Ethanol intoxication increases hepatic N-lysyl protein acetylation
Abstract
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.
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Chronic alcohol exposure suppressed the activities and protein amounts of sirtuin 1, 3 and 5 isoforms, in a CYP2E1-independent manner.
“Earlier reports also showed that chronic alcohol exposure suppressed the activities and protein amounts of sirtuin 1, 3 and 5 isoforms [142], [143], [144], [145], [149], [150], in a CYP2E1-independent manner [144].”
Cites
Substrate and Functional Diversity of Lysine Acetylation Revealed by a Proteomics Survey
Kim, S. C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., Cheng, T., Kho, Y., Xiao, H., Xiao, L., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.026 · Cited by 1,487 · see citing works
Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., & Horikawa, I. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0033 · Cited by 1,364 · see citing works
Jaeschke, H. (2002) · Toxicological Sciences · doi:10.1093/toxsci/65.2.166 · Cited by 1,308 · see citing works
Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216 · see citing works
Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.057 · Cited by 1,162 · see citing works
Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival
Yang, H., Yang, T., Baur, J. A., Perez, E., Matsui, T., Carmona, J. J., Lamming, D. W., Souza-Pinto, N. C., Bohr, V. A., Rosenzweig, A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.07.035 · Cited by 950 · see citing works
CYP2E1 and oxidative liver injury by alcohol
Lu, Y., & Cederbaum, A. I. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.004 · Cited by 805 · see citing works
Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
Hallows, W. C., Lee, S., & Denu, J. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604392103 · Cited by 792 · see citing works
Shi, T., Wang, F., Stieren, E., & Tong, Q. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414670200 · Cited by 712 · see citing works
Schwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., & Verdin, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603968103 · Cited by 705 · see citing works
Role of CYP2E1 in the Hepatotoxicity of Acetaminophen
Lee, S. S. T., Buters, J., Pineau, T., Fernández‐Salguero, P. M., & Gonzalez, F. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.20.12063 · Cited by 655 · see citing works
Schwer, B., North, B. J., Frye, R. A., Ott, M., & Verdin, E. M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205057 · Cited by 599 · see citing works
Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
Schlicker, C., Gertz, M., Papatheodorou, P., Kachholz, B., Becker, C. F. W., & Steegborn, C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.048 · Cited by 531 · see citing works
Regulation of Insulin Secretion by SIRT4, a Mitochondrial ADP-ribosyltransferase
Ahuja, N., Schwer, B., Carobbio, S., Waltregny, D., North, B. J., Castronovo, V., Maechler, P., & Verdin, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705488200 · Cited by 422 · see citing works
Sirtuins: The ‘ <i>magnificent seven</i> ’, function, metabolism and longevity
Dali‐Youcef, N., Lagouge, M., Froelich, S., Koehl, C., Schoonjans, K., & Auwerx, J. (2007) · Annals of Medicine · doi:10.1080/07853890701408194 · Cited by 402 · see citing works
Cytochrome P450 2E1 contributes to ethanol-induced fatty liver in mice
Lu, Y., Zhuge, J., Wang, X., Bai, J., & Cederbaum, A. I. (2008) · Hepatology · doi:10.1002/hep.22222 · Cited by 310 · see citing works
Ethanol Induces CYP2E1 by Protein Stabilization
Roberts, B. J., Song, B.-J., Soh, Y., Park, S. S., & Shoaf, S. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.50.29632 · Cited by 267 · see citing works
The time-course of the effects of ethanol on the redox and phosphorylation states of rat liver
Veech, R. L., Guynn, R. W., & Veloso, D. (1972) · Biochemical Journal · doi:10.1042/bj1270387 · Cited by 257 · see citing works
Involvement of mammalian sirtuin 1 in the action of ethanol in the liver
You, M., Liang, X., Ajmo, J. M., & Ness, G. C. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00575.2007 · Cited by 215 · see citing works
