Abstract:Glycosylation modification of proteins is a very common post-translational modification that affects the function of more than half of known eukaryotic proteins. Abnormal glycation of proteins is a common feature of malignant tumors. Aberrant protein glycosylation often leads to abnormalities in the structure and content of glycolipids and glycoproteins in a variety of ways, including genetic mutations in glycoproteins, changes in nucleotide sugar donors, and abnormal expression or localization of glycosyltransferases, which in turn lead to abnormal protein function and help promote malignant cancer progression. Because of the high malignancy and poor prognosis of glioma, there is an urgent need to search for key molecular events in the malignant progression of glioma. Numerous studies have found that abnormal protein glycosylation plays a crucial role in glioma development, progression and poor prognosis, while glycosylation associated with glioma has been extensively studied in early diagnosis and treatment. Therefore, this review focuses on three forms of glioma-related glycosylation, N-linked glycosylation, O-linked glycosylation and Glycosylphosphatidyl inositol (GPI) anchor, describes their mechanisms of occurrence and specific mechanisms of action, and explores the clinical potential of abnormal glycosylation in the detection and treatment of glioma, with the aim of providing a theoretical basis for addressing the current situation of poor prognosis of glioma.