| First Author | Picklo MJ Sr | Year | 2008 |
| Journal | Biochem Biophys Res Commun | Volume | 376 |
| Issue | 3 | Pages | 615-9 |
| PubMed ID | 18804449 | Mgi Jnum | J:142861 |
| Mgi Id | MGI:3822272 | Doi | 10.1016/j.bbrc.2008.09.039 |
| Citation | Picklo MJ Sr (2008) Ethanol intoxication increases hepatic N-lysyl protein acetylation. Biochem Biophys Res Commun 376(3):615-9 |
| abstractText | The acetylation of the epsilon-amino group of lysine to form N-acetyl lysine (N-AcLys)-modified proteins regulates the activity of metabolic proteins. Because of the multiple effects of ethanol upon hepatic metabolism, it was hypothesized that ethanol exposure increases the hepatic content of N-AcLys-modified proteins. To test this hypothesis, rats or mice were exposed to ethanol using a liquid diet regimen. Content of N-AcLys-modified proteins was elevated more than 5-fold after 6 weeks of ethanol exposure and persisted after ethanol withdrawal. Use of CYP2E1-knockout mice demonstrated that ethanol-induced acetylation was not dependent solely on CYP2E1 expression. The mitochondrial content of N-AcLys-modified proteins was elevated almost 5-fold following 6 weeks of ethanol exposure. Mitochondrial content of the deacetylase Sirt3 was unchanged by 6 weeks of ethanol exposure. These data indicate ethanol intoxication changes the acetylation status of, and likely the activity of, multiple mitochondrial proteins. |
