Mass Spectrometry-Based Glycoproteomic Workflows for Cancer Biomarker Discovery

Glycosylation has a clear role in cancer initiation and progression, with numerous studies identifying distinct glycan features or specific glycoproteoforms associated with cancer. Common findings include that aggressive cancers tend to have higher expression levels of enzymes that regulate glycosylation as well as glycoproteins with greater levels of complexity, increased branching, and enhanced chain length(1). Research in cancer glycoproteomics over the last 50-plus years has mainly focused on technology development used to observe global changes in glycosylation. Efforts have also been made to connect glycans to their protein carriers as well as to delineate the role of these modifications in intracellular signaling and subsequent cell function. This review discusses currently available techniques utilizing mass spectrometry-based technologies used to study glycosylation and highlights areas for future advancement.

Automated summary

Glycosylation plays a crucial role in cancer initiation and progression, with specific glycan features and glycoproteoforms associated with cancer being identified in numerous studies. Research has mainly focused on developing technologies to observe global changes in glycosylation and connecting glycans to their protein carriers, as well as understanding their role in intracellular signaling and cell function.