Dataset Information

Profiling of Subclass-Specific IgG Glycosylation in Gastric Cancer by nanoLC-ESI-MS/MS

ABSTRACT: Background:Gastric cancer (GC) is one of the most aggressive gastrointestinal malignancy and leading cause of cancer related deaths worldwide,warranting the urgent discovery of biomarkers for early detection. IgG glycosylation is strongly related to disease progression and specific IgG glycans have been regarded as the next-generation biomarker, whereas it is rarly studied on the association between subclass-specific IgG glycosylation profile and GC progression. Methods:A total of 141 individuals were enrolled and randomly sorted into discovery set consisting of normal (N=30) and cancer patients (N=20), and validation set including controls (N=30), benign (N=25) and cancer (N=36).IgG glycopeptides were tryptic digested and enrichmed by microcrystalline cellulose based solid phase extraction.Subclass-specific IgG N-glycosylation was analyzed by nanoLC-MS/MS. Results:It was found that GC progression was associated with increased sialylation and decreased bisection of IgG2, as well as substantially decreased sialylation of IgG1 and increased galactosylation of IgG3/4.Further analysis of individual glycopeptides showed the changes of particular glycosylation of IgGwere reflected by the specific glycans taht could apparently distinguish different stages of gastric disease patients from normal. Conclusions:Different subclasses of IgG glycosylation were differentially expressed in GC, specific IgG glycopeptides could be promising biomarker for early detection of GC patients.

INSTRUMENT(S): 4800 Proteomics Analyzer

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Cell, Blood Serum

DISEASE(S): Stomach Carcinoma

SUBMITTER: Si Liu

LAB HEAD: Xin Liu

PROVIDER: PXD027475 | Pride | 2025-05-06

REPOSITORIES: pride

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Dataset's files

Source:

			Action	DRS
	20210720_DiscoverySet_GastricCancer_01.wiff	Wiff
	20210720_DiscoverySet_GastricCancer_01.wiff.scan	Wiff
	20210720_DiscoverySet_GastricCancer_02.wiff	Wiff
	20210720_DiscoverySet_GastricCancer_02.wiff.scan	Wiff
	20210720_DiscoverySet_GastricCancer_03.wiff	Wiff

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Publications

Site-specific immunoglobulin G N-glycosylation is associated with gastric cancer progression.

Xu Tingting T Huang Jianmin J Lin Jiajing J Liu Yuanyuan Y Wang Yi Y Shen Wenkang W He Jianjie J Chen Shuyun S Zhu Xi X Que Yuqin Y Hu Mengting M Chen Yu Y Cheng Liming L He Honghao H Liu Xin X Liu Si S

BMC cancer 20250207 1

<h4>Background</h4>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.<h4>Methods</h4>The IgG N-glycome in GC was characterized using a custom high-throughput orthogonal mass spectrometry approach. Multiva ...[more]

PMID: 39920693

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Project description:Changes in IgG glycosylation have been reported to be associated with colorectal cancer (CRC), but the alteration in specific subclass of IgG is unknown. Herein, we optimized five common IgG glycopeptides enrichment methods to acquire comprehensive profiling of IgG glycoproteomics in CRC. Notably, incomplete tryptic digestion of IgG occurred when using ordinary ratio of protease to protein, which significantly impacted the final statistical analysis of association between IgG glycosylation and CRC. We introduced a method based on two-step enzymatic digestion, enabling the complete digestion of IgG glycopeptides and further improving the detection intensity of the target glycopeptides. By this approach, total 47 IgG glycopeptides can be identified by nanoLC-ESI-MS/MS. Following rapid and automatic data processing through the self-developed program, we observed that IgG1_H3N4F1 and IgG1_H3N4 were substantially increased in CRC, while IgG1_H5N5F1, IgG1_H5N4F1S1and IgG2_H5N4F1 were markedly decreased. Strikingly, these four glycopeptides were continually significantly changed in early and late stages of CRC. Further evaluation of the diagnostic performance showed they all obtained a fair performance in discriminating the patients from the normal. In terms of the glycan features, it demonstrated that CRC progression associates with the increased agalactosylation, and the decreased digalactosylation and galactosylation per antenna on diantennay glycans of IgG1 and IgG2. Concurrently, the decreased sialylation of IgG1 was strongly correlated with CRC. Moreover, tumor-specific glycosylation analysis showed that the alterations of subclass-specific IgG glycosylation were more significant in colon cancer, and no obvious difference between colon and rectal cancer was found. More importantly, all these findings were validated in an independent cohort. This two-step enzymatic approach is crucial to explore the relationship between the disease progression and IgG glycosylation.