Activation of p38 in stimulated human neutrophils: phosphorylation of the oxidase component p47phox by p38 and ERK but not by JNK.
Activation of p38 in stimulated human neutrophils: phosphorylation of the oxidase component p47phox by p38 and ERK but not by JNK.
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DOI：
10.1006/abbi.1996.0470
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发表时间：
1996-10
影响因子：
3.9
通讯作者：
J. Benna;J. Benna;Jiahuai Han;Jiahuai Han;J. Park;J. Park;Elmar Schmid;Elmar Schmid;
中科院分区：
文献类型：
--
作者：
J. Benna;J. Benna;Jiahuai Han;Jiahuai Han;J. Park;J. Park;Elmar Schmid;Elmar Schmid;
人中性粒细胞与FMLP（一种趋化肽或PMA，一种蛋白激酶C的刺激物）孵育，导致p38（一种脯氨酸导向的激酶）的激活。先前的研究表明，细胞外信号调节激酶（ERK），另一种脯氨酸定向激酶，在FMLP和PMA刺激的中性粒细胞中以类似的动力学被激活（1,2）。由于这些脯氨酸定向激酶的一个可能靶标是p47phox， p47phox是呼吸爆发氧化酶的一个组成部分，因此我们检测了p38和ERK以及中性粒细胞中存在的另一种脯氨酸定向激酶JNK对该蛋白的磷酸化作用。我们发现p38和ERK在相同的位点以相似的速率磷酸化p47phox，但p47phox不是JNK的底物。这些数据表明p38，像ERK一样，可以在中性粒细胞暴露于适当的刺激下被激活，并且一些但不是所有的脯氨酸定向激酶能够参与正常中性粒细胞功能所必需的蛋白质的磷酸化。
Incubation of human neutrophils with FMLP, a chemotactic peptide, or PMA, a stimulator of protein kinase C, resulted in the activation of p38, a proline-directed kinase. Previous studies had shown that extracellular signal-regulated kinase (ERK), another proline-directed kinase, was activated with similar kinetics in neutrophils stimulated with FMLP and PMA (1, 2). Because one possible target for these proline-directed kinases is p47phox, a component of the respiratory burst oxidase, we examined the phosphorylation of this protein by p38 and ERK, as well as JNK, another proline-directed kinase present in neutrophils. We found that both p38 and ERK phosphorylated p47phox at the same site and at similar rates, but that p47phox was not a substrate for JNK. These data show that p38, like ERK, can be activated in neutrophils exposed to an appropriate stimulus, and that some but not all proline-directed kinases are able to participate in the phosphorylation of a protein essential for normal neutrophil function.