J Cancer 2021; 12(5):1455-1466. doi:10.7150/jca.51604 This issue
1. Oral Disease Research Key Laboratory of Guizhou Tertiary Institution, School of Stomatology, Zunyi Medical University, Zunyi 563006, China.
2. Department of Gastroenterology, Affiliated Hospital of Zunyi Medical University, Zunyi 563000, China.
3. Microbial Resources and Drug Development Key Laboratory of Guizhou Tertiary Institution, Life Sciences Institute, Zunyi Medical University, Zunyi 563006, China.
Glycosylation is an important posttranslational modification of proteins, and it has a profound influence on diverse life processes. An abnormal polysaccharide structure and mutation of the glycosylation pathway are closely correlated with human cancer progression. Glycoproteins such as EGFR, E-cadherin, CD44, PD-1/PD-L1, B7-H3 and Muc1 play important roles in the progression of head and neck squamous cell carcinoma (HNSCC), and their levels of glycosylation and changes in glycosyl structure are closely linked to HNSCC progression and malignant transformation. The regulation of protein glycosylation in HNSCC provides potential strategies to control cancer stem cell (CSC) subgroup expansion, epithelial-mesenchymal transition (EMT), tumor-related immunity escape and autophagy. Glycoproteins with altered glycosylation can be used as biomarkers for the early diagnosis, monitoring and prognostication of HNSCC. However, the glycobiology of cancer is still a new field that needs to be deeply studied, especially in HNSCC.
Keywords: Glycosylation, HNSCC, EGFR, E-Cadherin, CD44, PD-1/PD-L1, B7-H3, Muc1