Cargando…
Cell Surface-Specific N-Glycan Profiling in Breast Cancer
Aberrant changes in specific glycans have been shown to be associated with immunosurveillance, tumorigenesis, tumor progression and metastasis. In this study, the N-glycan profiling of membrane proteins from human breast cancer cell lines and tissues was detected using modified DNA sequencer-assiste...
Autores principales: | , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3751845/ https://www.ncbi.nlm.nih.gov/pubmed/24009699 http://dx.doi.org/10.1371/journal.pone.0072704 |
_version_ | 1782281682275008512 |
---|---|
author | Liu, Xia Nie, Huan Zhang, Yubao Yao, Yuanfei Maitikabili, Alaiyi Qu, Youpeng Shi, Shuliang Chen, Cuiying Li, Yu |
author_facet | Liu, Xia Nie, Huan Zhang, Yubao Yao, Yuanfei Maitikabili, Alaiyi Qu, Youpeng Shi, Shuliang Chen, Cuiying Li, Yu |
author_sort | Liu, Xia |
collection | PubMed |
description | Aberrant changes in specific glycans have been shown to be associated with immunosurveillance, tumorigenesis, tumor progression and metastasis. In this study, the N-glycan profiling of membrane proteins from human breast cancer cell lines and tissues was detected using modified DNA sequencer-assisted fluorophore-assisted carbohydrate electrophoresis (DSA-FACE). The N-glycan profiles of membrane proteins were analyzed from 7 breast cancer cell lines and MCF 10A, as well as from 100 pairs of breast cancer and corresponding adjacent tissues. The results showed that, compared with the matched adjacent normal tissue samples, two biantennary N-glycans (NA2 and NA2FB) were significantly decreased (p <0.0001) in the breast cancer tissue samples, while the triantennary glycan (NA3FB) and a high-mannose glycan (M8) were dramatically increased (p = 0.001 and p <0.0001, respectively). Moreover, the alterations in these specific N-glycans occurred through the oncogenesis and progression of breast cancer. These results suggested that the modified method based on DSA-FACE is a high-throughput detection technology that is suited for analyzing cell surface N-glycans. These cell surface-specific N-glycans may be helpful in recognizing the mechanisms of tumor cell immunologic escape and could be potential targets for new breast cancer drugs. |
format | Online Article Text |
id | pubmed-3751845 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-37518452013-09-05 Cell Surface-Specific N-Glycan Profiling in Breast Cancer Liu, Xia Nie, Huan Zhang, Yubao Yao, Yuanfei Maitikabili, Alaiyi Qu, Youpeng Shi, Shuliang Chen, Cuiying Li, Yu PLoS One Research Article Aberrant changes in specific glycans have been shown to be associated with immunosurveillance, tumorigenesis, tumor progression and metastasis. In this study, the N-glycan profiling of membrane proteins from human breast cancer cell lines and tissues was detected using modified DNA sequencer-assisted fluorophore-assisted carbohydrate electrophoresis (DSA-FACE). The N-glycan profiles of membrane proteins were analyzed from 7 breast cancer cell lines and MCF 10A, as well as from 100 pairs of breast cancer and corresponding adjacent tissues. The results showed that, compared with the matched adjacent normal tissue samples, two biantennary N-glycans (NA2 and NA2FB) were significantly decreased (p <0.0001) in the breast cancer tissue samples, while the triantennary glycan (NA3FB) and a high-mannose glycan (M8) were dramatically increased (p = 0.001 and p <0.0001, respectively). Moreover, the alterations in these specific N-glycans occurred through the oncogenesis and progression of breast cancer. These results suggested that the modified method based on DSA-FACE is a high-throughput detection technology that is suited for analyzing cell surface N-glycans. These cell surface-specific N-glycans may be helpful in recognizing the mechanisms of tumor cell immunologic escape and could be potential targets for new breast cancer drugs. Public Library of Science 2013-08-23 /pmc/articles/PMC3751845/ /pubmed/24009699 http://dx.doi.org/10.1371/journal.pone.0072704 Text en © 2013 Liu et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Liu, Xia Nie, Huan Zhang, Yubao Yao, Yuanfei Maitikabili, Alaiyi Qu, Youpeng Shi, Shuliang Chen, Cuiying Li, Yu Cell Surface-Specific N-Glycan Profiling in Breast Cancer |
title | Cell Surface-Specific N-Glycan Profiling in Breast Cancer |
title_full | Cell Surface-Specific N-Glycan Profiling in Breast Cancer |
title_fullStr | Cell Surface-Specific N-Glycan Profiling in Breast Cancer |
title_full_unstemmed | Cell Surface-Specific N-Glycan Profiling in Breast Cancer |
title_short | Cell Surface-Specific N-Glycan Profiling in Breast Cancer |
title_sort | cell surface-specific n-glycan profiling in breast cancer |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3751845/ https://www.ncbi.nlm.nih.gov/pubmed/24009699 http://dx.doi.org/10.1371/journal.pone.0072704 |
work_keys_str_mv | AT liuxia cellsurfacespecificnglycanprofilinginbreastcancer AT niehuan cellsurfacespecificnglycanprofilinginbreastcancer AT zhangyubao cellsurfacespecificnglycanprofilinginbreastcancer AT yaoyuanfei cellsurfacespecificnglycanprofilinginbreastcancer AT maitikabilialaiyi cellsurfacespecificnglycanprofilinginbreastcancer AT quyoupeng cellsurfacespecificnglycanprofilinginbreastcancer AT shishuliang cellsurfacespecificnglycanprofilinginbreastcancer AT chencuiying cellsurfacespecificnglycanprofilinginbreastcancer AT liyu cellsurfacespecificnglycanprofilinginbreastcancer |