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子痫前期胎盘组织中热休克蛋白27与丝裂原活化蛋白激酶(p38和细胞外信号调节激酶)之间的相互作用增强。

Increased interaction between heat shock protein 27 and mitogen-activated protein kinase (p38 and extracellular signal-regulated kinase) in pre-eclamptic placentas.

作者信息

Shin Jeong-Kyu, Jeong Young-Taek, Jo Hyun-Cheol, Kang Min-Young, Chang In-Suk, Baek Jong-Chul, Park Ji-Kwon, Lee Soon-Ae, Lee Jong-Hak, Choi Wan-Sung, Paik Won-Young

机构信息

Department of Obstetrics and Gynecology, College of Medicine, Gyeongsang National University, Jinju, Korea.

出版信息

J Obstet Gynaecol Res. 2009 Oct;35(5):888-94. doi: 10.1111/j.1447-0756.2009.01053.x.

DOI:10.1111/j.1447-0756.2009.01053.x
PMID:20149037
Abstract

AIMS

Heat shock protein 27 (Hsp27) is a well-known stress response protein that is characterized by its phosphorylative capacity. Hsp27 becomes phosphorylated in response to various stimuli through interaction with several different kinases. The purpose of this study was to evaluate the interaction between Hsp27 and mitogen-activated protein kinase (MAPK) (p38, extracellular signal-regulated kinase [ERK], and c-Jun N-terminal kinase) in the human placenta derived from patients with pre-eclampsia.

METHODS

Western blot analysis was used to examine the levels of expression of Hsp27 and MAPK (p38, ERK, and c-Jun N-terminal kinase). Immunoprecipitation analysis was used to determine the interaction between Hsp27 and MAPK (p38 and ERK).

RESULTS

Western blotting analysis and immunohistochemistry showed that the expression of Hsp27 and p-Hsp27 in the placental tissues of the pre-eclampsia group were significantly higher than that in the normal pregnancy group. Immunoprecipitation analysis showed that the interaction between Hsp27 and MAPK (p38 and ERK) was significantly increased in the pre-eclamptic placenta tissues.

CONCLUSION

The interaction between Hsp27 and MAPK was increased, suggesting that phosphorylation of Hsp27 might be induced by p38 and ERK in placentas from patients with pre-eclampsia.

摘要

目的

热休克蛋白27(Hsp27)是一种著名的应激反应蛋白,其特点是具有磷酸化能力。Hsp27通过与几种不同的激酶相互作用,对各种刺激作出反应而发生磷酸化。本研究的目的是评估子痫前期患者胎盘组织中Hsp27与丝裂原活化蛋白激酶(MAPK)(p38、细胞外信号调节激酶[ERK]和c-Jun氨基末端激酶)之间的相互作用。

方法

采用蛋白质印迹法检测Hsp27和MAPK(p38、ERK和c-Jun氨基末端激酶)的表达水平。采用免疫沉淀分析法确定Hsp27与MAPK(p38和ERK)之间的相互作用。

结果

蛋白质印迹分析和免疫组织化学显示,子痫前期组胎盘组织中Hsp27和磷酸化Hsp27(p-Hsp27)的表达明显高于正常妊娠组。免疫沉淀分析显示,子痫前期胎盘组织中Hsp27与MAPK(p38和ERK)之间的相互作用显著增加。

结论

Hsp27与MAPK之间的相互作用增强,提示子痫前期患者胎盘组织中Hsp27的磷酸化可能由p38和ERK诱导。

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