TY - JOUR
T1 - Serum immunoglobulin G Fc region N-glycosylation profiling by matrix-assisted laser desorption/ionization mass spectrometry can distinguish breast cancer patients from cancer-free controls
AU - Kawaguchi-Sakita, Nobuko
AU - Kaneshiro-Nakagawa, Kaoru
AU - Kawashima, Masahiro
AU - Sugimoto, Masahiro
AU - Tokiwa, Mariko
AU - Suzuki, Eiji
AU - Kajihara, Shigeki
AU - Fujita, Yuichiro
AU - Iwamoto, Shinichi
AU - Tanaka, Koichi
AU - Toi, Masakazu
N1 - Funding Information:
The authors thank Dr Nagahiro Minato (Department of Immunology and Cell Biology, Graduate School of Medicine, Kyoto University), Dr Keiko Iwaisako (Department of Target Therapy Oncology, Kyoto University Graduate School of Medicine), Mr Masahiro Hirata, Dr Tatsuki R. Kataoka, Dr Takaki Sakurai (Department of Diagnostic Pathology, Kyoto University Hospital)and Dr Naoyuki Taniguchi (RIKEN Global Research Cluster) for helpful discussions. The authors also would like to thank the participants for kindly giving samples and the members of Breast Oncology Research Network Bio Bank (BBB), Kyoto Breast Cancer Research Network (KBCRN) for sample collection; we would particularly like to thank Dr Norimichi Kan (Kan Norimichi Clinic), Dr Susumu Mashima (Department of Surgery, Nara Social Insurance Hospital), and Dr Shigeru Tsuyuki (Department of Breast Surgery, Osaka Red Cross Hospital). This study was supported by the Japan Society for the Promotion of Science through its Funding Program for World-Leading Innovative R&D on Science and Technology (FIRST Program). The funding source had no role in any aspect of this study.
Publisher Copyright:
© 2015 Elsevier Inc. All rights reserved.
PY - 2016/1/22
Y1 - 2016/1/22
N2 - Herein, we report that breast cancer (BC) patients can be distinguished from cancer-free (NC) controls by serum immunoglobulin G (IgG) crystallizable fragment (Fc) region N-glycosylation profiling using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Recently, there has been much progress in the field of tumor immunology. However, to date, the role and biomarker potential of IgG Fc region N-glycosylation, which affects the function of antibodies, have not been examined in BC. In the present study, we profiled serum IgG Fc region N-glycans in BC patients (N = 90) and NC controls (N = 54) using MALDI-MS. An IgG Fc region N-glycan-based multiple logistic regression model was produced which could distinguish BC patients from NC controls (area under the receiver operative characteristic curve = 0.874). Furthermore, stage 0 patients could also be distinguished using this model. These results suggest that an unknown humoral factor or soluble mediator affects IgGs from the earliest stage of breast cancer, and also suggests that IgG Fc region N-glycosylation may play a role in tumor biology. Although further investigation is required, our findings are the evidence that IgG N-glycan profiling has the potential to be used as a breast cancer biomarker and may provide the insights into tumor immunology.
AB - Herein, we report that breast cancer (BC) patients can be distinguished from cancer-free (NC) controls by serum immunoglobulin G (IgG) crystallizable fragment (Fc) region N-glycosylation profiling using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Recently, there has been much progress in the field of tumor immunology. However, to date, the role and biomarker potential of IgG Fc region N-glycosylation, which affects the function of antibodies, have not been examined in BC. In the present study, we profiled serum IgG Fc region N-glycans in BC patients (N = 90) and NC controls (N = 54) using MALDI-MS. An IgG Fc region N-glycan-based multiple logistic regression model was produced which could distinguish BC patients from NC controls (area under the receiver operative characteristic curve = 0.874). Furthermore, stage 0 patients could also be distinguished using this model. These results suggest that an unknown humoral factor or soluble mediator affects IgGs from the earliest stage of breast cancer, and also suggests that IgG Fc region N-glycosylation may play a role in tumor biology. Although further investigation is required, our findings are the evidence that IgG N-glycan profiling has the potential to be used as a breast cancer biomarker and may provide the insights into tumor immunology.
KW - Biomarker
KW - Breast cancer
KW - IgG Fc region N-glycosylation
KW - Tumor immunity
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U2 - 10.1016/j.bbrc.2015.12.114
DO - 10.1016/j.bbrc.2015.12.114
M3 - Article
C2 - 26740182
AN - SCOPUS:84957838712
SN - 0006-291X
VL - 469
SP - 1140
EP - 1145
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -