Change in IgG₁Fc N‐linked glycosylation in human lung cancer: Age‐ and sex‐related diagnostic potential

Abstract

The interactions of IgG Fc region with Fc receptors are optimized by the tailoring of a single-conserved N-linked glycosylation site at Asn-297. Our previous study has demonstrated that the age-related Fc-glycosylation change is featured by sex specificity and that the Fc-glycosylation has the potential for disease discrimination. Here, we conducted a Fourier transform ion cyclotron resonance MS-based profiling study involving 410 control individuals and 259 lung cancer (LC) patients. As compared to healthy controls, the marked increase in IgG1 Fc-agalactosylation and decrease in galactosylation were observed in LC patients. The binary logistic regression in combination with the receiver operating characteristic curve was used to determine the diagnostic ability of IgG1 Fc-glycosylation. It was found that this diagnostic ability was both sex and age dependent. Additionally, the change in Fc-glycosylation upon many different physiological and pathological conditions was retrospectively discussed. The data furthered the understanding of the immune-associated change in human LC, and also might be useful in the future attempts for Fc-glycosylation-associated diagnostic evaluations and clinical assays.

Glycomics for Type 2 Diabetes Biomarker Discovery: Promise of Immunoglobulin G Subclass-Specific Fragment Crystallizable N-glycosylation in the Uyghur Population

“…''Population Glycomics'' is one of the new and emerging approaches to biomarker discovery for common complex diseases. For example, studies in various world populations have found changes in IgG glycosylation in relation to, for example, metabolic syndrome (Lu et al, 2011), lung cancer (Chen et al, 2013), colorectal cancer (Vuckovic et al, 2016), Parkinson's disease (Russell et al, 2017), hypertension (Liu et al, 2018b), and T2DM (Lemmers et al, 2017). Itoh et al (2007) reported minute increments in an N-glycan with a1,6core-fucose within the total N-glycome that was associated with T2DM.…”

Disease-specific IgG Fc N-glycosylation as personalized biomarkers to differentiate gastric cancer from benign gastric diseases

“…Recently, emerging evidence indicates that changes in the glycosylation of total serum IgG isolated using Protein A or Protein G are associated with pathophysiological states 30 31 32 33 34 35 . In this study, we employ our developed approach to obtain DSIgG, which only exists in patients with chronic diseases 26 .…”

Glycomic Signatures of Plasma IgG Improve Preoperative Prediction of the Invasiveness of Small Lung Nodules

“…Recent studies have indicated the importance of altered glycosylation patterns of IgG in autoimmune diseases, infectious diseases, and different types of cancer [18][19][20]. Although several studies have reported declining levels of galactosylated N-glycans and bisecting GlcNAc structures on IgG in lung cancer [21][22][23], no studies have investigated the relationship between IgG glycosylation and pathological staging of small-sized pulmonary nodules.…”