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Profiling of different pancreatic cancer cells used as models for metastatic behaviour shows large variation in their N-glycosylation
To characterise pancreatic cancer cells from different sources which are used as model systems to study the metastatic behaviour in pancreatic ductal adenocarcinoma (PDAC), we compared the N-glycan imprint of four PDAC cells which were previously shown to differ in their galectin-4 expression and me...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5709460/ https://www.ncbi.nlm.nih.gov/pubmed/29192278 http://dx.doi.org/10.1038/s41598-017-16811-6 |
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author | Holst, Stephanie Belo, Ana I. Giovannetti, Elisa van Die, Irma Wuhrer, Manfred |
author_facet | Holst, Stephanie Belo, Ana I. Giovannetti, Elisa van Die, Irma Wuhrer, Manfred |
author_sort | Holst, Stephanie |
collection | PubMed |
description | To characterise pancreatic cancer cells from different sources which are used as model systems to study the metastatic behaviour in pancreatic ductal adenocarcinoma (PDAC), we compared the N-glycan imprint of four PDAC cells which were previously shown to differ in their galectin-4 expression and metastatic potential in vivo. Next to the sister cell lines Pa-Tu-8988S and Pa-Tu-8988T, which were isolated from the same liver metastasis of a PDAC, this included two primary PDAC cell cultures, PDAC1 and PDAC2. Additionally, we extended the N-glycan profiling to a normal, immortalized pancreatic duct cell line. Our results revealed major differences in the N-glycosylation of the different PDAC cells as well as compared to the control cell line, suggesting changes of the N-glycosylation in PDAC. The N-glycan profiles of the PDAC cells, however, differed vastly as well and demonstrate the diversity of PDAC model systems, which ultimately affects the interpretation of functional studies. The results from this study form the basis for further biological evaluation of the role of protein glycosylation in PDAC and highlight that conclusions from one cell line cannot be generalised, but should be regarded in the context of the corresponding phenotype. |
format | Online Article Text |
id | pubmed-5709460 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-57094602017-12-06 Profiling of different pancreatic cancer cells used as models for metastatic behaviour shows large variation in their N-glycosylation Holst, Stephanie Belo, Ana I. Giovannetti, Elisa van Die, Irma Wuhrer, Manfred Sci Rep Article To characterise pancreatic cancer cells from different sources which are used as model systems to study the metastatic behaviour in pancreatic ductal adenocarcinoma (PDAC), we compared the N-glycan imprint of four PDAC cells which were previously shown to differ in their galectin-4 expression and metastatic potential in vivo. Next to the sister cell lines Pa-Tu-8988S and Pa-Tu-8988T, which were isolated from the same liver metastasis of a PDAC, this included two primary PDAC cell cultures, PDAC1 and PDAC2. Additionally, we extended the N-glycan profiling to a normal, immortalized pancreatic duct cell line. Our results revealed major differences in the N-glycosylation of the different PDAC cells as well as compared to the control cell line, suggesting changes of the N-glycosylation in PDAC. The N-glycan profiles of the PDAC cells, however, differed vastly as well and demonstrate the diversity of PDAC model systems, which ultimately affects the interpretation of functional studies. The results from this study form the basis for further biological evaluation of the role of protein glycosylation in PDAC and highlight that conclusions from one cell line cannot be generalised, but should be regarded in the context of the corresponding phenotype. Nature Publishing Group UK 2017-11-30 /pmc/articles/PMC5709460/ /pubmed/29192278 http://dx.doi.org/10.1038/s41598-017-16811-6 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Holst, Stephanie Belo, Ana I. Giovannetti, Elisa van Die, Irma Wuhrer, Manfred Profiling of different pancreatic cancer cells used as models for metastatic behaviour shows large variation in their N-glycosylation |
title | Profiling of different pancreatic cancer cells used as models for metastatic behaviour shows large variation in their N-glycosylation |
title_full | Profiling of different pancreatic cancer cells used as models for metastatic behaviour shows large variation in their N-glycosylation |
title_fullStr | Profiling of different pancreatic cancer cells used as models for metastatic behaviour shows large variation in their N-glycosylation |
title_full_unstemmed | Profiling of different pancreatic cancer cells used as models for metastatic behaviour shows large variation in their N-glycosylation |
title_short | Profiling of different pancreatic cancer cells used as models for metastatic behaviour shows large variation in their N-glycosylation |
title_sort | profiling of different pancreatic cancer cells used as models for metastatic behaviour shows large variation in their n-glycosylation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5709460/ https://www.ncbi.nlm.nih.gov/pubmed/29192278 http://dx.doi.org/10.1038/s41598-017-16811-6 |
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