Yang, T., Fu, M., Pestell, R. G., & Sauve, A. A. (2006) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2006.04.002 · Cited by 181 · see citing works
NAD metabolism and sirtuins: Metabolic regulation of protein deacetylation in stress and toxicity
Yang, T., & Sauve, A. A. (2006) · The AAPS Journal · doi:10.1208/aapsj080472 · Cited by 170 · see citing works
Coenzyme Specificity of Sir2 Protein Deacetylases
Schmidt, M. T., Smith, B. C., Jackson, M. D., & Denu, J. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407484200 · Cited by 146 · see citing works
The human SIRT3 protein deacetylase is exclusively mitochondrial
Cooper, H. M., & Spelbrink, J. N. (2008) · Biochemical Journal · doi:10.1042/bj20071624 · Cited by 133 · see citing works
You, M., Cao, Q., Liang, X., Ajmo, J. M., & Ness, G. C. (2008) · Journal of Nutrition · doi:10.1093/jn/138.3.497 · Cited by 91 · see citing works
Oxidation of 4‐hydroxy‐2‐nonenal by succinic semialdehyde dehydrogenase (ALDH5A)
Murphy, T. C., Amarnath, V., Gibson, K. M., & Picklo, M. J. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01839.x · Cited by 72 · see citing works
Self-citationSpach, P. I., & CUNNINGHAM, C. C. (1987) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(87)90125-3 · Cited by 72 · see citing works
Alcohol alters hepatic FoxO1, p53, and mitochondrial SIRT5 deacetylation function
Lieber, C. S., Leo, M. A., Wang, X., & DeCarli, L. M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.006 · Cited by 71 · see citing works
Role of CYP3A in Ethanol-Mediated Increases in Acetaminophen Hepatotoxicity
Kostrubsky, V. E., Szakacs, J. G., Jeffery, E. H., Wood, S. G., Bement, W. J., Wrighton, S. A., Sinclair, P. R., & Sinclair, J. F. (1997) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1996.8081 · Cited by 54 · see citing works
Lumeng, L., Bremer, J., & Davis, E. J. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33875-9 · Cited by 49 · see citing works
Metabolism, cytoskeleton and cellular signalling in the grip of protein Nϵ ‐ and O‐acetylation
Yang, X., & Grégoire, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400977 · Cited by 48 · see citing works
Removal of Acetaldehyde from the Body
Deitrich, R. A., Petersen, D. R., & Vasiliou, V. (2006) · Novartis Foundation symposium · doi:10.1002/9780470511848.ch3 · Cited by 44 · see citing works
Marcinkevičiūtė, A., Mildažienė, V., Crumm, S. E., Demin, O. O., Hoek, J. B., & Kholodenko, B. Ν. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3490519 · Cited by 42 · see citing works
Pharmacological targeting of lysine acetyltransferases in human disease: a progress report
Heery, D. M., & Fischer, P. M. (2006) · Drug Discovery Today · doi:10.1016/j.drudis.2006.11.012 · Cited by 41 · see citing works
Marcinkevičiūtė, A., Mildažienė, V., Crumm, S. E., et al. (2000) · Biochemical Journal · doi:10.1042/bj3490519 · Cited by 32 · see citing works
Ishino, K., Shibata, T., Ishii, T., Liu, Y., Toyokuni, S., Zhu, X., Sayre, L. M., & Uchida, K. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800080x · Cited by 30 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The growing landscape of lysine acetylation links metabolism and cell signalling
Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324 · see citing works
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · see citing works
Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics
Ali, I., Conrad, R. J., Verdin, E. M., & Ott, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00181 · Cited by 366 · see citing works
Mitochondrial sirtuins: regulators of protein acylation and metabolism
He, W., Newman, J. C., Wang, M. Z., Ho, L., & Verdin, E. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.07.004 · Cited by 262 · see citing works
Calorie restriction alters mitochondrial protein acetylation
Schwer, B., Eckersdorff, M., Li, Y., Silva, J. C., Fermin, D., Kurtev, M. V., Giallourakis, C., Comb, M. J., Alt, F. W., & Lombard, D. B. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00503.x · Cited by 259 · see citing works
“In mammals, acute fasting and chronic ethanol ingestion also alter hepatic mitochondrial protein acetylation (Kim et al., 2006; Picklo, 2008), suggesting that changes in acetylation represents an ancient, evolutionarily conserved mechanism for adaptation to metabolic ⁄ nutritional stress.”
