Peer-Reviewed Journal Details
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Monaghan, D,O'Connell, E,Cruickshank, FL,O'Sullivan, B,Giles, FJ,Hulme, AN,Fearnhead, HO
2014
January
Biochemical And Biophysical Research Communications
Inhibition of protein synthesis and JNK activation are not required for cell death induced by anisomycin and anisomycin analogues
Published
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Optional Fields
Apoptosis Ribotoxic stress Breast cancer Drug-resistance RIBOTOXIC STRESS-RESPONSE NEGATIVE BREAST-CANCER N-TERMINAL KINASE MULTIDRUG-RESISTANCE INDUCED APOPTOSIS CARCINOMA-CELLS P-GLYCOPROTEIN OLD DRUGS TUMOR AMPLIFICATION
443
761
767
Anisomycin was identified in a screen of clinical compounds as a drug that kills breast cancer cells (MDA16 cells, derived from the triple negative breast cancer cell line, MDA-MB-468) that express high levels of an efflux pump, ABCB1. We show the MDA16 cells died by a caspase-independent mechanism, while MDA-MB-468 cells died by apoptosis. There was no correlation between cell death and either protein synthesis or JNK activation, which had previously been implicated in anisomycin-induced cell death. In addition, anisomycin analogues that did not inhibit protein synthesis or activate JNK retained the ability to induce cell death. These data suggest that either a ribosome-ANS complex is a death signal in the absence of JNK activation or ANS kills cells by binding to an as yet unidentified target. (C) 2013 Elsevier Inc. All rights reserved.
DOI 10.1016/j.bbrc.2013.12.041
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