.",
author = "Kirstine Lavrsen and Madsen, {Caroline B} and Rasch, {Morten G} and Andersen, {Anders Woetmann} and Niels {\O}dum and Ulla Mandel and Henrik Clausen and Pedersen, {Anders E} and Wandall, {Hans H}",
year = "2013",
month = "4",
doi = "10.1007/s10719-012-9437-7",
language = "English",
volume = "30",
pages = "227--36",
journal = "Glycoconjugate Journal",
issn = "0282-0080",
publisher = "Springer",
number = "3",

}

RIS

TY - JOUR

T1 - Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity

AU - Lavrsen, Kirstine

AU - Madsen, Caroline B

AU - Rasch, Morten G

AU - Andersen, Anders Woetmann

AU - Ødum, Niels

AU - Mandel, Ulla

AU - Clausen, Henrik

AU - Pedersen, Anders E

AU - Wandall, Hans H

PY - 2013/4

Y1 - 2013/4

N2 - Protein glycosylation often changes during cancer development, resulting in the expression of cancer-associated carbohydrate antigens. In particular mucins such as MUC1 are subject to these changes. We previously identified an immunodominant Tn-MUC1 (GalNAc-α-MUC1) cancer-specific epitope not covered by immunological tolerance in MUC1 humanized mice and man. The objective of this study was to determine if mouse antibodies to this Tn-MUC1 epitope induce antibody-dependent cellular cytotoxicity (ADCC) pivotal for their potential use in cancer immunotherapy. Binding affinity of mAb 5E5 directed to Tn-MUC1 was investigated using BiaCore. The availability of Tn-MUC1 on the surface of breast cancer cells was evaluated by immunohistochemistry, confocal microscopy, and flow cytometry, followed by in vitro assessment of antibody-dependent cellular cytotoxicity by mAb 5E5. Biacore analysis demonstrated high affinity binding (KD = 1.7 nM) of mAb 5E5 to its target, Tn-MUC1. Immunolabelling with mAb 5E5 revealed surface expression of the Tn-MUC1 epitope in breast cancer tissue and cell lines, and mAb 5E5 induced ADCC in two human breast cancer cell lines, MCF7 and T47D. Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity suggesting that antibodies targeting glycopeptide epitopes on mucins are strong candidates for cancer-specific immunotherapies.

AB - Protein glycosylation often changes during cancer development, resulting in the expression of cancer-associated carbohydrate antigens. In particular mucins such as MUC1 are subject to these changes. We previously identified an immunodominant Tn-MUC1 (GalNAc-α-MUC1) cancer-specific epitope not covered by immunological tolerance in MUC1 humanized mice and man. The objective of this study was to determine if mouse antibodies to this Tn-MUC1 epitope induce antibody-dependent cellular cytotoxicity (ADCC) pivotal for their potential use in cancer immunotherapy. Binding affinity of mAb 5E5 directed to Tn-MUC1 was investigated using BiaCore. The availability of Tn-MUC1 on the surface of breast cancer cells was evaluated by immunohistochemistry, confocal microscopy, and flow cytometry, followed by in vitro assessment of antibody-dependent cellular cytotoxicity by mAb 5E5. Biacore analysis demonstrated high affinity binding (KD = 1.7 nM) of mAb 5E5 to its target, Tn-MUC1. Immunolabelling with mAb 5E5 revealed surface expression of the Tn-MUC1 epitope in breast cancer tissue and cell lines, and mAb 5E5 induced ADCC in two human breast cancer cell lines, MCF7 and T47D. Aberrantly glycosylated MUC1 is expressed on the surface of breast cancer cells and a target for antibody-dependent cell-mediated cytotoxicity suggesting that antibodies targeting glycopeptide epitopes on mucins are strong candidates for cancer-specific immunotherapies.

U2 - 10.1007/s10719-012-9437-7

DO - 10.1007/s10719-012-9437-7

M3 - Journal article

C2 - 22878593

VL - 30

SP - 227

EP - 236

JO - Glycoconjugate Journal

JF - Glycoconjugate Journal

SN - 0282-0080

IS - 3

ER -

ID: 47749031