BackgroundSIRT3, a pivotal actor in mitochondrial functions: metabolism, cell death and aging
Giralt, A., & Villarroya, F. (2012) · Biochemical Journal · doi:10.1042/bj20120030 · Cited by 253 · see citing works
Mitochondrial protein acetylation regulates metabolism
Anderson, K. A., & Hirschey, M. D. (2012) · Essays in Biochemistry · doi:10.1042/bse0520023 · Cited by 246 · see citing works
The cell biology of the hepatocyte: A membrane trafficking machine
Schulze, R. J., Schott, M. B., Casey, C. A., Tuma, P. L., & McNiven, M. A. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201903090 · Cited by 246 · see citing works
Newman, J. C., He, W., & Verdin, E. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.404863 · Cited by 207 · see citing works
Zhang, H., & Fu, L. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.02.008 · Cited by 153 · see citing works
Metabolic regulation by SIRT3: implications for tumorigenesis
Finley, L. W. S., & Haigis, M. C. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.05.004 · Cited by 130 · see citing works
4-hydroxynonenal inhibits SIRT3 via thiol-specific modification
Fritz, K. S., Galligan, J. J., Smathers, R. L., Roede, J. R., Shearn, C. T., Reigan, P., & Petersen, D. R. (2011) · Chemical Research in Toxicology · doi:10.1021/tx100355a · Cited by 127 · see citing works
Mitochondrial Sirtuins in the Regulation of Mitochondrial Activity and Metabolic Adaptation
Lombard, D. B., Tishkoff, D. X., & Bao, J. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_8 · Cited by 124 · see citing works
Song, B.-J., Akbar, M., Abdelmegeed, M. A., Byun, K., Lee, B., Yoon, S. K., & Hardwick, J. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.10.004 · Cited by 123 · see citing works
“After decreased glucose supply like during fasting or inefficient oxidative phosphorylation in certain disease states, the mitochondrial fat oxidation pathway becomes important in providing an alternative source of energy (e.g., ketone bodies) [1].”
BackgroundFritz, K. S., Galligan, J. J., Hirschey, M. D., Verdin, E., & Petersen, D. R. (2012) · Journal of Proteome Research · doi:10.1021/pr2008384 · Cited by 121 · see citing works
Dynamic Adaptation of Liver Mitochondria to Chronic Alcohol Feeding in Mice
Han, D., Ybanez, M. D., Johnson, H. S., McDonald, J. N., Mesropyan, L., Sancheti, H., Martin, G. G., Martin, A. M., Lim, A. M., Dara, L., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.377374 · Cited by 108 · see citing works
Alcohol-induced protein hyperacetylation: Mechanisms and consequences
Shepard, B. D. (2009) · World Journal of Gastroenterology · doi:10.3748/wjg.15.1219 · Cited by 83 · see citing works
Harris, P. S., Roy, S. R., Coughlan, C. M., Orlicky, D. J., Liang, Y., Shearn, C. T., Roede, J. R., & Fritz, K. S. (2015) · Redox Biology · doi:10.1016/j.redox.2015.06.021 · Cited by 77 · see citing works
Shulga, N., & Pastorino, J. G. (2010) · Journal of Cell Science · doi:10.1242/jcs.073502 · Cited by 75 · see citing works
RetractedPost-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications
Song, B.-J., Abdelmegeed, M. A., Yoo, S.-H., Kim, B.-J., Jo, S. A., Jo, I., & Moon, K.-H. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.05.013 · Cited by 73 · see citing works
Regulation of autophagy and mitophagy by nutrient availability and acetylation
Webster, B. R., Scott, I., Traba, J., Han, K., & Sack, M. N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2014.02.001 · Cited by 73 · see citing works
Role of Mitochondria in Alcoholic Liver Disease
García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2013) · Current Pathobiology Reports · doi:10.1007/s40139-013-0021-z · Cited by 70 · see citing works
Chronic Ethanol Consumption Induces Global Hepatic Protein Hyperacetylation
Shepard, B. D., Tuma, D. J., & Tuma, P. L. (2009) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2009.01091.x · Cited by 68 · see citing works
Ethanol Metabolism Modifies Hepatic Protein Acylation in Mice
Fritz, K. S., Green, M. F., Petersen, D. R., & Hirschey, M. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075868 · Cited by 53 · see citing works
Mitochondrial remodeling in the liver following chronic alcohol feeding to rats
Han, D., Johnson, H. S., Rao, M. P., Martin, G. G., Sancheti, H., Silkwood, K. H., Decker, C. W., Nguyen, K. T., Casian, J. G., Cadenas, E., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.020 · Cited by 51 · see citing works
Song, B., Akbar, M. D., Jo, I., Hardwick, J. P., & Abdelmegeed, M. A. (2015) · Advances in pharmacology · doi:10.1016/bs.apha.2015.04.002 · Cited by 49 · see citing works
Meyer, J. G., Softic, S., Basisty, N., Rardin, M. J., Verdin, E. M., Gibson, B. W., Ilkayeva, O., Newgard, C. B., Kahn, C. R., & Schilling, B. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208973 · Cited by 49 · see citing works
