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Changes in protein glycosylation have been reported in various types of cancer, including cholangiocarcinoma (CCA). Nanospray ionization-linear ion trap mass spectrometry (NSI-MS  n  ) was used in the present study to determine the comparative structural glycomics of the N -linked glycans in the serum of patients with CCA compared with healthy controls. A total of 5 high-mannose and 4 complex N -linked glycans were detected. Mannose 7 -N-acetyl-glucosamine 2 was the most abundant structure among the high-mannose types (control 12.12±2.54 vs. CCA 9.27±2.66%), whereas NeuAc2H2N2M3N2 predominated the complex types (control 61.17±2.55 vs. CCA 64.68±4.23%). The expression of 3 different N -glycans differed significantly between the CCA cases and controls. These included mannose 6 -N-acetyl-glucosamine 2 (P=0.044), mannose 9 -N-acetyl-glucosamine 2 (Ρ=0.030) and NeuAc3H3N3M3N2F (Ρ=0.002). These three glycan structures may therefore be associated with tumor progression in CCA and may be useful for its diagnosis.

Increased expression of the high‑mannose M6N2 and NeuAc3H3N3M3N2F tri‑antennary N‑glycans in cholangiocarcinoma