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• W2024154998 abstract "Intestinal epithelial cell (IEC) apoptosis induced by hypoxia compromise intestinal epithelium barrier function. Both Akt and Hsp90 have cytoprotective function. However, the specific role of Akt and <TEX>$Hsp90{beta}$</TEX> in IEC apoptosis induced by hypoxia has not been explored. We confirmed that hypoxia-induced apoptosis was reduced by <TEX>$Hsp90{beta}$</TEX> overexpression but enhanced by decreasing <TEX>$Hsp90{beta}$</TEX> expression. <TEX>$Hsp90{beta}$</TEX> overexpression enhanced BAD phosphorylation and thus reduced mitochondrial release of cytochrome C. Reducing <TEX>$Hsp90{beta}$</TEX> expression had opposite effects. The protective effect of <TEX>$Hsp90{beta}$</TEX> against apoptosis was negated by LY294002, an Akt inhibitor. Further study showed that Akt phosphorylation was enhanced by <TEX>$Hsp90{beta}$</TEX>, which was not due to the activation of upstream PI3K and PDK1 but because of stabilization of pAkt via direct interaction between <TEX>$Hsp90{beta}$</TEX> and pAkt. These results demonstrate that <TEX>$Hsp90{beta}$</TEX> may play a significant role in protecting IECs from hypoxia-induced apoptosis via stabilizing pAkt to phosphorylate BAD and reduce cytochrome C release." @default.
• W2024154998 created "2016-06-24" @default.
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• W2024154998 date "2013-01-31" @default.
• W2024154998 modified "2023-10-06" @default.
• W2024154998 title "Heat shock protein 90β inhibits apoptosis of intestinal epithelial cells induced by hypoxia through stabilizing phosphorylated Akt" @default.
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• W2024154998 doi "https://doi.org/10.5483/bmbrep.2013.46.1.037" @default.
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