Bone morphogenetic protein-7 (BMP-7), which belongs to the TGF-β superfamily, has been shown to reduce macrophage infiltration and tissue injury in animal models of inflammatory renal disease. To explore the mechanism involved in the anti-inflammatory effect, we investigated the effect of BMP-7 on monocyte chemoattractant protein-1 (MCP-1) expression in cultured human mesangial cells. BMP- 7 significantly inhibited constitutive and IL-1β-induced MCP-1 protein production and MCP-1 mRNA expression by mesangial cells in a time- and concentration-dependent manner. BMP-7 also inhibited IL-1β-induced monocyte chemotactic activity released from the mesangial cells. We examined the role of transcription factors NF-κB and AP-1 in BMP-7 inhibition of IL-1β-induced MCP-1 expression. IL-1β increased NF-κB and AP-1 activity and both transcription factors mediated IL-1β-induced MCP-1 expression in mesangial cells. BMP-7 inhibited IL-1β-induced AP-1 activity in a concentration-dependent manner. In contrast, IL-1β-induced NF-κB activity and IκBα degradation were not affected by BMP-7. Furthermore, IL-1β-induced phosphorylation of c-Jun N-terminal kinase was inhibited by BMP-7. These data suggest that BMP-7 inhibits constitutive and IL-1β-induced MCP-1 expression in human mesangial cells partly by inhibiting c-Jun N-terminal kinase activity and subsequent AP-1 activity, and provide new insight into the therapeutic potential of BMP-7 in the inflammatory renal diseases.
This study was to investigate the inhibitory activity of oxidation and acetylcholinesterase using acetone, hexane, ethyl acetate, hot water and ethanol extracts of mycelia obtained from submerged culture from Pleurotus eryngii (DC. ex Fr.) Quel. var. ferulae Lanzi for function tea development. Among various solvent extracts on the oxidation inhibitory activity, the ethanol extract obtained 66.18% of the maximum inhibitory activity. In the case of acetylcholinesterase inhibitory activity, the hot water extract obtained 13.24% of the maximum inhibitory activity. The maximum inhibitory activity of acetylcholinesterase was obtained 17.36% at 40℃ of extract temperature. The maximum inhibitory activity of oxidation was obtained 63.28% at 60℃. The oxidation inhibitory activity was increased from 50.63 to 60.17% when extract time was increased from 2hr to 4hr at 60℃. On the other hand, in the case of over 6hr of extract time, it was decreased to 55.43% at 12hr of extract time. Thermal and pH of acetylcholinesterase inhibitor were stable at 10-30℃ and pH 5.0 to 9.0. As a result, it is considered that this pretreatment effect is effective in promoting inhibitory activity of acetylcholinesterase and oxidation using P. eryngii (DC. ex Fr.) Quel. var. ferulae Lanzi mycelia.
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