Human biofluids are often used to discover disease-specific glycosylation, since abnormal changes in protein glycosylation can discern physiopathological states. Highly
glycosylated proteins in biofluids make it possible to identify disease signatures. Glycoproteomic studies on saliva
glycoproteins showed that fucosylation was significantly increased during
tumorigenesis and that
glycoproteins became hyperfucosylated in lung
metastases, and
tumor stage is associated with fucosylation. Quantification of salivary fucosylation can be achieved by mass spectrometric analysis of fucosylated
glycoproteins or fucosylated
glycans; however, the use of mass spectrometry is non-trivial for clinical practice. Here, we developed a high-throughput quantitative method,
lectin-affinity fluorescent labeling quantification (LAFLQ), to quantify fucosylated
glycoproteins without relying on mass spectrometry.
Lectins with a specific affinity for fucoses are immobilized on the resin and effectively capture fluorescently labeled fucosylated
glycoproteins, which are further quantitatively characterized by fluorescence detection in a 96-well plate. Our results demonstrated that serum
IgG can be accurately quantified by
lectin and fluorescence detection. Quantification in saliva showed significantly higher fucosylation in
lung cancer patients compared to healthy controls or other non-
cancer diseases, suggesting that this method has the potential to quantify stage-related fucosylation in
lung cancer saliva.