Role of heat shock protein 27 phosphorylation in migration of vascular smooth muscle cells

被引：7
作者：
Hai-Feng Chen
Liang-Di Xie
Chang-Sheng Xu
机构：
[1] Fujian Medical University,Fujian Hypertension Research Institute, First Affiliated Hospital
[2] Fujian Medical University,Department of Cardiology, Fujian Provincial Clinical College
来源：
Molecular and Cellular Biochemistry | 2009年 / 327卷
关键词：
Heat shock protein 27; Cytoskeleton; Cell migration; Vascular smooth muscle cells;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
Objective The aim of the present study was to investigate the role of heat shock protein 27 (HSP27) phosphorylation in the migration of vascular smooth muscle cells (VSMCs) induced by angiotensin II (AngII) and platelet derived growth factor-BB (PDGF-BB). Methods The activity of HSP27 was evaluated by Western blot with specific phospho-HSP27 antibody. F-actin polymerization was detected by FITC-Phalloidine staining using confocal microscopy. Modified Boyden chamber technique was employed for VSMCs migration assessment. Results The phosphorylation of HSP27 was induced by AngII and PDGF-BB in a time- and concentration-dependent manner in VSMCs, which was significantly blocked by the HSP inhibitor Quercetin in a concentration-dependent manner. Reorganization of actin stimulated by AngII and PDGF-BB was markedly inhibited by pretreatment with 100 μmol/l Quercetin. The migration of VSMCs induced by AngII and PDGF-BB was partially inhibited by Quercetin with peak inhibition concentration at 100 μmol/l. Conclusions HSP27 phosphorylation plays an important role in mediating the rearrangement of F-actin and migration of VSMCs induced by AngII and PDGF-BB. HSP27 may be a potential target for the interventional treatment of pathological process related to cell migration.
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页码：1 / 6
页数：5
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