Use of Lectin-based Affinity Techniques in Breast Cancer Glycoproteomics: A Review

Abstract

Changes in glycoprotein content, altered glycosylations, and aberrant glycan structures are increasingly recognized as cancer hallmarks. Because breast cancer is one of the most common causes of cancer deaths in the world, it is highly urgent to find other reliable biomarkers for its initial diagnosis and to learn as much as possible about this disease. In this Review, the applications of lectins to a screening of potential breast cancer biomarkers published during recent years are overviewed. These data provide a deeper insight into the use of modern strategies, technologies, and scientific knowledge in glycoproteomic breast cancer research. Particular attention is concentrated on the use of lectin-based affinity techniques, applied independently or most frequently in combination with mass spectrometry, as an effective tool for the targeting, separation, and reliable identification of glycoprotein molecules. Individual procedures and lectins used in published glycoproteomic studies of breast-cancer-related glycoproteins are discussed. The summarized approaches have the potential for use in diagnostic and predictive applications. Finally, the use of lectins is briefly discussed from the view of their future applications in the analysis of glycoproteins in cancer.

The possible association of clusterin fucosylation changes with male fertility disorders

“…It is consistent with the specificity of LTA, which detects fucose linked to galactose via α1,3 glycosidic bound, present in the antennary part of N-glycans, forming Le x oligosaccharide structure, and with the biological function of FUT4, which is responsible for i.a. Le x glycan structures formation 26 , 28 .…”

“…The specificity of lectins is not absolute, and they can react with more than one oligosaccharide residue. Lotus tetragonolobus agglutinin and Ulex europaeus agglutinin detect fucoses linked to the galactose or antennary N-acetylglucosamine by α1,3 glycosidic bond and α1,2 glycosidic bond, respectively 28 . Lens culinaris agglutinin was used for core fucose detection 29 .…”

A Two-Dimensional Affinity Capture and Separation Mini-Platform for the Isolation, Enrichment, and Quantification of Biomarkers and Its Potential Use for Liquid Biopsy

“…They are used as an effective tool for the targeting, separation, and reliable identification of glycoprotein molecules. Their importance stems from the understanding that changes in glycoprotein and glycopeptide content, altered glycosylations, and aberrant glycan structures are increasingly recognized as cancer hallmarks [ 162 , 163 , 164 , 165 ].…”

Recent advancements in glycoproteomic studies: Glycopeptide enrichment and derivatization, characterization of glycosylation in SARS CoV2, and interacting glycoproteins

“…Also, each type is associated with a specific linkage type. For N-glycosylation, the sugar is linked to the amide of asparagine (Asn), whereas for O-glycosylation, the sugar is attached through the hydroxyl of threonine (Thr), serine, or hydroxylysine (Lastovickova et al, 2020). Studying the glycoproteome becomes important because the same protein with the same glycosylation site(s) may have variable glycan compositions and linkage patterns.…”