ArticleACS omega2022
Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy.
Article in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Sialylation and fucosylation of mucin-type glycopeptides using recombinant glycosyltransferases.Methods in enzymology · 2026Article
- O-glycosylation in Cancer: Emerging Paradigms and Prospects for Precision Oncology.International journal of biological sciences · 2026Review
- Mass Spectrometry-Based Comparative Analysis ofACS chemical neuroscience · 2025Article
- Quantitative proteomic and glycoproteomic analysis identifies CLCA1, FBN1, and FGB as potential biomarkers for ulcerative colitis.RSC advances · 2025Article
- Post-translational modifications of protein and lung cancer.Frontiers in oncology · 2025Review
- FUT2 promotes the tumorigenicity and metastasis of colorectal cancer cells via the Wnt/β‑catenin pathway.International journal of oncology · 2023Article
- Quantitative analysis of fucosylated glycoproteins by immobilized lectin-affinity fluorescent labeling.RSC advances · 2023Article
- Recent development of analytical methods for disease-specific proteinRSC advances · 2022Review
- Protein glycosylation in lung cancer from a mass spectrometry perspective.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
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