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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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High sensitivity of embryonic stem cells to proteasome inhibitors correlates with low expression of heat shock protein and decrease of pluripotent cell marker expression

  • Park, Jeong-A (Department of Biochemistry, College of Natural Sciences, Chungbuk National University) ;
  • Kim, Young-Eun (Department of Biochemistry, College of Natural Sciences, Chungbuk National University) ;
  • Ha, Yang-Hwa (Department of Biochemistry, College of Natural Sciences, Chungbuk National University) ;
  • Kwon, Hyung-Joo (Center for Medical Science Research, College of Medicine, Hallym University) ;
  • Lee, Young-Hee (Department of Biochemistry, College of Natural Sciences, Chungbuk National University)
  • Received : 2011.12.02
  • Accepted : 2012.01.26
  • Published : 2012.05.31
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Abstract

The ubiquitin-proteasome system is a major proteolytic system for nonlysosomal degradation of cellular proteins. Here, we investigated the response of mouse embryonic stem (ES) cells under proteotoxic stress. Proteasome inhibitors induced expression of heat shock protein 70 (HSP70) in a concentration- and time-dependent manner, and also induced apoptosis of ES cells. Importantly, more apoptotic cells were observed in ES cells compared with other somatic cells. To understand this phenomenon, we further investigated the expression of HSP70 and pluripotent cell markers. HSP70 expression was more significantly increased in somatic cells than in ES cells, and expression levels of pluripotent cell markers such as Oct4 and Nanog were decreased in ES cells. These results suggest that higher sensitivity of ES cells to proteotoxic stress may be related with lower capacity of HSP70 expression and decreased pluripotent cell marker expression, which is essential for the survival of ES cells.

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