The role and potential mechanism of O-Glycosylation in gastrointestinal tumors

Abstract

Glycosylation is a critical post-translational modification (PTM) that affects the function of proteins and regulates cell signaling, thereby regulating various biological processes. Protein oxygen-N-acetylglucosamine (O-GlcNAc) glycosylation modifications are glycochemical modifications that occur within cells in the signal transduction and are frequently found in the cytoplasm and nucleus. Due to the rapid and reversible addition and removal, O-GlcNAc modifications are able to reversibly compete with certain phosphorylation modifications, immediately regulate the activity of proteins, and participate in kinds of cellular metabolic and signal transduction pathways, playing a pivotal role in the regulation of tumors, diabetes, and other diseases. This article provided a brief overview of O-GlcNAc glycosylation modification, introduced its role in altering the progression and immune response regulation of gastrointestinal tumors, and discussed its potential use as a marker of tumor neogenesis.

Keywords: CA(PubChem CID:6918774); GFAT(PubChem CID:381121321); Gastrointestinal tumor; Glycosylation modification; Luteolin(PubChem CID:5280445); Natural products; O-GlcNAc; O-GlcNAc modified regulator; OGA(PubChem CID:405229538); OGT(PubChem CID:405228932); Quercetin (PubChem CID:5280343); Resveratrol(PubChem CID:445154); Tumor biomarker; UDP-GlcNAc(PubChem CID:445675).