Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy

Abstract

Aberrant glycosylation is a hallmark of cancer found during tumorigenesis and tumor progression. Lung cancer 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 in cancer patients was significant increased. The fucosylation of α1,2 or α1,3 is also increased in cancer patients. We further analyzed the expression of fucosyltransferases responsible for α1,2, α1,3, 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 lung cancer from other diseases, and this feature has the potential to diagnose lung adenocarcinoma.TOCFucosylation biosynthesis in lung cancer. Saliva fucosylation contains α1,2-linked, α1,3-linked, α1,6-linked fucosylation in lung cancer.

FUT2 promotes the tumorigenicity and metastasis of colorectal cancer cells via the Wnt/β‑catenin pathway

“…plays vital biological roles in tumor development (14). The overexpression of FUT7 has been shown to promote A549 cell proliferation by activating the EGFR/AKT/mTOR signaling pathway (15).…”