Figures & data
Table 1. Applications of CCA-associated glycans and specific lectins in CCA
Figure 1. Schematic diagram for biosynthesis of CCA-associated glycans
Alteration of glycosylation in CCA leads to the expression of CCA-associated glycans that are potentially used as the targets for CCA treatment and as the biomarkers for diagnosis and prognostic prediction of CCA. After the protein is translated from mRNA, several nucleocytoplasmic proteins, such as transcription factors, are possibly modified by N-acetylglucosamine (GlcNAc) under the control of O-GlcNAc transferase (OGT) then translocated into the nucleus. The synthesis of mucin-type O-glycans, serine, or threonine residue was initially modified with N-acetylgalactosamine (GalNAc) by GalNAc-transferases (GalNTs), followed by the stepwise glycan extension. Terminal glycosylation with fucose or sialic acids was regulated by fucosyltransferases (FUTs) and sialyltransferases (STs). After complete glycosylation, the glycoproteins were transferred to the cell membrane or secreted out of the cells. Several CCA-associated glycans were found to be the potential targets for CCA treatment. O-GalNAc, O-GlcNAc, and fucosylated glycans were found to participate in metastasis, while sialylated glycan was identified to involve in chemoresistance of CCA. The secreted CCA-associated glycans were applicable as the glycobiomarker for diagnosis and prognostic prediction of CCA.
Table 2. Examples of glycosylation inhibitors