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Jaffrey, S.R., Erdjument-Bromage, H., Ferris, C.D., Tempst, P., Snyder, S.H., 2001. Protein S-nitrosylation: a physiological signal for neuronal nitric oxide. Nat Cell Biol 3, 193-197.

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Article

S-nitrosylation of Inhibitor-κB kinase: Identifying Novel Targets of Curcumin

1Department of Food Science, National Taiwan Ocean University, Keelung, Taiwan, R.O.C.


Journal of Food and Nutrition Research. 2016, Vol. 4 No. 9, 600-609
DOI: 10.12691/jfnr-4-9-7
Copyright © 2016 Science and Education Publishing

Cite this paper:
Ning-Jo Kao, Chien-Sheng Wu, Jia-Yuan Hu, Zwe-Ling Kong. S-nitrosylation of Inhibitor-κB kinase: Identifying Novel Targets of Curcumin. Journal of Food and Nutrition Research. 2016; 4(9):600-609. doi: 10.12691/jfnr-4-9-7.

Correspondence to: Zwe-Ling  Kong, Department of Food Science, National Taiwan Ocean University, Keelung, Taiwan, R.O.C.. Email: kongzl@mail.ntou.edu.tw

Abstract

In this study, we investigated the preventive effects of curcumin using LPS (Lipopolysaccharides)-induced Raw264.7 cells and the potential role of curcumin in regulation of anti-inflammation through S-nitrosylation. Western blot presented the protein expression of iNOS can be reduced by treated curcumin with 5, 10 and 15 μM separately for 12 and 24h. Consistently, pro-inflammatory cytokines, such as IL-1β, IL-6, TNFα and IFN-γ was also repressed. Moreover, 5, 10 and 15 μM curcumin reduced the amount of nitrite and nitrate in LPS-induced Raw264.7 cells maintained total S-nitrosylation level on proteins at 12h, the similar results was also observed at 24h that indicating curcumin inhibited NO oxidation. Furthermore, the protection of S-nitrosylation on IKKβ in LPS-induced Raw264.7 cells at 12h by curcumin caused the repression of IκB phosphorylation and NF-κB activation. In conclusion, this study verified that curcumin-mediated S-nitrosylation may be as an important regulator for anti-inflammation in LPS-induced Raw264.7 cells.

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