Salivary N-glycosylation as a biomarker of oral cancer: A pilot study

Sinevici, Nicoleta; Mittermayr, Stefan; Davey, Gavin P.; O'Sullivan, Jeff

doi:10.1093/glycob/cwz046

Cited by 19 publications

(17 citation statements)

References 20 publications

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“…The core-fucosylation of Man3 (H3N2F1) decreased slightly in LC, but the changes in H4N2F1 and H5N2F1 were negligible. The core-fucosylated high-mannose (H3N2F1) was found in human saliva, 55 and their possible biosynthetic pathways may involve FUT8 and α-mannosidase I. 56 Compared with those in HC, the OD of fucosylated high-mannoses is significantly reduced.…”

Section: Resultsmentioning

confidence: 99%

Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy

Gao

Han

et al. 2022

ACS Omega

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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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Section: Resultsmentioning

confidence: 99%

Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy

Gao

Han

et al. 2022

ACS Omega

View full text Add to dashboard Cite

show abstract

“…The core-fucosylation of Man3 (H3N2F1) decreased slightly in LC, but the changes in H4N2F1 and H5N2F1 were negligible. The core-fucosylated high-mannose (H3N2F1) was found in human saliva (Sinevici et al , 2019), and their possible biosynthetic pathways may involve FUT8 and α-mannosidase I (Nanno et al , 2020). Compared with those in HC, the OD of fucosylated high-mannoses is significantly reduced.…”

Section: Resultsmentioning

confidence: 99%

Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy

Yang

Gao

et al. 2021

Preprint

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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.

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“…Accumulating evidences have indicated that aberrant N-glycosylation occurs frequently in tumors and is closely associated with cancer metastasis ( 37 – 39 ). Our previous studies indicated that TIM-4 overexpression significantly promoted EMT process of NSCLC cells ( 26 ).…”

Section: Discussionmentioning

confidence: 99%

N-Glycosylation at Asn291 Stabilizes TIM-4 and Promotes the Metastasis of NSCLC

Chen

Wang

et al. 2022

Front. Oncol.

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T-cell immunoglobulin domain and mucin domain 4 (TIM-4) is a transmembrane protein that promotes epithelial-mesenchymal transition (EMT), migration and invasion of non-small cell lung cancer (NSCLC) cells. Most transmembrane proteins are modified by N-glycosylation and the importance of protein N-glycosylation in cancer cell metastasis has been well appreciated. However, whether TIM-4 is modified by N-glycosylation and the role of TIM-4 N-glycosylation in NSCLC remains largely unknown. In the current study, we reported that TIM-4 was extensively N-glycosylated at Asn291. After the removal of N-glycosylation, the stability of TIM-4 protein was decreased and TIM-4 was more susceptible to degradation by ER-localized ubiquitin ligase-mediated ERAD. Thus, the expression of TIM-4 on the cell surface was decreased, which suppressed TIM-4-mediated metastasis in NSCLC. In summary, the present study identifies TIM-4 N-glycosylation and its role in NSCLS migration, which would provide a valuable biomarker for developing drugs targeting N-glycosylation at Asn291 on TIM-4.

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Salivary N-glycosylation as a biomarker of oral cancer: A pilot study

Cited by 19 publications

References 20 publications

Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy

Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy

Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy

N-Glycosylation at Asn291 Stabilizes TIM-4 and Promotes the Metastasis of NSCLC

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