Biological significance of protein modifications in aging and calorie restriction
Nakamura, A., Kawakami, K., Kametani, F., Nakamoto, H., & Goto, S. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05374.x · Cited by 43 · see citing works
Assiri, M. A., Roy, S. R., Harris, P. S., Ali, H., Liang, Y., Shearn, C. T., Orlicky, D. J., Roede, J. R., Hirschey, M. D., Backos, D. S., et al. (2017) · Alcoholism Clinical and Experimental Research · doi:10.1111/acer.13473 · Cited by 40 · see citing works
SIRT3 Weighs Heavily in the Metabolic Balance: A New Role for SIRT3 in Metabolic Syndrome
Green, M. F., & Hirschey, M. D. (2012) · The Journals of Gerontology Series A · doi:10.1093/gerona/gls132 · Cited by 34 · see citing works
Phosphorylation and Acetylation of Acyl-Coa Synthetase- I
Frahm, J. L. (2011) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000180 · Cited by 30 · see citing works
Alcohol-induced microtubule acetylation leads to the accumulation of large, immobile lipid droplets
Groebner, J. L., Bravo, M. G., Rothberg, M. L., Adhikari, R., Tuma, D. J., & Tuma, P. L. (2019) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00026.2019 · Cited by 29 · see citing works
Parker, R., Schmidt, M. S., Cain, O. L., Gunson, B. K., & Brenner, C. (2020) · Hepatology Communications · doi:10.1002/hep4.1530 · Cited by 29 · see citing works
Osna, N. A., Carter, W. G., Ganesan, M., Kirpich, I., McClain, C. J., Petersen, D. R., Shearn, C. T., Tomasi, M. L., & Kharbanda, K. K. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i27.6192 · Cited by 28 · see citing works
Kriss, C. L., Gregory‐Lott, E., Storey, A. J., Tackett, A. J., Wahls, W. P., & Stevens, S. M. (2018) · Alcoholism Clinical and Experimental Research · doi:10.1111/acer.13843 · Cited by 25 · see citing works
Alcohol consumption impairs hepatic protein trafficking: mechanisms and consequences
Shepard, B. D., Fernandez, D. J., & Tuma, P. L. (2009) · Genes & Nutrition · doi:10.1007/s12263-009-0156-z · Cited by 24 · see citing works
Quantifying Competition among Mitochondrial Protein Acylation Events Induced by Ethanol Metabolism
Ali, H., Assiri, M. A., Harris, P. S., Michel, C. R., Yun, Y., Marentette, J., Huynh, F. K., Orlicky, D. J., Shearn, C. T., Saba, L. M., et al. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00800 · Cited by 23 · see citing works
The Altered Hepatic Tubulin Code in Alcoholic Liver Disease
Groebner, J. L., & Tuma, P. L. (2015) · Biomolecules · doi:10.3390/biom5032140 · Cited by 22 · see citing works
Mitoneet mediates TNFα induced necroptosis promoted by fructose and ethanol exposure
Shulga, N., & Pastorino, J. G. (2013) · Journal of Cell Science · doi:10.1242/jcs.140764 · Cited by 20 · see citing works
RetractedOxygen Flux Analysis to Understand the Biological Function of Sirtuins
Wang, D., Green, M. F., McDonnell, E., & Hirschey, M. D. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-637-5_16 · Cited by 20 · see citing works
Harris, P. S., Michel, C. R., Yun, Y., McGinnis, C. D., Assiri, M. A., Ahmadi, A. R., Sun, Z., Roede, J. R., Burchill, M. A., Orlicky, D. J., et al. (2021) · Alcohol · doi:10.1016/j.alcohol.2021.11.005 · Cited by 18 · see citing works
McGinnis, C. D., Jennings, E. Q., Harris, P. S., Galligan, J. J., & Fritz, K. S. (2022) · Cells · doi:10.3390/cells11132045 · Cited by 18 · see citing works
Alcoholic-Hepatitis, Links to Brain and Microbiome: Mechanisms, Clinical and Experimental Research
Neuman, M. G., Seitz, H. K., French, S. W., Malnick, S. D. H., Tsukamoto, H., Cohen, L. B., Hoffman, P. L., Tabakoff, B., Fasullo, M., Nagy, L. E., et al. (2020) · Biomedicines · doi:10.3390/biomedicines8030063 · Cited by 18 · see citing works
Kashem, M. A., Šerý, O., Pow, D. V., Rowlands, B. D., Rae, C. D., & Balcar, V. J. (2020) · Current Molecular Pharmacology · doi:10.2174/1874467213666200424155244 · Cited by 17 · see citing works
Singh, P., Ponnan, P., Krishnan, S., Tyagi, T. K., Priya, N., Bansal, S., Scumaci, D., Gaspari, M., Cuda, G., Joshi, P. C., et al. (2010) · The Journal of Biochemistry · doi:10.1093/jb/mvq002 · Cited by 16 · see citing works
Alcohol-induced defects in hepatic transcytosis may be explained by impaired dynein function
Groebner, J. L., Fernandez, D. J., Tuma, D. J., & Tuma, P. L. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-2190-4 · Cited by 12 · see citing works
Silva, I. D. F. O., Pereira, S. R. C., Fernandes, P. Á., Ribeiro, A. F., Pires, R. G. W., & Ribeiro, Â. M. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-014-0306-7 · Cited by 9 · see citing works
Mitochondria Lysine Acetylation and Phenotypic Control
Ciregia, F. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8367-0_4 · Cited by 8 · see citing works
HINT2 and fatty liver disease: Mitochondrial protein hyperacetylation gives a hint?
