Activation of MAPK in fibroblasts by Treponema denticola major outer sheath protein
Activation of MAPK in fibroblasts by Treponema denticola major outer sheath protein
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DOI：
10.1016/j.bbrc.2007.02.111
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发表时间：
2007-04-27
影响因子：
3.1
通讯作者：
Ellen, Richard P.
中科院分区：
文献类型：
--
作者：
Jobin, Marie-Claude;Virdee, Inderpreet;Ellen, Richard P.
齿垢密螺旋体的主要外鞘蛋白（Msp）诱导培养的成纤维细胞中的Ca 2+进入和肌动蛋白重组，但Msp介导这些反应的途径尚未确定。我们认为Msp可能激活蛋白激酶作为肌动蛋白重塑之前的应激反应。磷酸激酶筛选表明，Msp诱导的多种激酶的磷酸化的途径，响应细胞外激动剂和调节肌动蛋白组装。34种激酶被显著激活，包括p38和ERK 1/2。因此，通过免疫印迹和光密度测定法测量全细胞裂解物中p38和ERK 1/2的表达和磷酸化。这两种激酶对Msp暴露的反应呈剂量和时间依赖性，分别被SB 202190和U1026抑制。不受细胞外Ca ~（2+）的影响。这些数据表明，齿垢毛癣菌Msp可能通过激活MAP激酶途径对成纤维细胞施加瞬时应力。(c)2007年爱思唯尔公司All rights reserved.
The major outer sheath protein (Msp) of Treponema denticola induces Ca2+ entry and actin reorganization in cultured fibroblasts, but the pathways by which Msp mediates these responses are not yet defined. We considered that Msp may activate protein kinases as a stress response that precedes actin remodelling. Phospho-kinase screens showed that Msp induced phosphorylation of multiple kinases in pathways that respond to extracellular agonists and regulate actin assembly. 34 kinases were significantly activated, including p38 and ERK 1/2. Accordingly, the expression and phosphorylation of p38 and ERK 1/2 in whole cell lysates were measured by immunoblotting and densitometry. Both kinases responded in a dose- and time-dependent manner to Msp exposure, were inhibited by SB202190 and U1026, respectively. and were unaffected by extracellular Ca2+. These data indicate that T denticola Msp may exert transient stress on fibroblasts through activation of MAP kinase pathways. (c) 2007 Elsevier Inc. All rights reserved.