Published online Aug 26, 2014. doi: 10.4331/wjbc.v5.i3.377
Revised: April 2, 2014
Accepted: June 27, 2014
Published online: August 26, 2014
Processing time: 205 Days and 7.3 Hours
AIM: To determine if doxorubicin (Dox) alters hepatic proteome acetylation status and if acetylation status was associated with an apoptotic environment.
METHODS: Doxorubicin (20 mg/kg; Sigma, Saint Louis, MO; n = 8) or NaCl (0.9%; n = 7) was administered as an intraperitoneal injection to male F344 rats, 6-wk of age. Once animals were treated with Dox or saline, all animals were fasted until sacrifice 24 h later.
RESULTS: Dox treatment decreased proteome lysine acetylation likely due to a decrease in histone acetyltransferase activity. Proteome deacetylation may likely not be associated with a proapoptotic environment. Dox did not increase caspase-9, -8, or -3 activation nor poly (adenosine diphosphate-ribose) polymerase-1 cleavage. Dox did stimulate caspase-12 activation, however, it likely did not play a role in apoptosis induction.
CONCLUSION: Early effects of Dox involve hepatic proteome lysine deacetylation and caspase-12 activation under these experimental conditions.
Core tip: Doxorubicin (Dox) is an effective chemotherapeutic agent, but known to cause cardiotoxicity and hepatotoxicity. Cellular stress can alter proteome acetylation status in various experimental models, which has been associated with a proapoptotic environment. The effects of Dox on hepatic lysine acetylation status has not been studied. The study revealed five interesting findings that open the door for new areas of investigation: (1) Dox induces proteome lysine deacetylation; (2) lysine deacetylation is, at least in part, due to a decrease in histone acetyltransferase activity; (3) lysine deacetylation is likely not associated with an apoptotic environment; (4) Dox-induced hepatic injury is associated with caspase-12 activation; and (5) caspase-12 activation is not involved in apoptosis induction. These results may in the future translate to lysine acetylation homeostasis and/or caspase-12 as therapeutic targets.