Alterations in protein expression and site-specific N-glycosylation of prostate cancer tissues
Abstract Identifying molecular alterations occurring during cancer progression is essential for a deeper understanding of the underlying biological processes. Here we have analyzed cancerous and healthy prostate biopsies using nanoLC-MS(MS) to detect proteins with altered expression and N-glycosylat...
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Nature Portfolio
2021
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oai:doaj.org-article:558734aa26ea49b1b1b8c749c90177ec2021-12-02T16:36:37ZAlterations in protein expression and site-specific N-glycosylation of prostate cancer tissues10.1038/s41598-021-95417-52045-2322https://doaj.org/article/558734aa26ea49b1b1b8c749c90177ec2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-95417-5https://doaj.org/toc/2045-2322Abstract Identifying molecular alterations occurring during cancer progression is essential for a deeper understanding of the underlying biological processes. Here we have analyzed cancerous and healthy prostate biopsies using nanoLC-MS(MS) to detect proteins with altered expression and N-glycosylation. We have identified 75 proteins with significantly changing expression during disease progression. The biological processes involved were assigned based on protein–protein interaction networks. These include cellular component organization, metabolic and localization processes. Multiple glycoproteins were identified with aberrant glycosylation in prostate cancer, where differences in glycosite-specific sialylation, fucosylation, and galactosylation were the most substantial. Many of the glycoproteins with altered N-glycosylation were extracellular matrix constituents, and are heavily involved in the establishment of the tumor microenvironment.Simon SugárGábor TóthFanni BugyiKároly VékeyKatalin KarásziLászló DrahosLilla TuriákNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021) |
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Medicine R Science Q Simon Sugár Gábor Tóth Fanni Bugyi Károly Vékey Katalin Karászi László Drahos Lilla Turiák Alterations in protein expression and site-specific N-glycosylation of prostate cancer tissues |
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Abstract Identifying molecular alterations occurring during cancer progression is essential for a deeper understanding of the underlying biological processes. Here we have analyzed cancerous and healthy prostate biopsies using nanoLC-MS(MS) to detect proteins with altered expression and N-glycosylation. We have identified 75 proteins with significantly changing expression during disease progression. The biological processes involved were assigned based on protein–protein interaction networks. These include cellular component organization, metabolic and localization processes. Multiple glycoproteins were identified with aberrant glycosylation in prostate cancer, where differences in glycosite-specific sialylation, fucosylation, and galactosylation were the most substantial. Many of the glycoproteins with altered N-glycosylation were extracellular matrix constituents, and are heavily involved in the establishment of the tumor microenvironment. |
format |
article |
author |
Simon Sugár Gábor Tóth Fanni Bugyi Károly Vékey Katalin Karászi László Drahos Lilla Turiák |
author_facet |
Simon Sugár Gábor Tóth Fanni Bugyi Károly Vékey Katalin Karászi László Drahos Lilla Turiák |
author_sort |
Simon Sugár |
title |
Alterations in protein expression and site-specific N-glycosylation of prostate cancer tissues |
title_short |
Alterations in protein expression and site-specific N-glycosylation of prostate cancer tissues |
title_full |
Alterations in protein expression and site-specific N-glycosylation of prostate cancer tissues |
title_fullStr |
Alterations in protein expression and site-specific N-glycosylation of prostate cancer tissues |
title_full_unstemmed |
Alterations in protein expression and site-specific N-glycosylation of prostate cancer tissues |
title_sort |
alterations in protein expression and site-specific n-glycosylation of prostate cancer tissues |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/558734aa26ea49b1b1b8c749c90177ec |
work_keys_str_mv |
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