Anti-inflammatory activities of Reynoutria elliptica through suppression of mitogen-activated protein kinases and nuclear factor-kappa B activation pathways

Authors
Lee, GeumhoChoi, Tae WonKim, ChulwonNam, DongwooLee, Seok-GeunJang, Hyeung-JinLee, Jun-HeeUm, Jae-YoungJung, Sang HoonShim, Bum SangAhn, Kyoo SeokAhn, Kwang Seok
Issue Date
2012-06
Publisher
INFORMA HEALTHCARE
Citation
IMMUNOPHARMACOLOGY AND IMMUNOTOXICOLOGY, v.34, no.3, pp.454 - 464
Abstract
Reynoutria elliptica has been used in traditional Korean medicine to promote blood circulation, relieve pain, increase dieresis, and alleviate respiratory problems, through as yet undefined mechanisms. We set out to determine whether the anti-inflammatory effects of this plant are linked with its ability to suppress mitogen-activated protein kinases (MAPKs) and nuclear factor-kappa B (NF-kappa B) activation in lipopolysaccharide (LPS)-activated RAW 264.7 cells. We found for the first time that the hexane fraction of Reynoutria elliptica (HRE) significantly inhibited LPS-stimulated NO and PGE2 synthesis. This is due to the diminishing of the mRNA and protein expression of iNOS and COX-2, respectively. HRE also suppressed LPS-stimulated TNF-alpha secretion in a dose-dependent manner, which might be due to the suppression of LPS-induced MAPKs and NF-kappa B activation. Moreover, our HPLC data demonstrated that the major components of the HRE were bioactive compounds such as emodin-6-Glc, emodin, and physcion. Overall, our results indicate that Reynoutria elliptica could be provided as a potential candidate for anti-inflammation treatment.
Keywords
NITRIC-OXIDE SYNTHASE; VASCULAR ENDOTHELIAL-CELLS; TRANSCRIPTION FACTOR; INTERFERON-GAMMA; GENE-EXPRESSION; P38 MAPK; BACTERIAL LIPOPOLYSACCHARIDE; DOWN-REGULATION; PHORBOL ESTER; EMODIN; NITRIC-OXIDE SYNTHASE; VASCULAR ENDOTHELIAL-CELLS; TRANSCRIPTION FACTOR; INTERFERON-GAMMA; GENE-EXPRESSION; P38 MAPK; BACTERIAL LIPOPOLYSACCHARIDE; DOWN-REGULATION; PHORBOL ESTER; EMODIN; Reynoutria elliptica; NF-kappa B; MAPKs; nitric oxide; cyclooxygenase-2
ISSN
0892-3973
URI
https://pubs.kist.re.kr/handle/201004/129191
DOI
10.3109/08923973.2011.619195
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KIST Article > 2012
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