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Glycoproteomics and Glycomics in the Biomedical Area Special Issue

Glycans exist extensively in nature and play essential roles in human body. Glycomics is the comprehensive study of the structures and biological functions of glycans, which can be free or present in more complex molecules (e.g., proteins) in cells or organisms. Protein glycosylation is critical in many cellular processes. The dysregulation of glycosylation is associated with several human diseases, including diabetes, cancer, and cardiovascular disease. Modern mass spectrometry provides the best high-throughput approaches to characterize the glycosylation state of proteins, including glycans, glycosites, occupancy, and heterogeneity to answer the questions in the study of glycans. The isolation and characterization of the glycopeptides or glycoproteins, predominantly through the use of mass spectrometry, is called glycoproteomics. Glycoproteomics and glycomics are the subjects of this special issue. The development of glycoproteomics began in the early 1970s shortly after mass spectrometry was first applied to protein sequencing.[1] Over the years, the instruments and protocols were developed steadily.[2,3] There are two primary strategies to analyze glycoproteome using mass spectrometry: analyzing separated glycans and peptides or intact glycopeptides.[4] The former strategy can reduce the complexity of analysis to convert the glycoproteome analysis to two more straightforward problems: glycomics analysis and proteome analysis, both of which can be solved using existed analytical methods. However, the separation caused the loss of the information of glycosite and glycosylation heterogeneity. Analysis of the intact glycopeptides is challenging, which requires the improvements of both instrumentation and computational tools. Recently, many groups have applied analyses of intact glycopeptides to study glycosylation heterogeneity from a specific glycoprotein or complex samples.[5–10] Several software tools have been developed to assist the assignment of glycopeptides allowing for high-throughput identification of intact glycopeptides.[11–18] Till now, thousands of glycoproteins have been reported through identifying their glycosite-containing peptides using mass spectrometry. These data have facilitated a better understanding of the glycoprotein contents in humans and other organisms. The public information-rich resources of protein glycosylation in a variety of different cell types and tissues have been published with the effort of many groups in this community which bring profound insights into the fundamental mechanisms of protein glycosylation in health and disease.[19,20] The maturation of glycoproteomics and glycomics has also facilitated the identification of glycopeptides in a variety of diseases including neurodegenerative disease,[21,22] cancer,[23–25] and infectious disease.[26–28] In this special issue, we have collected the contributions of a bioinformatics tool of annotation of intact glycopeptides,[29] a