Inhibition of mitogen-activated protein kinase kinase blocks activation and redistribution of 5-lipoxygenase in HL-60 cells.
Inhibition of mitogen-activated protein kinase kinase blocks activation and redistribution of 5-lipoxygenase in HL-60 cells.
复制标题
抑制丝裂原激活的蛋白激酶激酶可阻断 HL-60 细胞中 5-脂氧合酶的激活和重新分布。
DOI：
10.1006/abbi.1996.0292
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Fitzpatrick,FA
中科院分区：
文献类型：
--
作者：
Lepley,RA;Fitzpatrick,FA
在Ca ~（2+）离子载体激活的HL-60粒细胞中，丝裂原活化蛋白激酶激酶-1抑制剂PD 098059阻断了5-脂氧合酶从胞质到核膜的转运和相应的酶激活。PD 098059抑制5-HETE形成，用A23187单独刺激的IC 50 = 9.4 μMin细胞，用A23187加20 μMarachidonic acid刺激的IC 50 = 12 μMin细胞。PD 098059以浓度依赖性方式抑制5-脂氧合酶的易位，IC 50约为10 μM。浓度低于100 μ M PD 098059对纯化的重组5-LO活性无影响。总的来说，这些数据表明，MAPKK-1参与的分子过程中管理的5-脂氧合酶的激活和易位从细胞质到核膜。
In Ca2+ionophore-activated HL-60 granulocytes the mitogen-activated protein kinase kinase-1 inhibitor, PD098059, blocked translocation of 5-lipoxygenase from the cytosol to the nuclear membrane and the corresponding enzyme activation. PD098059 inhibited 5-HETE formation with an IC50= 9.4 μMin cells stimulated with A23187 alone, and with an IC50= 12 μMin cells stimulated with A23187 plus 20 μMarachidonic acid. PD098059 inhibited translocation of 5-lipoxygenase in a concentration-dependent manner with an IC50approximately 10 μM. At concentrations less than 100 μMPD098059 had no effect on purified recombinant 5-LO activity. Collectively, these data indicate that MAPKK-1 participates in the molecular processes governing activation and translocation of 5-lipoxygenase from the cytosol to the nuclear membrane.