期刊
INTERNATIONAL JOURNAL OF ONCOLOGY
卷 46, 期 3, 页码 907-926出版社
SPANDIDOS PUBL LTD
DOI: 10.3892/ijo.2014.2791
关键词
Hsp90; chaperone; Hsp90 inhibitor; cancer; resistance
类别
资金
- Scientific Grant Agency of the Ministry of Education of the Slovak Republic [VEGA 1/0733/12]
Hsp90 is a molecular chaperone that maintains the structural and functional integrity of various client proteins involved in signaling and many other functions of cancer cells. The natural inhibitors, ansamycins influence the Hsp90 chaperone function by preventing its binding to client proteins and resulting in their proteasomal degradation. Nand C-terminal inhibitors of Hsp90 and their analogues are widely tested as potential anticancer agents in vitro, in vivo as well as in clinical trials. It seems that Hsp90 competitive inhibitors target different tumor types at nanomolar concentrations and might have therapeutic benefit. On the contrary, some Hsp90 inhibitors increased toxicity and resistance of cancer cells induced by heat shock response, and through the interaction of survival signals, that occured as side effects of treatments, could be very effectively limited via combination of therapies. The aim of our review was to collect the data from experimental and clinical trials where Hsp90 inhibitor was combined with other therapies in order to prevent resistance as well as to potentiate the cytotoxic and/or antiproliferative effects.
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