Vitisin A suppresses LPS-induced NO production by inhibiting ERK, p38, and NF-κB activation in RAW 264.7 cells

• Published in: International immunopharmacology Vol. 9; no. 3; pp. 319 - 323
• Main Authors: Mi Jeong Sung, Davaatseren, Munkhtugs, Kim, Won, Sung Kwang Park, Kim, Soon-Hee, Haeng Jeon Hur, Myung Sunny Kim, Kim, Young-Sup, Dae Young Kwon
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.03.2009
• Subjects: Inflammation; Macrophage; Mitogen-activated protein kinase (MAPK); Nitric oxide; Nuclear factor-κB (NF-κB); Vitisin A; Inflammation; Nuclear factor-κB (NF-κB); Nitric oxide; Mitogen-activated protein kinase (MAPK); Vitisin A; Macrophage
• ISSN: 1567-5769; 1878-1705
• DOI: 10.1016/j.intimp.2008.12.005

Vitisin A, a resveratrol tetramer isolated from Vitis vinifera roots, exhibits antioxidative, anticancer, antiapoptotic, and anti-inflammatory effects. It also inhibits nitric oxide (NO) production. Here, we examined the mechanism by which vitisin A inhibits NO production in lipopolysaccharide (LPS)-induced RAW 264.7 macrophage cells. Vitisin A dose dependently inhibited LPS-induced NO production and inducible NO synthase (iNOS) expression. In contrast, the production of proinflammatory cytokines such as tumor necrosis factor-α (TNF-α) and interleukin-6 (IL-6) was not altered by vitisin A. To investigate the signaling pathway for NO inhibition by vitisin A, we examined nuclear factor-κB (NF-κB) activation in the mitogen-activated protein kinase (MAPK) pathway, an inflammation-induced signal pathway in RAW 264.7 cells. Vitisin A inhibited LPS-induced extracellular signal-regulated kinase 1/2 (ERK1/2) and p38 phosphorylation and suppressed LPS-induced NF-κB activation in RAW 264.7 cells. This suggests that vitisin A decreased NO production via downregulation of ERK1/2 and p38 and the NF-κB signal pathway in RAW 264.7 cells.