Quantitative Analysis of Serum IgG Galactosylation Assists Differential Diagnosis of Ovarian Cancer

Qian, Yifan; Wang, Yisheng; Zhang, Qizhou; Zhou, Lei; Zhang, Zejian; Xu, Jiejie; Ruan, Yuanyuan; Ren, Shifang; Xu, Congjian; Gu, Jianxin

doi:10.1021/pr4003992

Cited by 67 publications

(59 citation statements)

References 56 publications

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“…On the other hand, all five of the features addressing galactosylation and all two features addressing sialylation met the criteria for significance, indicating differential galactosylation and sialylation on serum proteins in NSCLC. Differential galactosylation on the high abundance protein IgG has previously been implicated in multiple types of cancer (20–23) and autoimmune diseases (24–26). …”

Section: Resultsmentioning

confidence: 99%

Serum Glycans as Risk Markers for Non–Small Cell Lung Cancer

Ruhaak

Stroble

Dai

et al. 2016

Cancer Prevention Research

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Previous studies have suggested occurrence of altered serum glycan profiles in patients with lung cancer. Here, we aimed to determine the predictive value of serum glycans to distinguish non-small cell lung cancer (NSCLC) cases from controls in prediagnostic samples using a previously validated predictive protein marker pro-SFTPB, as anchor. Blinded prediagnostic serum samples were obtained from the Carotene and Retinol Efficacy Trial (CARET), and included a discovery set of 100 NSCLC cases and 199 healthy controls. A second test set consisted of 108 cases and 216 controls. Cases and controls were matched for age at baseline (5-year groups), sex, smoking status (current vs. former), study enrollment cohort, and date of blood draw. Serum glycan profiles were determined by mass spectrometry. Twelve glycan variables were identified to have significant discriminatory power between cases and controls in the discovery set (AUC > 0.6). Of these, four were confirmed in the independent validation set. A combination marker yielded AUCs of 0.74 and 0.64 in the discovery and test set, respectively. Four glycan variables exhibited significant incremental value when combined with pro-SFTPB compared with pro-SFTPB alone with AUCs of 0.73, 0.72, 0.72, and 0.72 in the test set, indicating that serum glycan signatures have relevance to risk assessment for NSCLC. Cancer Prev Res; 9(4); 317-23. Ó2016 AACR.

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Section: Resultsmentioning

confidence: 99%

Serum Glycans as Risk Markers for Non–Small Cell Lung Cancer

Ruhaak

Stroble

Dai

et al. 2016

Cancer Prevention Research

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“…In particular, a decline in plasma IgG galactosylation has been observed in multiple myeloma, prostate, gastric, lung and ovarian cancers3031323334353637. Previous studies investigated small sample sizes (<100 cancer cases).…”

Section: Discussionmentioning

confidence: 99%

Glycosylation of plasma IgG in colorectal cancer prognosis

Τheodoratou

Thaçi

Agakov³

et al. 2016

Sci Rep

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In this study we demonstrate the potential value of Immunoglobulin G (IgG) glycosylation as a novel prognostic biomarker of colorectal cancer (CRC). We analysed plasma IgG glycans in 1229 CRC patients and correlated with survival outcomes. We assessed the predictive value of clinical algorithms and compared this to algorithms that also included glycan predictors. Decreased galactosylation, decreased sialylation (of fucosylated IgG glycan structures) and increased bisecting GlcNAc in IgG glycan structures were strongly associated with all-cause (q < 0.01) and CRC mortality (q = 0.04 for galactosylation and sialylation). Clinical algorithms showed good prediction of all-cause and CRC mortality (Harrell’s C: 0.73, 0.77; AUC: 0.75, 0.79, IDI: 0.02, 0.04 respectively). The inclusion of IgG glycan data did not lead to any statistically significant improvements overall, but it improved the prediction over clinical models for stage 4 patients with the shortest follow-up time until death, with the median gain in the test AUC of 0.08. These glycan differences are consistent with significantly increased IgG pro-inflammatory activity being associated with poorer CRC prognosis, especially in late stage CRC. In the absence of validated biomarkers to improve upon prognostic information from existing clinicopathological factors, the potential of these novel IgG glycan biomarkers merits further investigation.

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“…However, studies of IgG glycosylation in cancer patients, and thus the role of the humoral immune response in this disease, are scarce. Recently, studies determined altered IgG glycosylation patterns with ovarian [29, 30] and gastric [31] cancer. Clearly altered glycosylation patterns were observed in both studies.…”

Section: Introductionmentioning

confidence: 99%

The serum immunoglobulin G glycosylation signature of gastric cancer

Ruhaak

Barkauskas

Torres

et al. 2015

EuPA Open Proteomics

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Biomarkers may facilitate detection of gastric cancer at an earlier stage and reduce mortality. Here we sought to determine if the glycosylation profile of serum immunoglobulin G (IgG) could distinguish patients with non-atrophic gastritis (NAG), duodenal ulcer (DU) and gastric cancer (GC). Serum IgG was released and analyzed using nano-LC-TOF mass spectrometry. Statistically significant false discovery rate (FDR)-adjusted p-values were observed for 18 glycans, eight that differed significantly between NAG and GC, three that distinguished NAG from DU, and eight that differed between DU and GC. The IgG glycosylation signature may be useful as a predictive marker for gastric cancer.

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Quantitative Analysis of Serum IgG Galactosylation Assists Differential Diagnosis of Ovarian Cancer

Cited by 67 publications

References 56 publications

Serum Glycans as Risk Markers for Non–Small Cell Lung Cancer

Serum Glycans as Risk Markers for Non–Small Cell Lung Cancer

Glycosylation of plasma IgG in colorectal cancer prognosis

The serum immunoglobulin G glycosylation signature of gastric cancer

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