An N-glycoproteomics Analysis Reveals Glycoprotein Alterations in Esophageal Squamous Cell Carcinoma

Background: Aberrant glycosylation has been recognized as a hallmark of cancer. It usually includes the changes of expression level and function of glycoproteins caused by abnormal glycosylation modification and changes of glycan structure of glycoproteins. N-glycosylation is one of the main types of glycosylation in all eukaryotes.Methods: We integrated global proteomics and N-glycoproteomics analysis of ten cases to reveal the N-glycoproteomics profiles in esophageal squamous cell carcinoma (ESCC) compared with normal tissues. Results: A series of differentially expressed glycoproteins (e.g. LAMP2, PLOD2) and some differentially glycoproteins enriched signaling pathway (e.g. metabolism-related pathway, ECM-receptor interaction, focal adhesion) were identified in ESCC. Seven significantly enriched motifs were found from all of the identified N-glycosylation sites. The dynamic profiling changes of glycoprotein during lymph node metastasis progression in ESCC was also investigated and three clusters showed the obvious increasing or decreasing trend with lymph node metastasis.Conclusion: In summary, we presented the characters of N-glycosylation and N-glycoprotein alterations associated with ESCC. Specific changes in the expression of glycoproteins or glycosylation occupancy have the potential to be used as the biomarker to discriminate ESCC from normal tissues and to improve our understanding of ESCC biology.