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2017 ; 18
(5
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Epigenetic Bases of Aberrant Glycosylation in Cancer
#MMPMID28481247
Dall'Olio F
; Trinchera M
Int J Mol Sci
2017[May]; 18
(5
): ä PMID28481247
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In this review, the sugar portions of glycoproteins, glycolipids, and
glycosaminoglycans constitute the glycome, and the genes involved in their
biosynthesis, degradation, transport and recognition are referred to as
"glycogenes". The extreme complexity of the glycome requires the regulatory layer
to be provided by the epigenetic mechanisms. Almost all types of cancers present
glycosylation aberrations, giving rise to phenotypic changes and to the
expression of tumor markers. In this review, we discuss how cancer-associated
alterations of promoter methylation, histone methylation/acetylation, and miRNAs
determine glycomic changes associated with the malignant phenotype. Usually,
increased promoter methylation and miRNA expression induce glycogene silencing.
However, treatment with demethylating agents sometimes results in silencing,
rather than in a reactivation of glycogenes, suggesting the involvement of
distant methylation-dependent regulatory elements. From a therapeutic perspective
aimed at the normalization of the malignant glycome, it appears that miRNA
targeting of cancer-deranged glycogenes can be a more specific and promising
approach than the use of drugs, which broad target methylation/acetylation. A
very specific type of glycosylation, the addition of GlcNAc to serine or
threonine (O-GlcNAc), is not only regulated by epigenetic mechanisms, but is an
epigenetic modifier of histones and transcription factors. Thus, glycosylation is
both under the control of epigenetic mechanisms and is an integral part of the
epigenetic code.
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