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Involvement of Aberrant Glycosylation in Thyroid Cancer
Glycosylation is one of the most common posttranslational modification reactions and nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in oligosaccharides structures are associated with many physiological and pathological events, including cell growth, migration and...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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Hindawi Publishing Corporation
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2906155/ https://www.ncbi.nlm.nih.gov/pubmed/20652009 http://dx.doi.org/10.1155/2010/816595 |
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author | Miyoshi, Eiji Ito, Yasuhiro Miyoshi, Yoko |
author_facet | Miyoshi, Eiji Ito, Yasuhiro Miyoshi, Yoko |
author_sort | Miyoshi, Eiji |
collection | PubMed |
description | Glycosylation is one of the most common posttranslational modification reactions and nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in oligosaccharides structures are associated with many physiological and pathological events, including cell growth, migration and differentiation, and tumor invasion. Therefore, functional glycomics, which is a comprehensive study of the structures and functions of glycans, is attracting the increasing attention of scientists in various fields of life science. In cases of thyroid cancer, the biological characters and prognosis are completely different in each type of histopathology, and their oligosaccharide structures as well as the expression of glycosyltransferases are also different. In this review, we summarized our previous papers on oligosaccharides and thyroid cancers and discussed a possible function of oligosaccharides in the carcinogenesis in thyroid cancer. |
format | Text |
id | pubmed-2906155 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-29061552010-07-22 Involvement of Aberrant Glycosylation in Thyroid Cancer Miyoshi, Eiji Ito, Yasuhiro Miyoshi, Yoko J Oncol Review Article Glycosylation is one of the most common posttranslational modification reactions and nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in oligosaccharides structures are associated with many physiological and pathological events, including cell growth, migration and differentiation, and tumor invasion. Therefore, functional glycomics, which is a comprehensive study of the structures and functions of glycans, is attracting the increasing attention of scientists in various fields of life science. In cases of thyroid cancer, the biological characters and prognosis are completely different in each type of histopathology, and their oligosaccharide structures as well as the expression of glycosyltransferases are also different. In this review, we summarized our previous papers on oligosaccharides and thyroid cancers and discussed a possible function of oligosaccharides in the carcinogenesis in thyroid cancer. Hindawi Publishing Corporation 2010 2010-06-27 /pmc/articles/PMC2906155/ /pubmed/20652009 http://dx.doi.org/10.1155/2010/816595 Text en Copyright © 2010 Eiji Miyoshi et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Miyoshi, Eiji Ito, Yasuhiro Miyoshi, Yoko Involvement of Aberrant Glycosylation in Thyroid Cancer |
title | Involvement of Aberrant Glycosylation in Thyroid Cancer |
title_full | Involvement of Aberrant Glycosylation in Thyroid Cancer |
title_fullStr | Involvement of Aberrant Glycosylation in Thyroid Cancer |
title_full_unstemmed | Involvement of Aberrant Glycosylation in Thyroid Cancer |
title_short | Involvement of Aberrant Glycosylation in Thyroid Cancer |
title_sort | involvement of aberrant glycosylation in thyroid cancer |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2906155/ https://www.ncbi.nlm.nih.gov/pubmed/20652009 http://dx.doi.org/10.1155/2010/816595 |
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