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Inhibitors of heat shock protein 90 augment endothelin-1-induced heat shock protein 27 through the SAPK/JNK signaling pathway in osteoblasts
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Inhibitors of heat shock protein 90 augment endothelin-1-induced heat shock protein 27 through the SAPK/JNK signaling pathway in osteoblasts
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Inhibitors of heat shock protein 90 augment endothelin-1-induced heat shock protein 27 through the SAPK/JNK signaling pathway in osteoblasts
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Journal Article
Inhibitors of heat shock protein 90 augment endothelin-1-induced heat shock protein 27 through the SAPK/JNK signaling pathway in osteoblasts
2018
Overview
It has been previously reported that endothelin-1 (ET-1) stimulates the induction of heat shock protein (HSP) 27 through the activation of p38 mitogen-activated protein (MAP) kinase and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in osteoblast-like MC3T3-E1 cells. The present study investigated whether HSP90, a high-molecular-weight HSP, was implicated in the ET-1-stimulated HSP27 induction in MC3T3-E1 cells. The effects of HSP90 inhibitors on the induction of HSP27 were examined. The HSP90 inhibitors geldanamycin and 17-demethoxygeldanamycin (17-DMAG) significantly amplified HSP27 induction stimulated by ET-1 in a dose-dependent manner. In addition, onalespib (another HSP90 inhibitor) significantly strengthened the ET-1-induced HSP27 protein levels. The ET-1-stimulated phosphorylation of p38 MAP kinase was minimally affected by geldanamycin, 17-DMAG or onalespib. Onalespib and 17-DMAG significantly enhanced the ET-1-induced phosphorylation of SAPK/JNK. In addition, SP600125, a SAPK/JNK inhibitor, notably reduced the amplification by onalespib of ET-1-induced HSP27. These results suggest that HSP90 limits ET-1-stimulated HSP27 induction at a point upstream of SAPK/JNK in osteoblasts. These results suggest that HSP90 may be a novel clinical target for metabolic bone diseases, including osteoporosis.
Publisher
D.A. Spandidos,Spandidos Publications,Spandidos Publications UK Ltd
