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. 2013 Sep 23;2013:964012. doi: 10.1155/2013/964012

Figure 5.

Figure 5

Resolvin D1 suppressed phosphorylation of PI3K/Akt in primary rat lung fibroblasts stimulated with LPS. Western blot analysis of P-AKT and phosphorylated ERK1/2. β-actin served as a loading control. Cultured and serum-deprived primary rat lung fibroblasts were treated with lipopolysaccharide (LPS) for 30 minutes for P-AKT and phosphorylated ERK1/2 measurement, with or without preincubation with resolvin D1. ((a), (b1), (b3)) The expressions of p-AKT and the phosphorylated ERK2 (P42) were stimulated by LPS for 30 minutes in primary rat lung fibroblasts, significantly downregulated by resolvin D1 (∗ P < 0.05 versus control, LPS + resolvin D1 groups). ((a), (b2)) However, no significant change in the expression of the phosphorylated ERK1 (P44) was observed between LPS group and LPS plus resolvin D1 group. Results shown are representative of four independent experiments.