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- W2077661681 abstract "Deciphering the molecular basis of stem cell pluripotency is fundamental to the understanding of stem cell biology, early embryonic development, and to the clinical application of regenerative medicine. We report here that the molecular chaperone heat shock protein 90 (Hsp90) is essential for mouse embryonic stem cell (ESC) pluripotency through regulating multiple pluripotency factors, including Oct4, Nanog, and signal transducer and activator of transcription 3. Inhibition of Hsp90 by either 17-N-Allylamino-17-demethoxygeldanamycin or miRNA led to ESC differentiation. Overexpression of Hsp90β partially rescued the phenotype; in particular, the levels of Oct4 and Nanog were restored. Notably, Hsp90 associated with Oct4 and Nanog in the same cellular complex and protected them from degradation by the ubiquitin proteasome pathway, suggesting that Oct4 and Nanog are potential novel Hsp90 client proteins. In addition, Hsp90 inhibition reduced the mRNA level of Oct4, but not that of Nanog, indicating that Hsp90 participates in Oct4 mRNA processing or maturation. Hsp90 inhibition also increased expression of some protein markers for mesodermal lineages, implying that Hsp90 suppresses mesodermal differentiation from ESCs. These findings support a new role for Hsp90 in maintaining ESC pluripotency by sustaining the level of multiple pluripotency factors, particularly Oct4 and Nanog." @default.
- W2077661681 created "2016-06-24" @default.
- W2077661681 creator A5012590158 @default.
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- W2077661681 creator A5086999165 @default.
- W2077661681 date "2012-07-24" @default.
- W2077661681 modified "2023-10-02" @default.
- W2077661681 title "Regulation of Embryonic Stem Cell Pluripotency by Heat Shock Protein 90" @default.
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- W2077661681 doi "https://doi.org/10.1002/stem.1143" @default.
- W2077661681 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3665290" @default.
- W2077661681 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22696450" @default.
- W2077661681 hasPublicationYear "2012" @default.
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