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Ethanol intoxication increases hepatic mitochondrial protein acetylation but not through sirtuin inhibition
Author(s) -
Picklo Matthew J.,
Lee Susan,
Denu John M
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.760.1
Subject(s) - sirt3 , acetylation , sirtuin , mitochondrion , biochemistry , ethanol , chemistry , ethanol metabolism , metabolite , biology , gene
Chronic ethanol intoxication induces a myriad of physiologic and biochemical changes in the liver. Recent work indicates that ethanol intoxication alters hepatic metabolism by promoting protein lysyl acetylation while inhibiting de‐acetylation. In this work, we tested the hypothesis that chronic ethanol intoxication (six weeks) in rats increases the lysyl acetylation of mitochondrial proteins in the liver. Six weeks of ethanol intoxication significantly increased the acetylation of several proteins in liver mitochondria. On the other hand, protein acetylation in heart mitochondria was not altered. Although mitochondrial protein acetylation is regulated by the mitochondrial de‐acetylase, Sirt3, mitochondrial content of Sirt3 was not altered by ethanol exposure. Mitochondrial levels of the sirtuin metabolite, O‐acetyl‐ADP‐ribose, were 3‐fold higher in ethanol‐treated rats than control rats, suggesting that sirtuin activity was not inhibited. These data suggest that chronic ethanol intoxication increased protein acetylation in hepatic mitochondria but not through inhibition of the sirtuin pathway. Funding : The Wisconsin Partnership Fund to JMD and SL and NIH grant R21 AA15145‐01 to MJP.