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- W2109731472 abstract "Heat-shock protein 90 (HSP90) is known to affect a variety of cellular activities. The present study showed that the HSP90-binding agents, geldanamycin, herbimycin A and radicicol, inhibited the murine thymocyte apoptosis induced by dexamethasone and was accompanied by the inhibition of the reduction of the mitochondrial transmembrane potential (ΔΨm). HSP90-binding agents did not inhibit etoposide-induced apoptosis. The inhibition of dexamethasone-induced apoptosis was in part due to the interference of HSP90 with the glucocorticoid receptor, resulting in the inhibition of nuclear translocation of the receptor. The expression of inositol 1, 4, 5-triphosphate receptors, which were shown to be involved in dexamethasone-induced apoptosis, did not participate in the inhibition of apoptosis." @default.
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- W2109731472 date "2004-01-01" @default.
- W2109731472 modified "2023-09-25" @default.
- W2109731472 title "MODULATION OF DEXAMETHASONE-INDUCED THYMOCYTE APOPTOSIS BY HEAT-SHOCK PROTEIN 90-BINDING AGENTS" @default.
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- W2109731472 doi "https://doi.org/10.2209/tdcpublication.45.1" @default.
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