Anti-inflammatory action of physalin A by blocking the activation of NF-κB signaling pathway

Ethnopharmacological relevance: Physalis Calyx seu Fructus is typically used to treat inflammatory diseases such as upper respiratory tract infection and acute tonsillitis in clinical practice of China. Physalin A, a main active ingredient of this traditional Chinese medicine (TCM), has been reported for its significant anti-tumor activity. However, most reports focused on the studies of its anti-tumor activity, the anti-inflammatory activity of physalin A and its molecular mechanism are still not elucidated clearly. Aim of the study: The aim of the study was to investigate the anti-inflammatory activities both in vitro and in vivo and molecular mechanism of physalin A. Materials and methods: The potential anti-inflammatory properties of physalin A were evaluated in vitro by lipopolysaccharide (LPS)-induced RAW 264.7 macrophage cells, and in vivo via two typical acute inflammation murine models. Some important inflammation-related molecules were analyzed by enzyme-linked immuno sorbent assay (ELISA) and Western blotting. Results: The results showed that physalin A inhibited carrageenan-induced paw edema of rats and capillary permeability of mice induced by acetic acid in vivo. Furthermore, physalin A also significantly reduced the release of inflammatory mediators nitric oxide (NO), prostaglandin E2 (PGE(2)), and tumor necrosis factor-alpha (TNF-alpha) induced by lipopolysaccharide (LPS) in RAW 264.7 in vitro. Further investigations indicated that physalin A can down-regulate the high expression of inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2) in a dose-dependent manner. Physalin A remarkably blocked the degradation of inhibitor of nuclear factor kappa B alpha (I kappa B-alpha) and the nuclear translocation of nuclear factor-kappa B (NF-kappa B) p65 induced by LPS in RAW 264.7 cells. However, physalin A did not significantly inhibit the phosphorylation of mitogen-activated protein kinases (MAPKs) family proteins c-Jun N-terminal kinase (JNK) or extracellular signal-regulated kinase (ERK) or p38. Conclusions: All the results clearly illustrated that the anti-inflammatory action of physalin A is due to the inactivation of NF-kappa B signal pathway, but is irrelevant to the MAPKs pathway.

Automated summary

The study aimed to investigate the anti-inflammatory activities and molecular mechanism of physalin A. Results showed that the anti-inflammatory action of physalin A is due to the inactivation of NF-kappa B signal pathway, but is irrelevant to the MAPKs pathway.