• heat shock protein 27 (Hsp27);
  • mitogen-activated protein kinase (MAPK);
  • placenta;
  • pre-eclampsia


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.