Effects of acute doxorubicin treatment on hepatic proteome lysine acetylation status and the apoptotic environment |
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Authors: | Amie J Dirks-Naylor Samir A Kouzi Joseph D Bero Ngan TK Tran Sendra Yang Raean Mabolo |
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Affiliation: | Amie J Dirks-Naylor, Samir A Kouzi, Joseph D Bero, Ngan TK Tran, Sendra Yang, Raean Mabolo, School of Pharmacy, Wingate University, Wingate, NC 28174, United States |
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Abstract: | 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 activa-tion under these experimental conditions. |
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Keywords: | Sirtuin Sirtuin Caspase Apoptosis Acetylation Histone deacetylase Histone acetyltransferase |
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