Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression
Abstract Background The relationship between cancer development and alterations in IgG N-glycosylation has been well-established. However, comprehensive profiling of the N-glycome and N-glycoproteome in gastric cancer (GC) remains limited. Furthermore, the prognostic potential of IgG N-glycan patter...
Saved in:
| Main Authors: | , , , , , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
BMC
2025-02-01
|
| Series: | BMC Cancer |
| Subjects: | |
| Online Access: | https://doi.org/10.1186/s12885-025-13616-z |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1823862016612237312 |
|---|---|
| author | Tingting Xu Jianmin Huang Jiajing Lin Yuanyuan Liu Yi Wang Wenkang Shen Jianjie He Shuyun Chen Xi Zhu Yuqin Que Mengting Hu Yu Chen Liming Cheng Honghao He Xin Liu Si Liu |
| author_facet | Tingting Xu Jianmin Huang Jiajing Lin Yuanyuan Liu Yi Wang Wenkang Shen Jianjie He Shuyun Chen Xi Zhu Yuqin Que Mengting Hu Yu Chen Liming Cheng Honghao He Xin Liu Si Liu |
| author_sort | Tingting Xu |
| collection | DOAJ |
| description | Abstract Background The relationship between cancer development and alterations in IgG N-glycosylation has been well-established. However, comprehensive profiling of the N-glycome and N-glycoproteome in gastric cancer (GC) remains limited. Furthermore, the prognostic potential of IgG N-glycan patterns in identifying precursors to GC has yet to be fully elucidated. Methods The IgG N-glycome in GC was characterized using a custom high-throughput orthogonal mass spectrometry approach. Multivariate analysis was employed to identify and assess glycomic alterations. A comprehensive bioinformatics analysis was also conducted to investigate the differential expression of N-glycosylation-related genes and their potential roles in GC pathogenesis. Additionally, interleukin-11 (IL-11) levels were quantified using a standardized enzyme-linked immunosorbent assay (ELISA). Results Galactosylation and sialylation of IgG decreased mainly in the IgG1 and IgG2 subclasses in GC, with subclass-specific changes in IgG3 and IgG4 galactosylation. These glycan modifications were represented by unique glycopeptides (IgG1_H5N5, IgG2_H4N3F1, IgG2_H4N4, IgG2_H4N4F1S1, IgG3/4_H4N4F1, IgG3/4_H4N4F1S1), which outperformed CA72-4 for GC diagnosis. Analysis of key glycogenes revealed differential expression patterns, implicating a functional role for IgG N-glycosylation in GC. Notably, the abundance of specific IgG glycosylation exhibited a significant correlation with serum level of IL-11. Conclusions Alterations in subclass-specific IgG N-glycosylation represent promising biomarkers for the detection and monitoring of GC progression, potentially influenced by cytokine-driven inflammation. Understanding these changes could improve our knowledge of molecular mechanisms, aiding in diagnostic improvements and therapeutic development. |
| format | Article |
| id | doaj-art-faf34b7b15f5491b86a159e515dc51d9 |
| institution | Kabale University |
| issn | 1471-2407 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Cancer |
| spelling | doaj-art-faf34b7b15f5491b86a159e515dc51d92025-02-09T12:41:35ZengBMCBMC Cancer1471-24072025-02-0125111310.1186/s12885-025-13616-zSite-specific immunoglobulin G N-glycosylation is associated with gastric cancer progressionTingting Xu0Jianmin Huang1Jiajing Lin2Yuanyuan Liu3Yi Wang4Wenkang Shen5Jianjie He6Shuyun Chen7Xi Zhu8Yuqin Que9Mengting Hu10Yu Chen11Liming Cheng12Honghao He13Xin Liu14Si Liu15Department of Epidemiology and Health Statistics, School of Public Health, Fujian Medical UniversityDigestive Endoscopy Center, Fuzhou University Affiliated Provincial HospitalThe Key Laboratory for Biomedical Photonics of MOE at Wuhan National Laboratory for Optoelectronics-Hubei Bioinformatics & Molecular Imaging Key Laboratory, Systems Biology Theme, Department of Biomedical Engineering, College of Life Science and Technology, Huazhong University of Science and TechnologyThe Key Laboratory for Biomedical Photonics of MOE at Wuhan National Laboratory for Optoelectronics-Hubei Bioinformatics & Molecular Imaging Key Laboratory, Systems Biology Theme, Department of Biomedical Engineering, College of Life Science and Technology, Huazhong University of Science and TechnologyDepartment of Laboratory Medicine, Tongji Hospital, Tongji Medical College, Huazhong University of Science and TechnologyDigestive Endoscopy Center, Fuzhou University Affiliated Provincial HospitalThe Key Laboratory for Biomedical Photonics of MOE at Wuhan National Laboratory for Optoelectronics-Hubei Bioinformatics & Molecular Imaging Key Laboratory, Systems Biology Theme, Department of Biomedical Engineering, College of Life Science and Technology, Huazhong University of Science and TechnologyDepartment of Epidemiology and Health Statistics, School of Public Health, Fujian Medical UniversityDepartment of Epidemiology and Health