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Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy
[Image: see text] 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, t...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9161393/ https://www.ncbi.nlm.nih.gov/pubmed/35664632 http://dx.doi.org/10.1021/acsomega.2c01193 |
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author | Gao, Ziyuan Wu, Zhen Han, Ying Zhang, Xumin Hao, Piliang Xu, Mingming Huang, Shan Li, Shuwei Xia, Jun Jiang, Junhong Yang, Shuang |
author_facet | Gao, Ziyuan Wu, Zhen Han, Ying Zhang, Xumin Hao, Piliang Xu, Mingming Huang, Shan Li, Shuwei Xia, Jun Jiang, Junhong Yang, Shuang |
author_sort | Gao, Ziyuan |
collection | PubMed |
description | [Image: see text] 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. |
format | Online Article Text |
id | pubmed-9161393 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-91613932022-06-03 Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy Gao, Ziyuan Wu, Zhen Han, Ying Zhang, Xumin Hao, Piliang Xu, Mingming Huang, Shan Li, Shuwei Xia, Jun Jiang, Junhong Yang, Shuang ACS Omega [Image: see text] 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. American Chemical Society 2022-05-19 /pmc/articles/PMC9161393/ /pubmed/35664632 http://dx.doi.org/10.1021/acsomega.2c01193 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Gao, Ziyuan Wu, Zhen Han, Ying Zhang, Xumin Hao, Piliang Xu, Mingming Huang, Shan Li, Shuwei Xia, Jun Jiang, Junhong Yang, Shuang Aberrant Fucosylation of Saliva Glycoprotein Defining Lung Adenocarcinomas Malignancy |
title | Aberrant Fucosylation of Saliva Glycoprotein Defining
Lung Adenocarcinomas Malignancy |
title_full | Aberrant Fucosylation of Saliva Glycoprotein Defining
Lung Adenocarcinomas Malignancy |
title_fullStr | Aberrant Fucosylation of Saliva Glycoprotein Defining
Lung Adenocarcinomas Malignancy |
title_full_unstemmed | Aberrant Fucosylation of Saliva Glycoprotein Defining
Lung Adenocarcinomas Malignancy |
title_short | Aberrant Fucosylation of Saliva Glycoprotein Defining
Lung Adenocarcinomas Malignancy |
title_sort | aberrant fucosylation of saliva glycoprotein defining
lung adenocarcinomas malignancy |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9161393/ https://www.ncbi.nlm.nih.gov/pubmed/35664632 http://dx.doi.org/10.1021/acsomega.2c01193 |
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