Abstract
Cervical cancer has become the most frequent female malignancy and presents as a general health challenge in many countries undergoing economic development. Various human papillomaviruses (HPV) types have appeared as one of the most critically identifiable causes of widespread cervical cancers. Conventional cervical cytological inspection has limitations of variable sensitivity according to cervical cytology. Glycobiology has been fundamental in related exploration in various gynecologic and reproductive fields and has contributed to our understanding of cervical cancer. It is associated with altered expression of N-linked glycan as well as abnormal expression of terminal glycan structures. The analytical approaches available to determine serum and tissue glycosylation, as well as potential underlying molecular mechanisms involved in the cellular glycosylation alterations, are monitored. Moreover, cellular glycosylation influences various aspects of cervical cancer biology, ranging from cell surface expressions, cell-cell adhesion, cancer signaling, cancer diagnosis, and management. In general, discoveries in glycan profiling make it technically reproducible and affordable to perform serum glycoproteomic analyses and build on previous work exploring an expanded variety of glycosylation markers in the majority of cervical cancer patients.
Highlights
In cervical cancer, the application of virus-induced glycosylated polypeptides for vaccine purposes was first documented over four decades ago [1]
Glycosylation is found on cell surfaces and in the extracellular microenvironment mediating the nascent attachment of cell contacts involved in cell-cell interactions [3, 6]
Owing to their structural complexity and methodological difficulties, O-GlcNAcylation research has lagged behind other forms of O-linked glycosylation
Summary
The application of virus-induced glycosylated polypeptides for vaccine purposes was first documented over four decades ago [1]. Some terminal structures are specific to O-glycans, blood group antigens with terminal galactose residues and Lewis structures with one or more fucose residues are attached to glycoproteins across human red blood cells [19] Owing to their structural complexity and methodological difficulties, O-GlcNAcylation research has lagged behind other forms of O-linked glycosylation. A novel method has been developed to quantify the glycosylation changes of proteins from serum samples using reverse lectin-based ELISA assay followed by the applications of glycosylation changes in cancer patients With this method, the increased fucosylation on haptoglobin was confirmed, in early-stage ovarian cancer compared with normal or benign cases, while the sialylated expressions of haptoglobin and IgG, as well as fucosylated expressions of IgG, displayed no remarkable alterations [103]. While Stage II and III cervical cancer patients that are positive for specific AGAs against diverse glycans have better therapeutic outcome than patients negative for AGA, when they are treated with EBRT plus BT, it remains possible that other unknown factors may explain the differential impact of AGA on survival between the two therapeutic outcome [96]
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