Protein Glycosylation in Cancer - Molecular Aspects and Clinical Application

Protein glycosylation alterations in cancer have been recognized for their potential as a diagnostic tool. This review aims to explore the structural diversity and functional significance of glycans, as well as the relationship between aberrant glycosylation and cancer. Currently used glycomic biomarkers and their translational features in selected types of cancer are described in detail. The potential of liquid biopsy glycomics as an oncological tool is discussed, presenting different analytical strategies for glycan analysis, including total serum N-glycan analysis, O-glycosylation, and proteoglycan analysis. These strategies utilize chromatographic methods and high-resolution mass spectrometry, offering high precision and useful information. Other approaches include in situ fluorescence imaging, as well as lectin- and antibody-based methods for the detection of specific glycoforms, which have gained attention for their relative simplicity in use and clinical interpretation. With the rapid development of novel technologies for glycan detection and characterization, as well as bioinformatics tools and databases, it is expected that exploring the molecular mechanisms of glycosylation in cancer will become more accessible in everyday clinical implementation. Integrating knowledge of altered glycosylation patterns, proteomics, genomics, and metabolomics (and other omics approaches) with clinical data has potential to contribute to a more comprehensive biomolecular characterization of malignant diseases.