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• W2016648276 abstract "We now evaluated the anti-inflammatory mechanisms of andrographolide on complement 5a (C5a)-induced macrophage recruitment in vitro. Andrographolide concentration dependently inhibited cell migration toward C5a with an IC50 of 5.6±0.7 μM. With relatively specific kinase inhibitors (PD98059, SB203580, SP600125, wortmannin and LY294002, respectively) the results showed that extracellular signal-regulated kinase1/2 (ERK1/2), p38 mitogen-activated protein kinase (p38 MAPK) and phosphatidylinositol-3-kinase (PI3K) were necessary for C5a-induced migration, whereas c-Jun N-terminal kinase (JNK) was nonessential. Andrographolide significantly attenuated C5a-stimulated phosphorylation of ERK1/2, and of its upstream activator, MAP kinase–ERK kinase (MEK1/2). C5a-activated ERK1/2 phosphorylation was 86±9% inhibited by 30 μM andrographolide. Under the same conditions, however, andrographolide failed to affect C5a-stimulated p38 MAPK and JNK phosphorylation. Andrographolide also strongly abolished C5a-stimulated Akt phosphorylation, a downstream target protein for PI3K. These results indicate that inhibition of cell migration by interfering with ERK1/2 and PI3K/Akt signal pathways may contribute to the anti-inflammatory activity of andrographolide." @default.
• W2016648276 created "2016-06-24" @default.
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• W2016648276 date "2004-09-01" @default.
• W2016648276 modified "2023-09-26" @default.
• W2016648276 title "Andrographolide acts through inhibition of ERK1/2 and Akt phosphorylation to suppress chemotactic migration" @default.
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• W2016648276 doi "https://doi.org/10.1016/j.ejphar.2004.07.077" @default.
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