Role of heat shock protein 70 in induction of stress fiber formation in rat arterial endothelial cells in response to stretch stress.
Role of heat shock protein 70 in induction of stress fiber formation in rat arterial endothelial cells in response to stretch stress.
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DOI：
10.1267/ahc.06011
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发表时间：
2007-02-27
影响因子：
2.4
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中科院分区：
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我们使用由大鼠动脉 EC 片组成的实验系统研究了内皮细胞 (EC) 抵抗各种形式的物理应激的机制。通过免疫荧光显微镜评估肌动蛋白应力纤维（SF）的形成和响应机械拉伸应力的内皮热休克应激蛋白（HSP）的表达。拉伸刺激增加了 HSP 25 和 70 的表达，但不增加 HSP 90 的表达。用 SB203580（一种在 HSP 25 激活级联上游起作用的 p38 MAP 激酶抑制剂）或用格尔德霉素（HSP 90 抑制剂）治疗，对 SF 形成对机械拉伸应力的反应没有影响。相比之下，槲皮素（一种 HSP 70 抑制剂）治疗可抑制内皮 HSP 70 的上调和响应拉应力的 SF 形成。此外，用细胞松弛素 D 处理拉伸的 EC，会破坏 SF 的形成，不会对拉伸诱导的内皮 HSP 70 上调产生不利影响。我们的数据表明，内皮 HSP 70 在响应拉应力诱导 SF 形成中发挥重要作用。
We investigated the mechanism by which endothelial cells (ECs) resist various forms of physical stress using an experimental system consisting of rat arterial EC sheets. Formation of actin stress fibers (SFs) and expression of endothelial heat-shock stress proteins (HSPs) in response to mechanical stretch stress were assessed by immunofluorescence microscopy. Stretch stimulation increased expression of HSPs 25 and 70, but not that of HSP 90. Treatment with SB203580, a p38 MAP kinase inhibitor that acts upstream of the HSP 25 activation cascade, or with geldanamycin, an inhibitor of HSP 90, had no effect on the SF formation response to mechanical stretch stress. In contrast, treatment with quercetin, an HSP 70 inhibitor, inhibited both upregulation of endothelial HSP 70 and formation of SFs in response to tensile stress. In addition, treatment of stretched ECs with cytochalasin D, which disrupts SF formation, did not adversely affect stretch-induced upregulation of endothelial HSP 70. Our data suggest that endothelial HSP 70 plays an important role in inducing SF formation in response to tensile stress.