Earticle

초록

영어

O-linked N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) is a post translational modification, which is modulated by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). In the present study, we determined that OGA regulates LPS-driven activation of iNOS/NO. PUGNAc, an inhibitor of OGA, suppress LPS-induced induction of iNOS/NO and the gene expression of proinflammatory mediators, indicating that O-GlcNAcase is important enzyme for LPS-mediated inflammatory response. PUGNAc did not affect the NF-κB O-GlcNAcylation in response to LPS. In addition, PUGNAc alter neither the binding of NF-κB subunits to the iNOS promoter nor the transcriptional activity of NF-κB, suggesting that inhibitory effect of PUGNAc on LPS-induced iNOS expression is not mediated by NF-κB inhibition. Instead, PUGNAc down-regulates increased phosphorylated AKT in response to LPS, suggesting that LPS-mediated AKT activation may be associate with OGA. In conclusion, our data demonstrate that LPS-mediated upregulation of iNOS/NO production via OGA regulation. Further studies should be ensued to define a possible mechanism of AKT on LPS-induced iNOS protein expression through OGA regulation.

저자

• Ji Sun Hwang [ Department of Physiology and Biophysics, College of Medicine, Inha University ]
• Mi Youn Kwon [ Department of Physiology and Biophysics, College of Medicine, Inha University ]
• Eun Hye Jung [ Department of Physiology and Biophysics, College of Medicine, Inha University ]
• Inn Oc Han [ Department of Physiology and Biophysics, College of Medicine, Inha University ]

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간행물

표지보기 관심저널 등록

• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614