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Epigenetic Regulation of Glycosylation in Cancer and Other Diseases

In the last few decades, the newly emerging field of epigenetic regulation of glycosylation acquired more importance because it is unraveling physiological and pathological mechanisms related to glycan functions. Glycosylation is a complex process in which proteins and lipids are modified by the att...

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Detalles Bibliográficos
Autores principales: Indellicato, Rossella, Trinchera, Marco
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7999748/
https://www.ncbi.nlm.nih.gov/pubmed/33804149
http://dx.doi.org/10.3390/ijms22062980
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author Indellicato, Rossella
Trinchera, Marco
author_facet Indellicato, Rossella
Trinchera, Marco
author_sort Indellicato, Rossella
collection PubMed
description In the last few decades, the newly emerging field of epigenetic regulation of glycosylation acquired more importance because it is unraveling physiological and pathological mechanisms related to glycan functions. Glycosylation is a complex process in which proteins and lipids are modified by the attachment of monosaccharides. The main actors in this kind of modification are the glycoenzymes, which are translated from glycosylation-related genes (or glycogenes). The expression of glycogenes is regulated by transcription factors and epigenetic mechanisms (mainly DNA methylation, histone acetylation and noncoding RNAs). This review focuses only on these last ones, in relation to cancer and other diseases, such as inflammatory bowel disease and IgA1 nephropathy. In fact, it is clear that a deeper knowledge in the fine-tuning of glycogenes is essential for acquiring new insights in the glycan field, especially if this could be useful for finding novel and personalized therapeutics.
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spelling pubmed-79997482021-03-28 Epigenetic Regulation of Glycosylation in Cancer and Other Diseases Indellicato, Rossella Trinchera, Marco Int J Mol Sci Review In the last few decades, the newly emerging field of epigenetic regulation of glycosylation acquired more importance because it is unraveling physiological and pathological mechanisms related to glycan functions. Glycosylation is a complex process in which proteins and lipids are modified by the attachment of monosaccharides. The main actors in this kind of modification are the glycoenzymes, which are translated from glycosylation-related genes (or glycogenes). The expression of glycogenes is regulated by transcription factors and epigenetic mechanisms (mainly DNA methylation, histone acetylation and noncoding RNAs). This review focuses only on these last ones, in relation to cancer and other diseases, such as inflammatory bowel disease and IgA1 nephropathy. In fact, it is clear that a deeper knowledge in the fine-tuning of glycogenes is essential for acquiring new insights in the glycan field, especially if this could be useful for finding novel and personalized therapeutics. MDPI 2021-03-15 /pmc/articles/PMC7999748/ /pubmed/33804149 http://dx.doi.org/10.3390/ijms22062980 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Indellicato, Rossella
Trinchera, Marco
Epigenetic Regulation of Glycosylation in Cancer and Other Diseases
title Epigenetic Regulation of Glycosylation in Cancer and Other Diseases
title_full Epigenetic Regulation of Glycosylation in Cancer and Other Diseases
title_fullStr Epigenetic Regulation of Glycosylation in Cancer and Other Diseases
title_full_unstemmed Epigenetic Regulation of Glycosylation in Cancer and Other Diseases
title_short Epigenetic Regulation of Glycosylation in Cancer and Other Diseases
title_sort epigenetic regulation of glycosylation in cancer and other diseases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7999748/
https://www.ncbi.nlm.nih.gov/pubmed/33804149
http://dx.doi.org/10.3390/ijms22062980
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