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Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer

Glycosylation is a common posttranslational modification on membrane-associated and secreted proteins that is of pivotal importance for regulating cell functions. Aberrant glycosylation can lead to uncontrolled cell proliferation, cell-matrix interactions, migration and differentiation, and has been...

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Autores principales: Zhang, Jing, ten Dijke, Peter, Wuhrer, Manfred, Zhang, Tao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Higher Education Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7862465/
https://www.ncbi.nlm.nih.gov/pubmed/32583064
http://dx.doi.org/10.1007/s13238-020-00741-7
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author Zhang, Jing
ten Dijke, Peter
Wuhrer, Manfred
Zhang, Tao
author_facet Zhang, Jing
ten Dijke, Peter
Wuhrer, Manfred
Zhang, Tao
author_sort Zhang, Jing
collection PubMed
description Glycosylation is a common posttranslational modification on membrane-associated and secreted proteins that is of pivotal importance for regulating cell functions. Aberrant glycosylation can lead to uncontrolled cell proliferation, cell-matrix interactions, migration and differentiation, and has been shown to be involved in cancer and other diseases. The epithelial-to-mesenchymal transition is a key step in the metastatic process by which cancer cells gain the ability to invade tissues and extravasate into the bloodstream. This cellular transformation process, which is associated by morphological change, loss of epithelial traits and gain of mesenchymal markers, is triggered by the secreted cytokine transforming growth factor-β (TGF-β). TGF-β bioactivity is carefully regulated, and its effects on cells are mediated by its receptors on the cell surface. In this review, we first provide a brief overview of major types of glycans, namely, N-glycans, O-glycans, glycosphingolipids and glycosaminoglycans that are involved in cancer progression. Thereafter, we summarize studies on how the glycosylation of TGF-β signaling components regulates TGF-β secretion, bioavailability and TGF-β receptor function. Then, we review glycosylation changes associated with TGF-β-induced epithelial-to-mesenchymal transition in cancer. Identifying and understanding the mechanisms by which glycosylation affects TGF-β signaling and downstream biological responses will facilitate the identification of glycans as biomarkers and enable novel therapeutic approaches.
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spelling pubmed-78624652021-02-16 Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer Zhang, Jing ten Dijke, Peter Wuhrer, Manfred Zhang, Tao Protein Cell Review Glycosylation is a common posttranslational modification on membrane-associated and secreted proteins that is of pivotal importance for regulating cell functions. Aberrant glycosylation can lead to uncontrolled cell proliferation, cell-matrix interactions, migration and differentiation, and has been shown to be involved in cancer and other diseases. The epithelial-to-mesenchymal transition is a key step in the metastatic process by which cancer cells gain the ability to invade tissues and extravasate into the bloodstream. This cellular transformation process, which is associated by morphological change, loss of epithelial traits and gain of mesenchymal markers, is triggered by the secreted cytokine transforming growth factor-β (TGF-β). TGF-β bioactivity is carefully regulated, and its effects on cells are mediated by its receptors on the cell surface. In this review, we first provide a brief overview of major types of glycans, namely, N-glycans, O-glycans, glycosphingolipids and glycosaminoglycans that are involved in cancer progression. Thereafter, we summarize studies on how the glycosylation of TGF-β signaling components regulates TGF-β secretion, bioavailability and TGF-β receptor function. Then, we review glycosylation changes associated with TGF-β-induced epithelial-to-mesenchymal transition in cancer. Identifying and understanding the mechanisms by which glycosylation affects TGF-β signaling and downstream biological responses will facilitate the identification of glycans as biomarkers and enable novel therapeutic approaches. Higher Education Press 2020-06-25 2021-02 /pmc/articles/PMC7862465/ /pubmed/32583064 http://dx.doi.org/10.1007/s13238-020-00741-7 Text en © The Author(s) 2020 Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Review
Zhang, Jing
ten Dijke, Peter
Wuhrer, Manfred
Zhang, Tao
Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer
title Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer
title_full Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer
title_fullStr Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer
title_full_unstemmed Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer
title_short Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer
title_sort role of glycosylation in tgf-β signaling and epithelial-to-mesenchymal transition in cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7862465/
https://www.ncbi.nlm.nih.gov/pubmed/32583064
http://dx.doi.org/10.1007/s13238-020-00741-7
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