Glycosylation modification of proteins is a common type of post-translational modification that affects the function of more than half of known eukaryotic proteins. Abnormal glycosylation of proteins is a common feature of malignant tumors and often leads to abnormalities in the structure and content of glycolipids and glycoproteins in a variety of ways such as gene 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 the malignant progression of cancer. Due to the high malignancy and poor prognosis of glioma， it is urgent to search for key molecular events in the malignant progression of glioma. Numerous studies have shown that abnormal glycosylation of proteins plays a crucial role in the development， progression， and poor prognosis of glioma， while glycation associated with glioma has been extensively studied in early diagnosis and treatment. Therefore， this article mainly introduces three forms of glioma-associated glycosylation， i.e.， N-linked glycosylation， O-linked glycosylation， and glycosylphosphatidyl inositol （GPI） anchor， elaborates on their mechanisms of occurrence and specific mechanisms of action， and explores the clinical potential of abnormal glycosylation in the identification and treatment of glioma， so as to provide a theoretical basis for addressing the current situation of the poor prognosis of glioma.