HSP27 and αB-crystallin are highly up-regulated in corpus uteri myometrium at labor

［ABSTRACT］AIM: To investigate the expression of heat-shock protein 27 (HSP27) and α-cystallin B chain (αB-crystallin) proteins in corpus uteri myometrium in not-in-labor and in-labor situations.METHODS: Comparative proteomics technique was used to identify HSP27 and αB-crystallin in corpus uteri myometrium in not-in-labor and in-labor situations. The methods of half quantitative RT-PCR, Western blotting analysis and immunohistochemistry were performed to determine the differential expression levels of HSP27. RESULTS: The protein levels of HSP27 and αB-crystallin were highly up-regulated in corpus uteri myometrium at term spontaneous labor (P<0.05). Four HSP27 spots were identified with identical molecular weight and different isoelectric points from 2 two-dimensional gel electrophoresis profiles of corpus uteri myometrium. ImageMaster 2D Platinum software analysis showed that only one HSP27 spot had differential significance (P<0.05),and the rest spots had no significant difference between the 2 profiles (P>0.05). CONCLUSION: The protein levels of HSP27 and αB-crystallin are highly up-regulated in corpus uteri myometrium at term spontaneous labor, suggesting that the two small heat-shock proteins participate in human myometrial contraction at labor and will be potential targets for future tocolytic design.