Statistics, School of Public Health, Fujian Medical UniversityDepartment of Epidemiology and Health Statistics, School of Public Health, Fujian Medical UniversityDepartment of Epidemiology and Health Statistics, School of Public Health, Fujian Medical UniversityDepartment of Epidemiology and Health Statistics, School of Public Health, Fujian Medical UniversityDepartment of Laboratory Medicine, Tongji Hospital, Tongji Medical College, Huazhong University of Science and TechnologySino-US Telemed (Wuhan) Co., LtdThe Key Laboratory for Biomedical Photonics of MOE at Wuhan National Laboratory for Optoelectronics-Hubei Bioinformatics & Molecular Imaging Key Laboratory, Systems Biology Theme, Department of Biomedical Engineering, College of Life Science and Technology, Huazhong University of Science and TechnologyDepartment of Epidemiology and Health Statistics, School of Public Health, Fujian Medical UniversityAbstract Background The relationship between cancer development and alterations in IgG N-glycosylation has been well-established. However, comprehensive profiling of the N-glycome and N-glycoproteome in gastric cancer (GC) remains limited. Furthermore, the prognostic potential of IgG N-glycan patterns in identifying precursors to GC has yet to be fully elucidated. Methods The IgG N-glycome in GC was characterized using a custom high-throughput orthogonal mass spectrometry approach. Multivariate analysis was employed to identify and assess glycomic alterations. A comprehensive bioinformatics analysis was also conducted to investigate the differential expression of N-glycosylation-related genes and their potential roles in GC pathogenesis. Additionally, interleukin-11 (IL-11) levels were quantified using a standardized enzyme-linked immunosorbent assay (ELISA). Results Galactosylation and sialylation of IgG decreased mainly in the IgG1 and IgG2 subclasses in GC, with subclass-specific changes in IgG3 and IgG4 galactosylation. These glycan modifications were represented by unique glycopeptides (IgG1_H5N5, IgG2_H4N3F1, IgG2_H4N4, IgG2_H4N4F1S1, IgG3/4_H4N4F1, IgG3/4_H4N4F1S1), which outperformed CA72-4 for GC diagnosis. Analysis of key glycogenes revealed differential expression patterns, implicating a functional role for IgG N-glycosylation in GC. Notably, the abundance of specific IgG glycosylation exhibited a significant correlation with serum level of IL-11. Conclusions Alterations in subclass-specific IgG N-glycosylation represent promising biomarkers for the detection and monitoring of GC progression, potentially influenced by cytokine-driven inflammation. Understanding these changes could improve our knowledge of molecular mechanisms, aiding in diagnostic improvements and therapeutic development.https://doi.org/10.1186/s12885-025-13616-zGastric cancerIgG N-glycansIgG glycopeptidesIL-11Bioinformatics analysis |
| spellingShingle | Tingting Xu Jianmin Huang Jiajing Lin Yuanyuan Liu Yi Wang Wenkang Shen Jianjie He Shuyun Chen Xi Zhu Yuqin Que Mengting Hu Yu Chen Liming Cheng Honghao He Xin Liu Si Liu Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression BMC Cancer Gastric cancer IgG N-glycans IgG glycopeptides IL-11 Bioinformatics analysis |
| title | Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression |
| title_full | Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression |
| title_fullStr | Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression |
| title_full_unstemmed | Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression |
| title_short | Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression |
| title_sort | site specific immunoglobulin g n glycosylation is associated with gastric cancer progression |
| topic | Gastric cancer IgG N-glycans IgG glycopeptides IL-11 Bioinformatics analysis |
| url | https://doi.org/10.1186/s12885-025-13616-z |
| work_keys_str_mv | AT tingtingxu sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT jianminhuang sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT jiajinglin sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT yuanyuanliu sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT yiwang sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT wenkangshen sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT jianjiehe sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT shuyunchen sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT xizhu sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT yuqinque sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT mengtinghu sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT yuchen sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT limingcheng sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT honghaohe sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT xinliu sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression AT siliu sitespecificimmunoglobulingnglycosylationisassociatedwithgastriccancerprogression |