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
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 bee...
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Published in | Biochemical and biophysical research communications Vol. 469; no. 4; pp. 1140 - 1145 |
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Main Authors | , , , , , , , , , , |
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22.01.2016
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Abstract | 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.
•Serum IgG Fc region N-glycans were profiled in breast cancer patients and controls.•Breast cancer patients had a characteristic pattern of IgG Fc region N-glycosylation.•This pattern can be used to distinguish breast cancer (including stage 0) patients.•IgG N-glycan profiling might be a potential new biomarker for breast cancer.•Role of IgG Fc region N-glycosylation in tumor immunity should be examined. |
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AbstractList | 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. 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. •Serum IgG Fc region N-glycans were profiled in breast cancer patients and controls.•Breast cancer patients had a characteristic pattern of IgG Fc region N-glycosylation.•This pattern can be used to distinguish breast cancer (including stage 0) patients.•IgG N-glycan profiling might be a potential new biomarker for breast cancer.•Role of IgG Fc region N-glycosylation in tumor immunity should be examined. |
Author | Fujita, Yuichiro Kawaguchi-Sakita, Nobuko Kajihara, Shigeki Iwamoto, Shinichi Kaneshiro-Nakagawa, Kaoru Kawashima, Masahiro Tanaka, Koichi Tokiwa, Mariko Suzuki, Eiji Toi, Masakazu Sugimoto, Masahiro |
Author_xml | – sequence: 1 givenname: Nobuko orcidid: 0000-0001-8667-1427 surname: Kawaguchi-Sakita fullname: Kawaguchi-Sakita, Nobuko email: nobuko75@kuhp.kyoto-u.ac.jp organization: Department of Breast Surgery, Kyoto University Hospital, 54 Shogoin-Kawaracho, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 2 givenname: Kaoru surname: Kaneshiro-Nakagawa fullname: Kaneshiro-Nakagawa, Kaoru organization: Shimadzu Corporation, 1 Nishinokyo-Kuwabaracho, Nakagyo-ku, Kyoto 604-8511, Japan – sequence: 3 givenname: Masahiro surname: Kawashima fullname: Kawashima, Masahiro organization: Department of Breast Surgery, Kyoto University Hospital, 54 Shogoin-Kawaracho, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 4 givenname: Masahiro surname: Sugimoto fullname: Sugimoto, Masahiro organization: Institute for Advanced Bioscience, Keio University, 246-2 Mizukami, Kakuganji, Tsuruoka, Yamagata 997-0052, Japan – sequence: 5 givenname: Mariko surname: Tokiwa fullname: Tokiwa, Mariko organization: Department of Breast Surgery, Kyoto University Graduate School of Medicine, 54 Shogoin-Kawaracho, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 6 givenname: Eiji surname: Suzuki fullname: Suzuki, Eiji organization: Department of Breast Surgery, Kyoto University Hospital, 54 Shogoin-Kawaracho, Sakyo-ku, Kyoto 606-8507, Japan – sequence: 7 givenname: Shigeki surname: Kajihara fullname: Kajihara, Shigeki organization: Shimadzu Corporation, 1 Nishinokyo-Kuwabaracho, Nakagyo-ku, Kyoto 604-8511, Japan – sequence: 8 givenname: Yuichiro surname: Fujita fullname: Fujita, Yuichiro organization: Shimadzu Corporation, 1 Nishinokyo-Kuwabaracho, Nakagyo-ku, Kyoto 604-8511, Japan – sequence: 9 givenname: Shinichi surname: Iwamoto fullname: Iwamoto, Shinichi organization: Shimadzu Corporation, 1 Nishinokyo-Kuwabaracho, Nakagyo-ku, Kyoto 604-8511, Japan – sequence: 10 givenname: Koichi surname: Tanaka fullname: Tanaka, Koichi organization: Shimadzu Corporation, 1 Nishinokyo-Kuwabaracho, Nakagyo-ku, Kyoto 604-8511, Japan – sequence: 11 givenname: Masakazu surname: Toi fullname: Toi, Masakazu organization: Department of Breast Surgery, Kyoto University Hospital, 54 Shogoin-Kawaracho, Sakyo-ku, Kyoto 606-8507, Japan |
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Snippet | Herein, we report that breast cancer (BC) patients can be distinguished from cancer-free (NC) controls by serum immunoglobulin G (IgG) crystallizable fragment... |
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SubjectTerms | Biomarker Biomarkers, Tumor - blood Breast cancer Breast Neoplasms - blood Breast Neoplasms - diagnosis Female Gene Expression Profiling - methods Glycosylation Humans IgG Fc region N-glycosylation Immunoglobulin Fc Fragments - blood Immunoglobulin G - blood Polysaccharides - blood Reproducibility of Results Sensitivity and Specificity Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods Tumor immunity |
Title | 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 |
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