Epigenetic silencing of HNF1A associates with changes in the composition of the human plasma N-glycome (CROSBI ID 583904)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Horvat, Tomislav ; Knežević, Ana ; McCarthy, Mark I ; Rudan, Igor ; Herceg, Zdenko ; Lauc, Gordan ; Zoldoš, Vlatka
engleski
Epigenetic silencing of HNF1A associates with changes in the composition of the human plasma N-glycome
Protein glycosylation is a ubiquitous modification which affects protein structure and function. Recent genome wide association study identified transcription factor HNF1A as an important regulator of plasma protein N-glycosylation. To evaluate the potential impact of epigenetic regulation of HNF1A on protein glycosylation we quantified its CpG methylation in 810 individuals. Correlations between methylation of four CpG sites and the composition of plasma and IgG glycomes were analyzed. Several significant associations were observed between the level of HNF1A methylation and plasma N-glycans, the most significant one at the level of branched N-glycan structures, while there were no significant associations with IgG glycans. The hypothesis that inactivation of HNF1A promotes glycan branching was supported by the analysis of plasma N-glycomes in 61 patients with inactivating mutations in HNF1A, where the increase in plasma glycan branching was observed as well. This study represents the first demonstration of epigenetic regulation of plasma N-glycome composition, suggesting potential mechanism by which epigenetic deregulation of the glycome may contribute to disease development.
bisulphite sequencing; HNF1A; DNA methylation; N-glycosylation; transcription factor
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Podaci o prilogu
85-x.
2011.
objavljeno
Podaci o matičnoj publikaciji
Program and Abstract Book of the Sixth Meeting on Chromatin Structure and Function.
Kouzarides, Tony
Abcam
Podaci o skupu
The sixth meeting on Chromatin Structure and Function
poster
05.12.2011-08.12.2011
Aruba