Histone deacetylase (
HDAC) inhibitors are candidates of anti-
cancer drugs as they can effectively kill
cancer cells while have little or no toxicity to non-
cancer cells, but the molecular mechanism underlying this process remains unclear. We previously reported that
HDAC inhibitors could protect normal mouse hepatocytes from apoptosis induced by transforming growth factor-β1 (TGF-β1) with the requirement of
extracellular signal-regulated kinase 1/2 (ERK1/2). In this study, we investigate the roles of
trichostatin A (
TSA), a typical
HDAC inhibitor, on three non-
cancer cell lines AML-12, MDCK and 3T3-L1, and four
cancer cell lines Hep-3B, HeLa, A549 and MCF-7.
TSA is a fermentation product of Streptomyces originally used as an
antifungal agent. Our results showed that
TSA blocked not only the TGF-β1-induced apoptosis but also serum
starvation-induced apoptosis in all the non-
cancer cells, whereas it could induce strong apoptosis in all the
cancer cells. Further investigation revealed that
TSA can induce the activation of ERK1/2 in the three non-
cancer cells but not in the
cancer cells. In summary, these findings indicated that
TSA protect non-
cancer cells from apoptosis via activating ERK1/2, providing a useful insight into the better application of
HDAC inhibitors in
cancer therapy.