Anderson, K. A., Wang, D., & Hirschey, M. D. (2012) · Hepatology · doi:10.1002/hep.26085 · Cited by 7 · see citing works
Neuman, M. G., Seitz, H. K., Tuma, P. L., Osna, N. A., Casey, C. A., Kharbanda, K. K., Cohen, L. B., Malnick, S. D. H., Adhikari, R., Mitra, R., et al. (2022) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2022.104750 · Cited by 6 · see citing works
Methionine Adenosyltransferase 1A and S-Adenosylmethionine in Alcohol-Associated Liver Disease
Barbier‐Torres, L., Chhimwal, J., Mato, J. M., & Lu, S. C.-L. (2025) · Antioxidants · doi:10.3390/antiox14121486 · Cited by 5 · see citing works
Distinct peroxisome populations differentially respond to alcohol-associated hepatic injury
Mitra, R., Adhikari, R., Davis, S. S., McVicker, B. L., & Tuma, P. L. (2024) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-06-0252 · Cited by 5 · see citing works
Cao, G., Chen, B., Sun, Y., Qiao, J., Liu, T., Hou, J., Han, X., Tang, Y., Fu, Y., Ye, J., et al. (2025) · BMC Psychiatry · doi:10.1186/s12888-025-07014-9 · Cited by 4 · see citing works
Mitochondrial Regulation by Protein Acetylation
Lombard, D. B., Tishkoff, D. X., & Zwaans, B. M. M. (2012) · Oxidative stress and disease · doi:10.1201/b12308-17 · Cited by 3 · see citing works
Acetyl-CoA and acetylation in biology and disease
Puglielli, L., Rigby, M. J., & Fernandez-Fuente, G. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95582-9.00009-7 · Cited by 2 · see citing works
Haak, J. L., Kregel, K. C., & Bloomer, S. A. (2023) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00610.2023 · Cited by 1 · see citing works
Thornton, J. A., Koc, Z. C., Sollars, V. E., Valentovic, M. A., Denvir, J., Wilkinson, J., & Koc, E. C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158344 · Cited by 2 · see citing works
Novel NAD+ metabolomic technologies and their applications to Nicotinamide Riboside interventions
Trammell, S. A. J., Wright, M. E., Piper, R. C., Brenner, C., Slusarski, D. C., & Wilson, M. E. (2016) · doi:10.17077/etd.mk206led · Cited by 1 · see citing works
Role of iron in ethanol derived hepatic stress
Thornton, J. A. (2013)
Meyer, J. G. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/662841
- Authors
- Picklo, M. J.
- Affiliations
- University of North Dakota (US)
- Corresponding author
- Picklo, Matthew J.
- ORCID
- Picklo, Matthew J.
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2008-11
- Volume
- 376
- Issue
- 3
- Pages
- 615-619
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W1996800526
- Cited by
- 60
- References
- 35
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 2 · 2022: 2 · 2021: 2 · 2020: 3 · 2019: 5 · 2018: 3 · 2017: 1 · 2016: 3 · 2015: 3 · 2014: 5 · 2013: 5 · 2012: 10
- FWCI
- 2.84
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Alcohol Abuse and Alcoholism (R21AA015145, AA 15145-01)
- Topics
- Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Drug-Induced Hepatotoxicity and Protection
- Keywords
- ethanol intoxication, hepatic proteins, mitochondrial proteins, CYP2E1, SIRT3, ethanol withdrawal, hepatic metabolism, protein acetylation
- MeSH terms
- Acetylation, Ethanol, Alcoholic Intoxication, Animals, Female, Liver, Lysine, Male, Mice, Mutant Strains, Protein Processing, Post-Translational, Rats, Sprague-Dawley, Cytochrome P-450 CYP2E1, Mitochondrial Proteins, Mice, Rats
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