Lal A S, Clifton A D, Rouse J, Segal A W, Cohen P
Department of Biochemistry, University College London, Dundee, DD1 5EH, United Kingdom.
Biochem Biophys Res Commun. 1999 Jun 7;259(2):465-70. doi: 10.1006/bbrc.1999.0759.
Activation of the neutrophil NADPH oxidase by either the bacterial peptide fMLP or phorbol myristate acetate (PMA) is partially suppressed by SB 203580, a specific inhibitor of the MAP kinase family member, SAPK2/p38. The concentration of SB 203580 that suppresses activation of NADPH oxidase is similar to that which inhibits SAPK2/p38 in vitro, and both fMLP and PMA induce an extremely rapid and potent activation of SAPK2/p38 in neutrophils. SB 203580 does not exert its effect by preventing the neutrophil priming reaction, by suppressing the phosphorylation of p47phax, or by preventing the translocation of p47phax/p67phax to the plasma membrane.
细菌肽fMLP或佛波醇肉豆蔻酸酯乙酸酯(PMA)对中性粒细胞NADPH氧化酶的激活作用,会被MAP激酶家族成员SAPK2/p38的特异性抑制剂SB 203580部分抑制。抑制NADPH氧化酶激活的SB 203580浓度,与体外抑制SAPK2/p38的浓度相似,且fMLP和PMA均可在中性粒细胞中诱导SAPK2/p38极其快速且有效的激活。SB 203580并非通过阻止中性粒细胞的预激活反应、抑制p47phax的磷酸化或阻止p47phax/p67phax转位至质膜来发挥其作用。