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首页> 外文期刊>Molecular and Cellular Biology >Neutrophils Stimulated with a Variety of Chemoattractants Exhibit Rapid Activation of p21-Activated Kinases (Paks): Separate Signals Are Required for Activation and Inactivation of Paks
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Neutrophils Stimulated with a Variety of Chemoattractants Exhibit Rapid Activation of p21-Activated Kinases (Paks): Separate Signals Are Required for Activation and Inactivation of Paks

机译：受多种趋化因子刺激的嗜中性粒细胞表现出p21活化的激酶（Paks）的快速激活：Paks的激活和失活需要单独的信号

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Activation of the p21-activated protein kinases (Paks) was compared in neutrophils stimulated with a wide variety of agonists that bind to receptors coupled to heterotrimeric G proteins. Neutrophils stimulated with sulfatide, a ligand for the L-selectin receptor, or the chemoattractant fMet-Leu-Phe (fMLP), platelet-activating factor, leukotriene B4, interleukin-8, or the chemokine RANTES exhibited a rapid and transient activation of the 63- and 69-kDa Paks. These kinases exhibited maximal activation with each of these agonists within 15 s followed by significant inactivation at 3 min. In contrast, neutrophils treated with the chemoattractant and anaphylatoxin C5a exhibited a prolonged activation (>15 min) of these Paks even though the receptor for this ligand may activate the same overall population of complex G proteins as the fMLP receptor. Addition of fMLP to neutrophils already stimulated with C5a resulted in the inactivation of the 63- and 69-kDa Paks. Optimal activation of Paks could be observed at concentrations of these agonists that elicited only shape changes and chemotaxis in neutrophils. While all of the agonists listed above triggered quantitatively similar activation of the 63- and 69-kDa Paks, fMLP was far superior to the other stimuli in triggering activation of the c-Jun N-terminal kinase (JNK) and the p38 mitogen-activated protein kinase (MAPK). These data indicate that separate signals are required for activation and inactivation of Paks and that, in contrast to other cell types, activated Pak does not trigger activation of JNK or p38-MAPK in neutrophils. These results are consistent with the recent hypothesis that G-protein-coupled receptors may initiate signals independent of those transmitted by the α and βγ subunits of complex G proteins.
机译：在由各种激动剂刺激的嗜中性粒细胞中比较了p21活化的蛋白激酶（Paks）的激活，这些激动剂结合了与异三聚体G蛋白偶联的受体。嗜中性粒细胞受硫化物，L-选择蛋白受体的配体或趋化因子fMet-Leu-Phe（fMLP），血小板活化因子，白三烯B 4 ，白介素8或趋化因子RANTES刺激表现出63 kDa和69 kDa Paks的快速和瞬时激活。这些激酶在15 s内对每种激动剂均表现出最大的活化作用，随后在3分钟时明显失活。相反，经化学趋化剂和过敏毒素C5a处理的嗜中性粒细胞显示了这些Paks的活化时间延长（> 15分钟），即使该配体的受体可能活化了与fMLP受体相同的总复合G蛋白。在已经用C5a刺激的嗜中性粒细胞中加入fMLP导致63 kDa和69 kDa Paks失活。在仅引起嗜中性粒细胞的形状改变和趋化性的这些激动剂的浓度下，可以观察到Paks的最佳活化。尽管上面列出的所有激动剂在数量上都触发了63-和69-kDa Paks的相似活化，但fMLP在触发c-Jun N端激酶（JNK）和p38促分裂原活化的活化方面远远优于其他刺激剂。蛋白激酶（MAPK）。这些数据表明，Paks的激活和失活需要单独的信号，并且与其他细胞类型相比，激活的Pak不会在嗜中性粒细胞中触发JNK或p38-MAPK的激活。这些结果与最近的假说相符，即G蛋白偶联受体可以独立于复杂G蛋白的α和βγ亚基传递的信号而启动信号。

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