Open AccessAberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy
Author(s) -
Ziyuan Gao,
Zhen Wu,
Ying Han,
Xumin Zhang,
Piliang Hao,
Mingming Xu,
Shan Huang,
Shuwei Li,
Jun Xia,
JianHua Jiang,
Shuang Yang
Publication year - 2022
Publication title -
acs omega
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.779
H-Index - 40
ISSN - 2470-1343
DOI - 10.1021/acsomega.2c01193
Subject(s) - fucosylation , saliva , glycoprotein , glycosylation , mucin , lung cancer , cancer research , cancer , carcinogenesis , immunology , biology , medicine , chemistry , microbiology and biotechnology , fucose , biochemistry
Aberrant glycosylation is a hallmark of cancer found during tumorigenesis and tumor progression. Lung cancer (LC) induced by oncogene mutations has been detected in the patient's saliva, and saliva glycosylation has been altered. Saliva contains highly glycosylated glycoproteins, the characteristics of which may be related to various diseases. Therefore, elucidating cancer-specific glycosylation in the saliva of healthy, non-cancer, and cancer patients can reveal whether tumor glycosylation has unique characteristics for early diagnosis. In this work, we used a solid-phase chemoenzymatic method to study the glycosylation of saliva glycoproteins in clinical specimens. The results showed that the α1,6-core fucosylation of glycoproteins was increased in cancer patients, whereas α1,2 or α1,3 fucosylation was significantly increased. We further analyzed the expression of fucosyltransferases responsible for α1,2, α1,3, and α1,6 fucosylation. The fucosylation of the saliva of cancer patients is drastically different from that of non-cancer or health controls. These results indicate that the glycoform of saliva fucosylation distinguishes LC from other diseases, and this feature has the potential to diagnose lung adenocarcinoma.