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Gene expression of O-GlcNAc cycling enzymes in human breast cancers
O-GlcNAcylation is an abundant, dynamic, and inducible posttranslational modification in which single β-N-acetylglucosamine residues are attached by O-glycosidic linkage to serine or treonine residues. It is suggested that abnormally regulated O-GlcNAcylation may contribute to the pathology of cance...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Milan
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3295997/ https://www.ncbi.nlm.nih.gov/pubmed/21567137 http://dx.doi.org/10.1007/s10238-011-0138-5 |
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author | Krześlak, Anna Forma, Ewa Bernaciak, Magdalena Romanowicz, Hanna Bryś, Magdalena |
author_facet | Krześlak, Anna Forma, Ewa Bernaciak, Magdalena Romanowicz, Hanna Bryś, Magdalena |
author_sort | Krześlak, Anna |
collection | PubMed |
description | O-GlcNAcylation is an abundant, dynamic, and inducible posttranslational modification in which single β-N-acetylglucosamine residues are attached by O-glycosidic linkage to serine or treonine residues. It is suggested that abnormally regulated O-GlcNAcylation may contribute to the pathology of cancer. Cycling of O-GlcNAc residues on intracellular proteins is controlled by two enzymes, O-GlcNAc transferease (OGT), which catalyses the addition of O-GlcNAc residues and nucleocytoplasmic β-N-acetylglucosaminidase (O-GlcNAcase; encoded by MGEA5 gene), an enzyme involved in the removal of O-GlcNAc. In this study, relationship between the mRNA expressions of genes coding O-GlcNAc cycling enzymes in breast ductal carcinomas and clinicopathological parameters were analyzed. The results showed that poorly differentiated tumors (grade II and III) had significantly higher OGT expression than grade I tumors. Contrary, MGEA5 transcript levels were significantly lower in grade II and III in comparison with grade I tumors. The Spearman rank correlation showed the expressions of OGT and MGEA5 in breast cancer was negatively correlated (r = −0.430, P = 0.0002). Lymph node metastasis status was significantly associated with decreased MGEA5 mRNA expression. This result suggests that elevation in O-GlcNAc modification of proteins may be implicated in breast tumor progression and metastasis. |
format | Online Article Text |
id | pubmed-3295997 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Springer Milan |
record_format | MEDLINE/PubMed |
spelling | pubmed-32959972012-03-21 Gene expression of O-GlcNAc cycling enzymes in human breast cancers Krześlak, Anna Forma, Ewa Bernaciak, Magdalena Romanowicz, Hanna Bryś, Magdalena Clin Exp Med Short Communication O-GlcNAcylation is an abundant, dynamic, and inducible posttranslational modification in which single β-N-acetylglucosamine residues are attached by O-glycosidic linkage to serine or treonine residues. It is suggested that abnormally regulated O-GlcNAcylation may contribute to the pathology of cancer. Cycling of O-GlcNAc residues on intracellular proteins is controlled by two enzymes, O-GlcNAc transferease (OGT), which catalyses the addition of O-GlcNAc residues and nucleocytoplasmic β-N-acetylglucosaminidase (O-GlcNAcase; encoded by MGEA5 gene), an enzyme involved in the removal of O-GlcNAc. In this study, relationship between the mRNA expressions of genes coding O-GlcNAc cycling enzymes in breast ductal carcinomas and clinicopathological parameters were analyzed. The results showed that poorly differentiated tumors (grade II and III) had significantly higher OGT expression than grade I tumors. Contrary, MGEA5 transcript levels were significantly lower in grade II and III in comparison with grade I tumors. The Spearman rank correlation showed the expressions of OGT and MGEA5 in breast cancer was negatively correlated (r = −0.430, P = 0.0002). Lymph node metastasis status was significantly associated with decreased MGEA5 mRNA expression. This result suggests that elevation in O-GlcNAc modification of proteins may be implicated in breast tumor progression and metastasis. Springer Milan 2011-05-13 2012 /pmc/articles/PMC3295997/ /pubmed/21567137 http://dx.doi.org/10.1007/s10238-011-0138-5 Text en © The Author(s) 2011 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. |
spellingShingle | Short Communication Krześlak, Anna Forma, Ewa Bernaciak, Magdalena Romanowicz, Hanna Bryś, Magdalena Gene expression of O-GlcNAc cycling enzymes in human breast cancers |
title | Gene expression of O-GlcNAc cycling enzymes in human breast cancers |
title_full | Gene expression of O-GlcNAc cycling enzymes in human breast cancers |
title_fullStr | Gene expression of O-GlcNAc cycling enzymes in human breast cancers |
title_full_unstemmed | Gene expression of O-GlcNAc cycling enzymes in human breast cancers |
title_short | Gene expression of O-GlcNAc cycling enzymes in human breast cancers |
title_sort | gene expression of o-glcnac cycling enzymes in human breast cancers |
topic | Short Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3295997/ https://www.ncbi.nlm.nih.gov/pubmed/21567137 http://dx.doi.org/10.1007/s10238-011-0138-5 |
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