Figure 3 | Experimental & Molecular Medicine

Figure 3

From: NADPH oxidase activation contributes to native low-density lipoprotein-induced proliferation of human aortic smooth muscle cells

Figure 3

Native low-density lipoprotein (nLDL) stimulated independent phosphorylation of extracellular signal-regulated kinase 1/2 (Erk1/2) mitogen-activated protein kinase (MAPK) and protein kinase C (PKC) that were associated with p47phox–p22phox interaction. The nLDL stimulation induced maximal phosphorylation of Erk1/2 MAPK at 3 min and PKC at 30 s (a, * vs untreated, ** vs untreated, *** vs untreated, P<0.01, n=4). Erk1/2 MAPK phosphorylation was not blocked by the PKC inhibitors rottlerin (Rotln; 10 μM) and mPKCθ (100 μM) (b). Preincubation with PD98059 (10 μM) and mPKCθ did not reduce PKCθ (c) or PKCβ (d) phosphorylation by nLDL incubation for 10 min. (e) Human aortic smooth muscle cell (hAoSMC) lysates were immunoprecipitated with antiserum against p47phox after nLDL stimulation. p47phox showed increased interaction with phosphorylated Erk1/2 MAPK, phosphorylated PKCθ, and phosphorylated PKCβ. Angiotensin II (10 nM, 10 min) stimulation was used as a control. The representative blot was from three independent experiments.

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