High sensitivity of embryonic stem cells to proteasome inhibitors correlates with low expression of heat shock protein and decrease of pluripotent cell marker expression
The ubiquitin-proteasome system is a major proteolytic systemfor nonlysosomal degradation of cellular proteins. Here, we investigatedthe response of mouse embryonic stem (ES) cells underproteotoxic stress. Proteasome inhibitors induced expressionof heat shock protein 70 (HSP70) in a concentration- a...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Korean Society for Biochemistry and Molecular Biology
2012-05-01
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| Series: | BMB Reports |
| Subjects: | |
| Online Access: | http://bmbreports.org/jbmb/pdf.php?data=MTMxMTA4MTVAcGRmX3JhaW50cmFjZV9sZWV5c0AlNUI0NS01JTVEMTIwNTI0MjAyM18lMjgyOTktMzA0JTI5Qk1CXzExLTI1OS5wZGY= |
| Summary: | The ubiquitin-proteasome system is a major proteolytic systemfor nonlysosomal degradation of cellular proteins. Here, we investigatedthe response of mouse embryonic stem (ES) cells underproteotoxic stress. Proteasome inhibitors induced expressionof heat shock protein 70 (HSP70) in a concentration- andtime-dependent manner, and also induced apoptosis of ES cells.Importantly, more apoptotic cells were observed in ES cellscompared with other somatic cells. To understand this phenomenon,we further investigated the expression of HSP70 and pluripotentcell markers. HSP70 expression was more significantlyincreased in somatic cells than in ES cells, and expression levelsof pluripotent cell markers such as Oct4 and Nanog were decreasedin ES cells. These results suggest that higher sensitivityof ES cells to proteotoxic stress may be related with lower capacityof HSP70 expression and decreased pluripotent cellmarker expression, which is essential for the survival of ES cells.[BMB reports 2012; 45(5): 299-304] |
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| ISSN: | 1976-6696 1976-670X |