Analysis of blood-based glycans represents a new strategy for cancer diagnosis. Immunoglobin G (IgG), a highly abundant glycoprotein in serum, is known to mediate a variety of blood immune responses. There has been an increasing interest in the analysis of the N-glycan profile of human IgG in healthy and disease states, such as auto-immune diseases and cancer. Although altered glycosylation of total serum IgG has been profiled individually in ovarian, prostate, gastric cancers, no studies have systematically investigated the alteration of IgG glycosylation in multiple cancers simultaneously. In addition, the sample sizes in previous studies were limited. With high throughput analytical method based on mass spectrometry for relative quantitative analysis of IgG glycans we previously developed, we designed for the first time a large-scale（n=5600）, multi-institute study to assess the quantitative changes of IgG glycosylation in 12 types of cancers，inflammatory diseases, benign conditions as well as healthy individuals simultaneously. We demonstrated that the distribution patterns of serum IgG galactosylation have similar alterations in multiple types of cancer. And thus we provided evidences for the first time that serum IgG galactosylation has great potential to be used as a non-invasive pan-cancer biomarker for early-stage cancer detection and cancer screening. More studies are underway to investigate the role and mechanism of IgG galactosylation in readout of immunological status.

Human serum IgG glycosylation as a promising biomarker for cancer diagnosis

256th National Meeting (2018)

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