Emodin Isolated from Polygoni cuspidati Radix Inhibits TNF-alpha and IL-6 Release by Blockading NF-kappaB and MAP Kinase Pathways in Mast Cells Stimulated with PMA Plus A23187.
- Author:
Yue LU
1
;
Yong Tae JEONG
;
Xian LI
;
Mi Jin KIM
;
Pil Hoon PARK
;
Seung Lark HWANG
;
Jong Keun SON
;
Hyeun Wook CHANG
Author Information
1. School of Pharmacy, Shanghai University of Traditional Chinese Medicine, Shanghai, 201203, China.
- Publication Type:Original Article
- Keywords:
Emodin;
Pro-inflammatory cytokine;
NF-kappaB;
Mitogen-activated protein kinase;
Bone marrow-derived mast cells;
PMA plus A23187
- MeSH:
Animals;
Calcimycin*;
Calcium;
Cytokines;
Emodin*;
I-kappa B Kinase;
Interleukin-6*;
Interleukins;
Mast Cells*;
Mice;
Mitogen-Activated Protein Kinases;
NF-kappa B*;
p38 Mitogen-Activated Protein Kinases;
Phosphorylation;
Phosphotransferases*;
Protein Kinases;
Tumor Necrosis Factor-alpha*
- From:Biomolecules & Therapeutics
2013;21(6):435-441
- CountryRepublic of Korea
- Language:English
-
Abstract:
Emodin, a naturally occurring anthraquinone derivative isolated from Polygoni cuspidati radix, has several beneficial pharmacologic effects, which include anti-cancer, anti-diabetic, and anti-inflammatory activities. In this study, the authors examined the effect of emodin on the production of proinflammatory cytokines, such as, tumor necrosis factor (TNF)-alpha and interleukin (IL)-6, in mouse bone marrow-derived mast cells (BMMCs) stimulated with phorbol 12-myristate 13-acetate (PMA) plus the calcium ionophore A23187. To investigate the mechanism responsible for the regulation of pro-inflammatory cytokine production by emodin, the authors assessed its effects on the activations of transcriptional factor nuclear factor-kappaB (NF-kappaB) and mitogen-activated protein kinases (MAPKs). Emodin attenuated the nuclear translocation of (NF)-kappaB p65 and its DNA-binding activity by reducing the phosphorylation and degradation of IkappaBalpha and the phosphorylation of IkappaB kinase B (IKK). Furthermore, emodin dose-dependently attenuated the phosphorylations of MAPKs, such as, extracellular signal-regulated kinase 1/2 (ERK1/2), p38 MAP kinase, and the stress-activated protein kinases (SAPK)/c-Jun-N-terminal kinase (JNK). Taken together, the findings of this study suggest that the anti-inflammatory effects of emodin on PMA plus A23187-stimulated BMMCs are mediated via the inhibition of NF-kappaB activation and of the MAPK pathway.
