XAV939, a Wnt/β-catenin pathway modulator, has inhibitory effects on LPS-induced inflammatory response.

In this study, we report the anti-inflammatory activity of XAV939, a modulator of the Wnt/β-catenin pathway. WNT/β-catenin pathway and NF-κB signaling pathway were examined in LPS-stimulated human bronchial epithelial cells and effects of XAV939 on these pathways were analyzed. The effect of XAV939 was confirmed in human umbilical vein endothelial cells.

Berberine activates AMPK to suppress proteolytic processing, nuclear translocation and target DNA binding of SREBP-1c in 3T3-L1 adipocytes.

AMP-activated protein kinase (AMPK) and sterol regulatory element binding protein (SREBP)‑1c are major therapeutic targets in the treatment of metabolic diseases. In the present study, the fat‑reducing mechanisms of berberine (BBR), a natural isoquinoline, was investigated by examining the AMPK‑mediated modulation of SREBP‑1c in 3T3‑L1 adipocytes. BBR activated AMPK in a dose‑ and time‑dependent manner, and increased the phosphorylation of the 125‑kDa precursor form of SREBP‑1c, which suppressed its proteolytic processing into the mature 68‑kDa form and its subsequent nuclear translocation.

Lipoteichoic acid upregulates NF-κB and proinflammatory cytokines by modulating β-catenin in bronchial epithelial cells.

Lipoteichoic acid (LTA) is a major cell wall component and virulence factor of gram-positive bacteria. The present study investigated the LTA‑induced inflammatory response of BEAS‑2B human bronchial epithelial cells, and detected the expression levels of proinflammatory cytokines interleukin (IL)‑6, IL‑8, IL‑1β, tumour necrosis factor‑α and monocyte chemotactic protein‑1, the upregulation of NF‑κB, and the phosphorylation and degradation of I‑κB. During the LTA‑induced inflammatory response of the BEAS‑2B human bronchial epithelial cells, the activity levels of the β‑catenin‑dependent promoter, and the protein expression levels of β‑catenin were significantly upregulated, whereas β‑catenin phosphorylation and the expression levels of AXIN were significantly downregulated.