Makoto Isono, Akinori Sato, Kazuki Okubo, Takako Asano, Tomohiko Asano
Oncology Research, Vol.24, No.5, pp. 327-335, 2016, DOI:10.3727/096504016X14666990347635
Abstract The histone deacetylase (HDAC) inhibitor belinostat increases the amount of unfolded proteins in cells by promoting the acetylation of heat shock protein 90 (HSP90), thereby disrupting its chaperone function. The human
immunodeficiency virus protease inhibitor ritonavir, on the other hand, not only increases unfolded proteins by
suppressing HSP90 but also acts as a proteasome inhibitor. We thought that belinostat and ritonavir together
would induce endoplasmic reticulum (ER) stress and kill renal cancer cells effectively. The combination of
belinostat and ritonavir induced drastic apoptosis and inhibited the growth of renal cancer cells synergistically.
Mechanistically, the combination More >
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