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Retracted : 1,3,5‐ T rihydroxy‐13,13‐dimethyl‐2 H ‐pyran [7,6‐b] xanthone directly targets heat shock protein 27 in hepatocellular carcinoma
Author(s) -
Fu Weiming,
Wang Weimao,
Wang Hua,
Zhu Xiao,
Liang Yan,
Kung Hsiangfu,
Zhang Jinfang
Publication year - 2014
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1002/cbin.10193
Subject(s) - hsp27 , heat shock protein , chemistry , hepatocellular carcinoma , proteasome , hsp90 , hsp70 , xanthone , pin1 , in vitro , apoptosis , chaperone (clinical) , recombinant dna , microbiology and biotechnology , biochemistry , cancer research , biology , enzyme , gene , stereochemistry , isomerase , medicine , pathology
We previously showed that the small molecule 1,3,5‐trihydroxy‐13,13‐dimethyl‐2H‐pyran [7,6‐b] xanthone (TDP) induces apoptosis in hepatocellular carcinoma (HCC) by suppressing Hsp27 expression, although the mechanism is not fully understood. To investigate the functional association between TDP and Hsp27 protein in HCC, recombinant Hsp27 protein was incubated with TDP at room temperature, and assayed by mass spectrum (MS) and natural electrophoresis. TDP effectively stimulated Hsp27 to form aggregates ex vitro, leading to suppression of its chaperone activity. The aggregates were degraded by the ubiquitin–proteasome (UPS) pathway. TDP directly interacted with Asp17 and Phe55 in chain C of Hsp27 on the basis of bioinformatic prediction. In conclusion, Hsp27 is a direct target of TDP in its anti‐cancer activity, which provides strong support for a clinical application.