A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells
Author(s) -
Andrew J. Massey,
D.S. Williamson,
Helen Browne,
James B. Murray,
P. Dokurno,
T. Shaw,
Alba T. Macias,
Zoe Daniels,
Stephanie Geoffroy,
Melanie Dopson,
Paul Lavan,
Natalia Matassova,
Geraint L. Francis,
Christopher J Graham,
Rachel Parsons,
Yikang Wang,
Antony Padfield,
M.Margaret Comer,
Martin J. Drysdale,
Mike Wood
Publication year - 2009
Publication title -
cancer chemotherapy and pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.112
H-Index - 111
eISSN - 1432-0843
pISSN - 0344-5704
DOI - 10.1007/s00280-009-1194-3
Subject(s) - apoptosis , hsp90 , heat shock protein , hsp70 , hsp90 inhibitor , cell culture , biology , cell growth , cancer research , cancer cell , caspase , programmed cell death , chemistry , microbiology and biotechnology , biochemistry , cancer , genetics , gene
The anti-apoptotic function of the 70 kDa family of heat shock proteins and their role in cancer is well documented. Dual targeting of Hsc70 and Hsp70 with siRNA induces proteasome-dependent degradation of Hsp90 client proteins and extensive tumor specific apoptosis as well as the potentiation of tumor cell apoptosis following pharmacological Hsp90 inhibition.
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