Pan‐cancer analysis of altered glycosyltransferases confers poor clinical outcomes

Abstract

Glycosylation is a post-translational modification (PTM) process that attaches carbohydrates to proteins and lipids. Protein glycosylation can be N-linked or O-linked depending on adding sugars onto the side chains of Asn or Ser/Thr residues, respectively. PTM comprises glycan-modifying enzymes glycosyltransferases (GTs) and glycosidases. Oglycan truncation, N-glycan branching, sialylation and fucosylation are the most well-known cancer-associated glycosylations. The glycan-modifying enzymes stimulate various malignant behaviours of tumours, such as tumour proliferation, invasion, epithelial-mesenchymal transition, metastasis, angiogenesis, immune modulation and cellmatrix interactions. 1,2 Over 200 GTs regulate glycosylation. An unbiased global approach must be used to identify glycogenes in cancer. In this study, Li et al. 3 (2022) investigated the fascinating examination of GTs in pan-cancer using bioinformatics investigation from CCLE, TCGA,This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.