Bibliographic Details
| Title: |
Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression. |
| Authors: |
Xu, Tingting1 (AUTHOR), Huang, Jianmin2 (AUTHOR), Lin, Jiajing3 (AUTHOR), Liu, Yuanyuan3 (AUTHOR), Wang, Yi4 (AUTHOR), Shen, Wenkang2 (AUTHOR), He, Jianjie3 (AUTHOR), Chen, Shuyun1 (AUTHOR), Zhu, Xi1 (AUTHOR), Que, Yuqin1 (AUTHOR), Hu, Mengting1 (AUTHOR), Chen, Yu1 (AUTHOR), Cheng, Liming4 (AUTHOR), He, Honghao5 (AUTHOR), Liu, Xin3 (AUTHOR) xliu@mail.hust.edu.cn, Liu, Si1 (AUTHOR) siliu@fjmu.edu.cn |
| Source: |
BMC Cancer. 2/7/2025, Vol. 25 Issue 1, p1-13. 13p. |
| Subject Terms: |
*ENZYME-linked immunosorbent assay, *IMMUNOGLOBULIN G, *CYTOLOGY, *STOMACH cancer, *LIFE sciences |
| 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. [ABSTRACT FROM AUTHOR] |
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