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

Abstract

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 (PGE2), and tumor necrosis factor-α (TNF-α) 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 (IκB-α) and the nuclear translocation of nuclear factor-κB (NF-κB) 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-κB signal pathway, but is irrelevant to the MAPKs pathway.

• Authors: Liying Wang, Jinpo Gu, Mingyue Zong, Qingran Zhang, Huixiang Li, Danna Li, Xiaofeng Mou, Pan Liu, Yanan Liu, Feng Qiu, Feng Zhao
• Journal: Journal of ethnopharmacology (J Ethnopharmacol) Vol. 267 Pg. 113490 (Mar 01 2021) ISSN: 1872-7573 [Electronic] Ireland
• PMID: 33091501 (Publication Type: Journal Article)
• Copyright: Copyright © 2020 Elsevier B.V. All rights reserved.

Chemical References

• Anti-Inflammatory Agents
• Inflammation Mediators
• NF-kappa B
• Withanolides
• physalin A
• Carrageenan
• Luteolin
• Acetic Acid

Topics

• Acetic Acid
• Animals
• Anti-Inflammatory Agents (pharmacology)
• Capillary Permeability (drug effects)
• Carrageenan
• Disease Models, Animal
• Drug Synergism
• Edema (chemically induced, metabolism, pathology, prevention & control)
• Inflammation (chemically induced, metabolism, prevention & control)
• Inflammation Mediators (metabolism)
• Luteolin (pharmacology)
• Macrophages (drug effects, metabolism)
• Male
• Mice
• NF-kappa B (metabolism)
• RAW 264.7 Cells
• Rats, Sprague-Dawley
• Signal Transduction
• Withanolides (pharmacology)