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Oxidative Medicine and Cellular Longevity
Volume 2017 (2017), Article ID 9821543, 11 pages
https://doi.org/10.1155/2017/9821543
Research Article

Salidroside Inhibits HMGB1 Acetylation and Release through Upregulation of SirT1 during Inflammation

1Department of Biochemistry, Wannan Medical College, Wuhu, Anhui, China
2Anhui Province Key Laboratory of Active Biological Macromolecules, Wuhu, Anhui, China
3Department of Microbiology and Immunology, Wannan Medical College, Wuhu, Anhui, China

Correspondence should be addressed to Zhilin Qi

Received 9 March 2017; Revised 25 May 2017; Accepted 25 July 2017; Published 3 December 2017

Academic Editor: Anandh B. P. Velayutham

Copyright © 2017 Zhilin Qi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

HMGB1, a highly conserved nonhistone DNA-binding protein, plays an important role in inflammatory diseases. Once released to the extracellular space, HMGB1 acts as a proinflammatory cytokine that triggers inflammatory reaction. Our previous study showed that salidroside exerts anti-inflammatory effect via inhibiting the JAK2-STAT3 signalling pathway. However, whether salidroside inhibits the release of HMGB1 is still unclear. In this study, we aim to study the effects of salidroside on HMGB1 release and then investigate the potential molecular mechanisms. In an experimental rat model of sepsis caused by CLP, salidroside administration significantly attenuated lung injury and reduced the serum HMGB1 level. In RAW264.7 cells, we investigated the effects of salidroside on LPS-induced HMGB1 release and then explored the underlying molecular mechanisms. We found that salidroside significantly inhibited LPS-induced HMGB1 release, and the inhibitory effect was correlated with the HMGB1 acetylation levels. Mechanismly, salidroside inhibits HMGB1 acetylation through the AMPK-SirT1 pathway. In addition, SirT1 overexpression attenuated LPS-induced HMGB1 acetylation and nucleocytoplasmic translocation. Furthermore, in SirT1 shRNA plasmid-transfected cells, salidroside treatment enhanced SirT1 expression and reduced LPS-activated HMGB1 acetylation and nucleocytoplasmic translocation. Collectively, these results demonstrated that salidroside might reduce HMGB1 release through the AMPK-SirT1 signalling pathway and suppress HMGB1 acetylation and nucleocytoplasmic translocation.