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Figure 4 Effects of cerivastatin on p42^mapk and p70^S6K: In cultured human saphenous vein, SMC PDGF-BB (10 ng/ml, 10 min) markedly stimulated (or phosphorylated) p42^mapk as demonstrated by the slower mobility of the enzyme on Western blots. The activation of p42^mapk was not inhibited by cerivastatin (10^–6 mol/liter), but was markedly reduced by the specific inhibitor of MAPK kinase (MEK), PD98059 (5 x 10^–5 mol/liter), while the PI3K inhibitor (wortmannin, 10^–5 mol/liter) or the p70^S6K inhibitor (rapamycin, 10^–5 mol/liter) had no effects on p42^mapk activation. The same blots were used for analysis of p70^S6K. PDGF-BB stimulated p70^S6K activation (or phosphorylation) as demonstrated by the slower mobility of the enzyme on Western blots, which was not influenced by cerivastatin or by PD98095, the specific inhibitor of MEK. In contrast, activation of p70^S6K was completely prevented by wortmannin or rapamycin. The results were repeated with three independent experiments.