Abstract
BackgroundBecause glycosylation is one of the most common post-translational modifications of proteins and because changes in glycosylation have been shown to have a significant correlation with the development of many cancer types, we investigated the serum N-glycome used to diagnose, stage and evaluate the pathological outcomes in IgD multiple myeloma.MethodsSerum samples were available for 20 patients with IgD multiple myeloma, 41 patients with light chain multiple myeloma and 42 healthy control subjects. Serum N-glycans were released and analysed using DNA sequencer-assisted fluorophore-assisted capillary electrophoresis.ResultsCharacteristic changes were revealed in the serum N-glycome of IgD myeloma. In particular, three N-glycans (NG1(6)A2F, Peak3; NG1(3)A2F, Peak4; NA2FB, Peak7) showed increased clinical value. The best area under the ROC curve of NG1(6)A2F to diagnose IgD myeloma was 0.981, with a 95.0% sensitivity and 95.2% specificity, and that of NG1(3)A2F was 0.936, with a 95.0% sensitivity and 78.6% specificity. The best area under the ROC curve of NA2FB/NG1(3)A2F to differentially diagnose IgD myeloma versus light chain myeloma was 0.744, with a 95.3% sensitivity and 50.0% specificity. The level of NG1(3)A2F was correlated with the international staging system, while the higher abundance of NA2FB presented in IgD myeloma was predictive of a shorter progression-free survival.ConclusionsThe advent of serum N-glycan signatures may play a role in the diagnosis, staging and prognosis of IgD myeloma and will serve as the foundation for a precision medicine approach to this rare subtype of multiple myeloma.
Highlights
Because glycosylation is one of the most common post-translational modifications of proteins and because changes in glycosylation have been shown to have a significant correlation with the development of many cancer types, we investigated the serum N-glycome used to diagnose, stage and evaluate the pathological outcomes in IgD multiple myeloma
Mittermayr S et al [10] have demonstrates the feasibility of mapping glycan modifications on the IgG molecule and provided the principle that differential IgG glycosylation patterns can be successfully identified in monoclonal gammopathy of undetermined significance (MGUS), smoldering multiple myeloma (SMM), active MM, complete-response post-treatment MM and relapse MM
We recently demonstrated that the serum N-glycan profile models distinguished patients with light chain multiple myeloma (LCMM) from healthy control subjects (CTRs) and differentiated LCMM from other subtypes of multiple myeloma (IgG and IgA) [19]
Summary
Because glycosylation is one of the most common post-translational modifications of proteins and because changes in glycosylation have been shown to have a significant correlation with the development of many cancer types, we investigated the serum N-glycome used to diagnose, stage and evaluate the pathological outcomes in IgD multiple myeloma. Variations in N-linked oligosaccharides are involved in many pathological conditions such as chronic diseases and cancers [6,7,8,9]. Mittermayr S et al [10] have demonstrates the feasibility of mapping glycan modifications on the IgG molecule and provided the principle that differential IgG glycosylation patterns can be successfully identified in monoclonal gammopathy of undetermined significance (MGUS), smoldering multiple myeloma (SMM), active MM, complete-response post-treatment MM and relapse MM. Kovacs Z et al [11] have indicated 12 N-glycan
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