Abnormal sialylation and fucosylation of saliva glycoproteins: Characteristics of lung cancer-specific biomarkers

Current Research in Pharmacology and Drug Discovery

Mingming Xu¹  Shuang Yue²  Huang Shan³  Jun Xia⁴  Ziyuan Gao⁴  Junhong Jiang⁴  Shuang Yang⁴ 

[1] Department of Respiratory and Critical Care Medicine, Dushu Lake Hospital to Soochow University, Suzhou, Jiangsu, 215125, China;Department of Respiratory and Critical Care Medicine, The First Affiliated Hospital of Soochow University;Suzhou Jiangsu, 215006, China;Center for Clinical Mass Spectrometry, School of Pharmaceutical Sciences, Soochow University, Jiangsu, 215123, China;

关键词: Glycoenzyme;    Glycosylation;    Saliva;    Tumor biomarker;    Mass spectrometry;   

DOI  :  

来源: DOAJ

【 摘 要 】

Dysregulated surface glycoproteins play an important role in tumor cell proliferation and progression. Abnormal glycosylation of these glycoproteins may activate tumor signal transduction and lead to tumor development. The tumor microenvironment alters its molecular composition, some of which regulate protein glycosylation biosynthesis. The glycosylation of saliva proteins in lung cancer patients is different from healthy controls, in which the glycans of cancer patients are highly sialylated and hyperfucosylated. Most studies have shown that O-glycans from cancer are truncated O-glycans, while N-glycans contain fucoses and sialic acids. Because glycosylation analysis is challenging, there are few reports on how glycosylation of saliva proteins is related to the occurrence or progression of lung cancer. In this review, we discussed glycoenzymes involved in protein glycosylation, their changes in tumor microenvironment, potential tumor biomarkers present in body fluids, and abnormal glycosylation of saliva or lung glycoproteins. We further explored the effect of glycosylation changes on tumor signal transduction, and emphasized the role of receptor tyrosine kinases in tumorigenesis and metastasis.

【 授权许可】

Unknown