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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Elevated O-GlcNAcylation promotes colonic inflammation and tumorigenesis by modulating NF-κB signaling

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Title
Elevated O-GlcNAcylation promotes colonic inflammation and tumorigenesis by modulating NF-κB signaling
Author
Yang, Yong RyoulKim, Dae HyunSeo, Young-KyoPark, DohyunJang, Hyun-JunChoi, Soo YounLee, Yong HwaLee, Gyun HuiNakajima, KazukiTaniguchi, NaoyukiKim, Jung-MinChoi, Eun-JeongMoon, Hyo YoulKim, Il ShinChoi, Jang HyunLee, HoRyu, Sung HoCocco, LucioSuh, Pann-Ghill
Issue Date
2015-05
Publisher
IMPACT JOURNALS LLC
Citation
ONCOTARGET, v.6, no.14, pp.12529 - 12542
Abstract
O-GlcNAcylation is a reversible post-translational modification. O-GlcNAc addition and removal is catalyzed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), respectively. More recent evidence indicates that regulation of O-GlcNAcylation is important for inflammatory diseases and tumorigenesis. In this study, we revealed that O-GlcNAcylation was increased in the colonic tissues of dextran sodium sulfate (DSS)-induced colitis and azoxymethane (AOM)/DSS-induced colitis-associated cancer (CAC) animal models. Moreover, the O-GlcNAcylation level was elevated in human CAC tissues compared with matched normal counterparts. To investigate the functional role of O-GlcNAcylation in colitis, we used OGA heterozygote mice, which have an increased level of O-GlcNAcylation. OGA+/- mice have higher susceptibility to DSS-induced colitis than OGA+/+ mice. OGA +/- mice exhibited a higher incidence of colon tumors than OGA+/+ mice. In molecular studies, elevated O-GlcNAc levels were shown to enhance the activation of NF-κB signaling through increasing the binding of RelA/p65 to its target promoters. We also found that Thr-322 and Thr352 in the p65- O-GlcNAcylation sites are critical for p65 promoter binding. These results suggest that the elevated O-GlcNAcylation level in colonic tissues contributes to the development of colitis and CAC by disrupting regulation of NF-κB-dependent transcriptional activity.
URI
https://scholarworks.unist.ac.kr/handle/201301/12773
URL
http://www.impactjournals.com/oncotarget/index.php?journal=oncotarget&page=article&op=view&path[]=3725&pubmed-linkout=1
DOI
10.18632/oncotarget.3725
ISSN
1949-2553
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